FUNCTION: Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Membrane; Lipid-anchor. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ2 subfamily.


FUNCTION: May have a role in proliferation and/or differentiation. SIMILARITY: Belongs to the PRR15 family.


FUNCTION: Involved in the efflux of purine ribonucleosides, such as guanosine, adenosine and inosine, as well as purine bases guanine, adenine and hypoxanthine, and purine base analogs 2,6-diaminopurine and 6-mercaptopurine. Therefore plays a role in maintaining the cellular purine base pools and protecting cells against toxic purine base analogs. Modulates expression of the purR and G-box regulons (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. PbuE (TC 2.A.1.2.25) subfamily.


FUNCTION: Could be part of the type IV piliation system (T4P). May contribute at the cohesion between the S-layer and the outer membrane by forming oligomers. Could also be the main channel through which trafficking is managed. SUBCELLULAR LOCATION: Cell envelope. SIMILARITY: Belongs to the bacterial secretin family.


SIMILARITY: Belongs to the SCO1/2 family.


SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.


FUNCTION: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola (PubMed:15387811, PubMed:18272357, PubMed:19762440). SirD catalyzes the O-prenylation of L-tyrosine (L- Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O- dimethylallyl-L-Tyr, and therefore represents probably the first pathway-specific enzyme in the biosynthesis of sirodesmin PL (PubMed:19762440, PubMed:21038099, PubMed:24083562). 4-O-dimethylallyl- L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed by the non-ribosomal peptide synthase sirP to form the diketopiperazine (DKP) backbone (PubMed:18272357). Further bishydroxylation of the DKP performed by the cytochrome P450 monooxygenase sirC leads to the production of the intermediate phomamide (PubMed:27390873). This step is essential to form the reactive thiol group required for toxicity of sirodesmin PL (PubMed:27390873). The next steps of sirodesmin biosynthesis are not well understood yet, but some predictions could be made from intermediate compounds identification (PubMed:18272357). Phomamide is converted into phomalizarine via oxidation, probably by sirT (PubMed:18272357). Further oxidation, methylation (by sirM or sirN) and reduction steps convert phomalizarine to deacetyl sirodesmin (PubMed:18272357). Finally, acetyltransferase sirH probably acetylates deacetyl sirodesmin to produce sirodesmin PL (PubMed:18272357). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. Highly divergent.


FUNCTION: Together with RDM3, required for transcriptional gene silencing (TGS) by DNA methylation and repressive histone modifications (H3K9me2) of several chromatin loci (PubMed:21738482). Component of the RISC complex that associate with the small interfering RNA (siRNA) pathway involved in direct cytosine methylation at endogenous DNA repeats. Forms a AGO4/NRPE1/siRNA complex in cajal body, facilitating its function in RNA-directed gene silencing of target loci. Required for CpNpG and asymmetric DNA methylation as well as histone H3 'Lys-9' methylation (H3K9me) at SUP and SN1 loci. May be not required for CpG methylation. Required for the production and maintenance of retrotransposon SN1 and Copia and ribosomal 5S 25 nucleotide siRNAs specialized in gene silencing at chromatin level. Involved in de novo methylation of FWA gene and required for the maintenance of RNA- directed DNA methylation (RdDM) triggered by inverted repeat transgenes. Interacts with miRNA miR390 and miR172, targeting respectively TAS3 and AP2 mRNAs, and mediates cleavage of miRNA targets. Associates mainly with small RNAs of 24 nucleotide in length and preferentially recruits small RNAs with a 5' terminal adenosine. Targeted by the turnip yellows virus (TuYV) protein P0 (via F-box-like domain) for probable proteasome degradation and thereby inactivating AGO4 function in RNA silencing. Required for resistance to the bacterial pathogen P.syringae. Works independently of the RdDM pathway in mediating resistance to P.syringae. RdDM is involved in viral genome methylation as an epigenetic defense against geminiviruses (PubMed:12522258, PubMed:14988555, PubMed:15242620, PubMed:16839878, PubMed:16839879, PubMed:16998468, PubMed:17869110, PubMed:17938239, PubMed:17993621, PubMed:18342361, PubMed:18596098, PubMed:19377477, PubMed:20173091). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm Nucleus, Cajal body Note=Also located in AB-bodies that are distincts from the Cajal bodies and immediately adjacent to the condensed 45S ribosomal DNA (rDNA) loci (PubMed:18266474). Colocalizes with AGO4 and polymerase V in the nucleoplasm (PubMed:19410546). SIMILARITY: Belongs to the argonaute family. Ago subfamily.


FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. SIMILARITY: Belongs to the cyanase family. SIMILARITY: Belongs to the cyanase family.


FUNCTION: Transcription factor that establishes leaf shape by repressing growth in specific subdomains of the leaf. Negatively regulates knox homeobox gene KNAT1/BP expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/BELL homeobox family.


FUNCTION: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre- mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. STRAP may play a role in the cellular distribution of the SMN complex (By similarity). SIMILARITY: Belongs to the WD repeat STRAP family.


FUNCTION: Required for disulfide bond formation in some proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family. BdbC subfamily.


SIMILARITY: Belongs to the IIV-6 201R/289L family.


FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not lead to PLK1 degradation. The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway. It is therefore an amino acid-dependent activator within the amino acid-sensing branch of the TORC1 pathway, indirectly regulating different cellular processes including cell growth and autophagy. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Nucleus Lysosome Note=Mainly cytoplasmic in prophase and prometaphase. Associates with the mitotic spindle as the cells reach chromosome bi-orientation. Localizes to the centrosomes shortly before cells enter anaphase After anaphase onset, predominantly associates with the polar microtubules connecting the 2 opposing centrosomes and gradually diffuses into the cytoplasm during telophase. Localizes to the nucleus upon amino acid starvation. Relocalizes to the cytosol and associates with lysosomes when amino acids are available.


FUNCTION: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. May act as a tumor suppressor. SUBCELLULAR LOCATION: Membrane; Single- pass type I membrane protein Membrane, coated pit. SIMILARITY: Belongs to the LDLR family.


FUNCTION: Required for pre-18S rRNA processing. May bind microtubules (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NOP5/NOP56 family.


FUNCTION: Associates with the serine/threonine-protein phosphatase PP2A regulatory subunits A and B' to positively regulates beta-oxidation of fatty acids and protoauxins in peroxisomes by dephosphorylating peroxisomal beta-oxidation-related proteins (PubMed:25489022). Involved in the positive regulation of salt stress responses. May function by increasing chloride channel activities on vacuolar membranes (PubMed:27676158). SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome Note=Interacts with B'THETA in the cytosol and peroxisomal import occurs by a piggybacking transport. SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL15 family.


FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)- methyltransferase that methylates pseudouridine at position 1189 (Psi1189) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. N1-methylation is independent on acp- modification at the N3-position of U1191. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 (RPS19A/RPS19B) during the formation of pre-ribosomes. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family.


FUNCTION: Cuticular proteins play a significant role in determining the physical properties of cuticles.


SIMILARITY: Belongs to the melanin-concentrating hormone family.


FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome- nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for Rab5-GDP and participate in the activation of Rab5. SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass type II membrane protein Nucleus envelope Endosome membrane; Single-pass type II membrane protein Note=Colocalizes with KASH5 at sites of telomere attachment in meiocytes.


FUNCTION: S antigens are soluble heat-stable proteins present in the sera of some infected individuals. SUBCELLULAR LOCATION: Parasitophorous vacuole Note=Localizes to the cell periphery in early schizonts and then to the parasitophorous vacuole in late schizonts. Following schizont rupture, the S-antigen is released in host sera.


FUNCTION: Inhibits a wide spectrum of lactic acid bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family.


FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6 subfamily.


FUNCTION: Lethal neurotoxin. Selectively blocks tetrodotoxin-sensitive voltage-gated sodium channels (Nav). Does not affect tetrodotoxin- resistant voltage-gated sodium channels or calcium channels (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 15 (Hntx-3) subfamily.


FUNCTION: Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA. SUBCELLULAR LOCATION: Cytoplasm. Note=Localizes to the septum at mid- cell, in a FtsZ-like pattern. SIMILARITY: Belongs to the ZapB family.


FUNCTION: Non-heme-dependent dioxygenase that catalyzes the oxidative epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)- epoxypropylphosphonate, the final step in the biosynthesis of fosfomycin antibiotic. SIMILARITY: Belongs to the non-heme iron-dependent dioxygenase family.


FUNCTION: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface. May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein Peroxisome Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. SIMILARITY: Belongs to the Tango11 family.


FUNCTION: Effector that suppresses flg22-induced post-translational MAP kinase activation in tomato but not in Arabidopsis. The perception of highly conserved pathogen- or microbe-associated molecular patterns (PAMPs/MAMPs), such as flg22, triggers converging signaling pathways recruiting MAP kinase cascades and inducing transcriptional re- programming, yielding a generic antimicrobial response (PubMed:24763622). Also partially attenuates INF1-triggered cell death (PubMed:24763622). SUBCELLULAR LOCATION: Secreted Host cytoplasm Host cell membrane. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 3 subfamily.


FUNCTION: Insect active toxin causing rapid but reversible paralysis in crickets. No activity shown in mammals. Does not show effect on mammalian voltage-gated calcium channels (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 01 (U2-agtx) family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL30 family.


FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides (Probable). SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.


FUNCTION: May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion (By similarity). SUBCELLULAR LOCATION: Synapse, synaptosome Note=Complexed with macromolecular elements of the nerve terminal. SIMILARITY: Belongs to the SNAP-25 family.


FUNCTION: Has menaquinol-oxidizing activity. HmeC and HmeD subunits may together mediate electron transfer from menaquinol to an unidentified electron acceptor on the cytoplasmic side of the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: Plays a continuous role in plant development probably in the structural organization of compartments. SUBCELLULAR LOCATION: Membrane; Lipid-anchor.


FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Nucleus Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. SIMILARITY: Belongs to the GST superfamily. Pi family.


FUNCTION: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:28209804, PubMed:23766516, PubMed:9096315). Preferentially activates arachidonate and eicosapentaenoate as substrates (PubMed:9096315). Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET (PubMed:23766516). Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (PubMed:23766516). Modulates prostaglandin E2 secretion (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type III membrane protein Peroxisome membrane; Single-pass type III membrane protein Microsome membrane; Single-pass type III membrane protein Endoplasmic reticulum membrane; Single-pass type III membrane protein Cell membrane. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: Possible structural role in the sperm tail. It is associated with axonemal structures. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GatC family.


FUNCTION: Plays an important role in the cytoplasmic envelopment of tegument proteins and capsids during the assembly and egress processes. Participates also in viral entry at the fusion step probably by regulating the core fusion machinery. SUBCELLULAR LOCATION: Virion tegument Virion membrane; Lipid-anchor Host cell membrane; Lipid-anchor; Cytoplasmic side Host Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side Note=Virion membrane-associated tegument protein. Associates with host membrane lipids rafts. During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). SIMILARITY: Belongs to the herpesviridae HHV-1 UL11 family.


SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.


FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with Cetn2 appears to stabilize Xpc. May protect Xpc from proteasomal degradation (By similarity). FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, Xpa, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. Xpc:Rad22b induces a bend in DNA upon binding. Xpc:Rad23b stimulates the activity of DNA glycosylases Tdg and Smug1 (By similarity). FUNCTION: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RAD23 family.


FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state; disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps. SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.


FUNCTION: Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. GalD subfamily.


FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function. SUBCELLULAR LOCATION: Cytoplasm, cytosol Secreted Nucleus Cytoplasmic granule Cell membrane Note=Sumoylated form is predominant in the nucleus (PubMed:16443219). Stored in alpha granules in platelets (By similarity). SIMILARITY: Belongs to the PDGF/VEGF growth factor family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.


FUNCTION: Transcription regulator which may participate in NGFR/p75(NTR)-mediated apoptosis. Probably acts as a transcription repressor: specifically binds to the 3'-end of zinc-finger coding genes and recruiting chromatin-modifying proteins such as SETDB1 and TRIM28/KAP1, leading to transcription repression (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co- chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co- chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation (PubMed:28842558). FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co- chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone- mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1- mediated SMAD3 ubiquitination and degradation and facilitates STUB1- mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. FUNCTION: (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Secreted Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. SIMILARITY: Belongs to the heat shock protein 70 family.


FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecA family.


FUNCTION: Component of the large subunit of mitochondrial ribosome. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family.


FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, stress fiber Cytoplasm, cell cortex Cytoplasm, myofibril, sarcomere Note=Has a punctate cytoplasmic distribution as well as centrosomal distribution typical of dynactin (By similarity). Overexpression in cultured mammalian cells revealed colocalization with cortical actin, stress fibers, and focal adhesion sites, sites of potential interaction between microtubules and the cell cortex (By similarity). In skeletal muscles, costamere localization requires the presence of ANK2 (PubMed:19109891). SIMILARITY: Belongs to the dynactin subunit 4 family.


FUNCTION: An L-glutamate ligase that catalyzes the ATP-dependent post- translational addition of glutamate residues to the C-terminus of ribosomal protein bS6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH. FUNCTION: An L-glutamate ligase that catalyzes the ATP-dependent post- translational addition of glutamate residues to the C-terminus of ribosomal protein bS6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH. SIMILARITY: Belongs to the RimK family.


FUNCTION: May form an ATP-driven capsule polysaccharide export apparatus, in association with the CtrB and CtrD proteins. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC-2 integral membrane protein family.


FUNCTION: Transcription factor involved in endoplasmic reticulum (ER) stress response. Acts as ER stress sensor and activates the transcription factor BZIP50 and the chaperone BIP1. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Nucleus Note=The bZIP domain is translocated into the nucleus in response to ER stress. SIMILARITY: Belongs to the bZIP family.


FUNCTION: Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell surface. SIMILARITY: Belongs to the type I cytokine receptor family. Type 4 subfamily.


FUNCTION: Protein phosphatase involved in abscisic acid (ABA) signaling. Together with PYL3 and SAPK10, may form an ABA signaling module involved in stress response. SIMILARITY: Belongs to the PP2C family.


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BRX family.


FUNCTION: Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL22 family.


FUNCTION: Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HesA/MoeB/ThiF family.


FUNCTION: [Isoform 3]: Does not affect cell growth. SUBCELLULAR LOCATION: Note=Contrary to isoforms 1 and 2, isoform 3 does not localize to the mitochondria.


FUNCTION: Pseudouridine synthase that catalyzes pseudouridylation of mRNAs and tRNAs. Mediates pseudouridylation of mRNAs with the consensus sequence 5'-GUUCNANNC-3', harboring a stem-loop structure. Constitutes the major pseudouridine synthase acting on mRNAs. Also catalyzes pseudouridylation of some tRNAs, including synthesis of pseudouridine(55) from uracil-55, in the psi GC loop of a subset of tRNAs. Promotes the processing of pri-let-7 microRNAs (pri-miRNAs) independently of its RNA pseudouridylate synthase activity. Acts by binding to the stem-loop structure on pri-let-7, preventing LIN28- binding (LIN28A and/or LIN28B), thereby enhancing the interaction between pri-let-7 and the microprocessor DGCR8, which mediates miRNA maturation. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Note=Catalyzes pseudouridylation of mRNAs in the nucleus. SIMILARITY: Belongs to the pseudouridine synthase TruB family.


FUNCTION: Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. FUNCTION: Acts as a chaperone for newly synthesized free N protein, so- called N(0). Stabilizes the L protein upon binding it. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the respirovirus P protein family.


FUNCTION: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes. Plays a role in dendrite formation by melanocytes. SIMILARITY: Belongs to the copine family.


FUNCTION: Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress. May require iron for activity. FUNCTION: Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress, such as ytfE, hmpA and ygbA. May require iron for activity. Does not regulate its own transcription.


FUNCTION: Methyltransferase involved in methanogenesis in the methanol pathway. Catalyzes the methylation of the MtaC-bound cob(I)amide. SIMILARITY: Belongs to the MtaB family.


FUNCTION: An FAD-requiring monooxygenase active on some tetracycline antibiotic derivatives, which leads to their inactivation. Hydroxylates carbon 11a of tetracycline and some analogs. FUNCTION: Confers resistance to tetracycline via an oxidoreductase activity; NADPH is more active than NAD (Probable). Expression in E.coli leads to breakdown of tetracycline. Confers resistance to doxycycline, chlortetracycline, oxytetracycline and minocycline (PubMed:2644186). FUNCTION: This bacteria is able to grow in the presence of moderate concentrations of tetracycline and its analogs, presumably due to the presence of this protein (PubMed:19187139). Expression in E.coli leads to breakdown of tetracycline; the initial products include a monooxygenated compound. After 2 hours intact tetracycline is no longer detectable in the culture supernatant, while degradation intermediates remain detectable for at least 20 hours (PubMed:26038239). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aromatic-ring hydroxylase family. TetX subfamily.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MscS (TC 1.A.23) family.


FUNCTION: Specifically methylates the guanosine in position 748 of 23S rRNA. Confers resistance to the macrolide antibiotic tylosine. SIMILARITY: Belongs to the methyltransferase superfamily. RlmA family.


FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.


FUNCTION: Modulates postsynaptic dendritic arbor elaboration and synaptic maturation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Synapse. SIMILARITY: Belongs to the neuritin family.


FUNCTION: Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein OPG116. Serves as a bridge which links the DNA polymerase OPG071 and the uracil DNA glycosylase. SIMILARITY: Belongs to the orthopoxvirus OPG148 family.


FUNCTION: Functions as a general transcription factor playing a role in the process of transcriptional elongation. May mediate the reciprocal stimulatory effect of splicing on transcriptional elongation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HTATSF1 family.


FUNCTION: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, FMR1, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1, CHTOP and MAP3K5/ASK1 (PubMed:12737817, PubMed:15837430, PubMed:18492485, PubMed:22095282, PubMed:19405910). Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation (By similarity). May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway (By similarity). Methylates RBM15, promoting ubiquitination and degradation of RBM15 (By similarity). Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity (By similarity). Methylates CHTOP and this methylation is critical for its 5- hydroxymethylcytosine (5hmC)-binding activity (By similarity). Methylates MAP3K5/ASK1 at 'Arg-85' and 'Arg-87' which promotes association of MAP3K5 with thioredoxin and negatively regulates MAP3K5 association with TRAF2, inhibiting MAP3K5 stimulation and MAP3K5- induced activation of JNK (PubMed:22095282). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity). Plays a role in regulating alternative splicing in the heart (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Cytoplasm, cytosol Cytoplasm Note=Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction (By similarity). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.


FUNCTION: Catalyzes the hydrolysis of glucose from the disaccharide unit linked to hydroxylysine residues of collagen and collagen-like proteins. SIMILARITY: Belongs to the glycosyl hydrolase 65 family.


FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins (By similarity). Regulates cilium formation and structure (PubMed:23807208). SUBCELLULAR LOCATION: Cytoplasm Cell projection. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily.


FUNCTION: Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis. SUBCELLULAR LOCATION: Membrane; Single- pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.


FUNCTION: Acts as GTPase-activating protein for RAB3A, RAB22A, RAB27A and RAB35. Does not act on RAB2A and RAB6A (By similarity). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin. SIMILARITY: Belongs to the chalcone isomerase family.


FUNCTION: A probable role in capsular biogenesis. It is likely that the caf1A molecule binds F1 antigen subunits during the extracellular secretion process. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family.


FUNCTION: Plays a role in regulating Notch activity. Plays a role in regulating the expression of CDKN1A and several members of the Wnt pathway, probably via its effects on Notch activity. Required during embryogenesis for inner mass cell survival (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NLE1/RSA4 family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL24 family.


FUNCTION: Regulator of the budABC operon for 2,3-butanediol synthesis. SIMILARITY: Belongs to the LysR transcriptional regulatory family.


SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.


FUNCTION: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. Energy is transferred from the carotenoid and chlorophyll C (or B) to chlorophyll A and the photosynthetic reaction centers where it is used to synthesize ATP and reducing power. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi- pass membrane protein. Note=FCPs are probably transported across the endoplasmic reticulum membranes that surround the plastid via a signal peptide, followed by translocation across the thylakoid membrane via a transit peptide. SIMILARITY: Belongs to the fucoxanthin chlorophyll protein family.


FUNCTION: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded glycoproteins. May be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the derlin family.


FUNCTION: Promotes guanine-nucleotide exchange on ARF1, ARF5 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization, through regulation of ARF6 activity. FUNCTION: Promotes guanine-nucleotide exchange on ARF1, ARF5 and ARF6 (PubMed:18042453, PubMed:20080746). Promotes the activation of ARF factors through replacement of GDP with GTP (PubMed:18042453). Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization, through regulation of ARF6 activity (PubMed:20080746, PubMed:29420262). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Cytoplasm, cytosol Cell junction, tight junction Cell junction, adherens junction Note=Colocalized with TJP1 during epithelial polarization. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Cytoplasm, cytosol Cell junction, tight junction Cell junction, adherens junction Note=Colocalized with TJP1 during epithelial polarization (PubMed:20080746).


FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals. SIMILARITY: Belongs to the metallothionein superfamily. Type 4 family.


FUNCTION: May play a role in meiotic resumption and pronuclear formation, mediated by a WW domain-signaling pathway during fertilization.


FUNCTION: Secreted heat soluble protein acting as a molecular shield in water-deficient condition (PubMed:28306513). Tardigrade-specific intrinsically disordered proteins (TDPs) are essential for desiccation tolerance by forming non-crystalline amorphous solids upon desiccation, and this vitrified state mirrors their protective capabilities (PubMed:28306513). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Secretory-abundant heat soluble protein (SAHS) family.


FUNCTION: Positively regulates a late step in synaptic vesicle exocytosis. Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. Also involved in glucose-induced secretion of insulin by pancreatic beta-cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Perikaryon Presynapse Note=Enriched at synaptic-releasing sites in mature neurons. SIMILARITY: Belongs to the complexin/synaphin family.


FUNCTION: Involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. Binds to dvl2/dsh and impedes the degradation of beta-catenin (ctnnb1-A and possibly ctnnb1-B), thereby enhancing the transcriptional activation of target genes of the Wnt signaling pathway. Also promotes catenin delta/ctnnd1 stability which in turn promotes zbtb33/kaiso sequestration and thus is involved in the regulation of zbtb33/kaiso-mediated transcriptional repression. May also bind to and directly stimulate the transcriptional activity of tcf7l1-A. Required for eye development and neural patterning. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the dapper family.


FUNCTION: Involved in rRNA-processing at A0, A1 and A2 sites through its action in U18 and U24 snoRNA 3'-end final trimming. Negative regulator of telomerase through competition for binding to EST2 with TLC1. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the PINX1 family.


FUNCTION: Plays a central role in executing Spemann's organizer phenomenon (the dorsal blastopore lip of the early Xenopus laevis gastrula can organize a complete secondary body axis when transplanted to another embryo). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily.


FUNCTION: Appears to function during host infection, and may play a role in suppressing the host immune response. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Secreted Host nucleus Host cell membrane. SIMILARITY: Belongs to the RBT5 family.


FUNCTION: Is required for normal leaf, flower and seed development and controls cotyledon and leaf patterning by inhibiting premature differentiation. Regulates the expression of a subset of PcG target genes. Is required for the repression of the floral specific genes PI, SEP2, and SEP3, but also for the activation of FLC (PubMed:20647345). Involved in response to cold. Involved in the regulation of COR15A, COR15B, BAM3 and AMY3 transcripts, and ascorbate levels in response to prolonged chilling temperatures (PubMed:20674078). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=May shuttle between the nucleus and the cytoplasm.


FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein- or glycolipid-linked sialopolylactosamines chain or of a distal or internal lactosamine unit of a neutral glycoprotein- or glycolipid- linked polylactosamines chain through an alpha-1,3 glycosidic linkage and participates in surface expression of the sialyl Lewis X (sLe(x)), Lewis X (Le(x)) and non sialylated VIM2 determinants. Moreover transfers fucose to H-type 2 (Fucalpha1-2Galbeta1-4GlcNAc) chain acceptor substrates and participates in difucosylated sialyl Lewis x determinants. Also fucosylates a polylactosamine substrate having a 6 sulfate modification at the GlcNAc moiety and gives rise to sialyl and non-sialyl 6-sulfo lewis X. Does not have activity towards type 1 ((Galbeta1-3GlcNAc)) and H-type 1 chain (Fucalpha1-2Galbeta1-3GlcNAc) acceptors substrates. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein Golgi apparatus Secreted Note=Membrane-bound form in trans cisternae of Golgi. SIMILARITY: Belongs to the glycosyltransferase 10 family.


FUNCTION: Might play a role in cell proliferation. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (PubMed:3002446). The full-length protein has collagenase activity, while both the 116 kDa and 98 kDa forms act on gelatin (PubMed:7961400). In vitro digestion of soluble calf skin collagen fibrils requires both ColG and ColH; ColG forms missing the second collagen-binding domain is also synergistic with ColH, although their overall efficiency is decreased (PubMed:18374061, PubMed:22099748). Digestion of collagen requires Ca(2+) and is inhibited by EDTA (PubMed:9452493). The activator domain (residues 119- 388) and catalytic subdomain (330-601) open and close around substrate allowing digestion when the protein is closed (PubMed:23703618). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M9B family. Collagenase subfamily.


FUNCTION: May be involved in strigolactone signaling pathway (By similarity). Essential for plant responses to karrikins, a class of butenolide compounds, structurally similar to strigolactones, released from burning vegetation that stimulate seed germination and enhance seedling photomorphogenesis. Mediates a specific perception of karrikin. Required for the establishment of symbiosis with the arbuscular mycorrhizal fungi (AMF) Rhizophagus irregularis and Gigaspora rosea (PubMed:26680197). Karrikin binding induces a conformational change (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the AB hydrolase superfamily.


FUNCTION: Multidrug exporter. Is implicated for the resistance to bacteriocidal quaternary ammonium compounds and ethidium bromide. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CD225/Dispanin family.


FUNCTION: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate (PubMed:4557653, PubMed:8606183). Is required for E.coli to grow on glycolate as a sole source of carbon (PubMed:8606183). Is also able to oxidize D-lactate ((R)-lactate) with a similar rate (PubMed:4557653). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown (PubMed:4557653). SUBCELLULAR LOCATION: Cell inner membrane Note=Glycolate oxidoreductase activity was shown to be firmly associated with the cytoplasmic membranes (PubMed:2689218). And the GlcF subunit itself could only be detected in the membrane fraction (PubMed:8606183).


FUNCTION: Cleaves the N-terminal leader peptide from preflagellins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A24 family. Archaeal preflagellin peptidase subfamily.


SIMILARITY: To B.subtilis XkdV.


FUNCTION: Transcription inhibitory protein for the torCAD operon. Also acts as an excisionase and plays an essential role in the defective prophage CPS53 excision (By similarity). FUNCTION: Transcription inhibitory protein for the torCAD operon. Also acts as an excisionase and plays an essential role in the defective prophage CPS53 excision. FUNCTION: Excisionase and integrase are necessary for the excision of prophage from the host genome by site-specific recombination at the att site. SIMILARITY: Belongs to the phage alpA excisionase family. SIMILARITY: Belongs to the phage AlpA excisionase family.


FUNCTION: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft- association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication. SUBCELLULAR LOCATION: Virion membrane Host apical cell membrane; Single-pass type II membrane protein Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane (By similarity). SIMILARITY: Belongs to the glycosyl hydrolase 34 family.


FUNCTION: Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases. FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1B family.


FUNCTION: Transcriptional repressor of the nikABCDE operon. Is active in the presence of excessive concentrations of intracellular nickel. SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDS family.


SUBCELLULAR LOCATION: Virion membrane. SIMILARITY: Belongs to the asfivirus EP84R family.


FUNCTION: May be involved in polysaccharide transport. FUNCTION: May be involved in polysaccharide transport. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BexD/CtrA/VexA family.


FUNCTION: Scytalone dehydratase-like protein; part of the Pks2 gene cluster that mediates the formation of infectious structures (appressoria), enabling these fungi to kill insects faster (PubMed:29958281). The product of the Pks2 gene cluster is different from the one of Pks1 and has still not been identified (PubMed:29958281). SIMILARITY: Belongs to the scytalone dehydratase family.


FUNCTION: In nitrogen-limiting conditions, when the ratio of Gln to 2- ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity). SIMILARITY: Belongs to the P(II) protein family.


FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S- nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of pro- inflammatory mediators such as IL6 and IL8. SUBCELLULAR LOCATION: Cytoplasm, cytosol Note=Localizes as discrete foci scattered throughout the cytosol and in the presence of SPSB1 and SPSB4, exhibits a more diffuse cytosolic localization. SIMILARITY: Belongs to the NOS family.


FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family.


SIMILARITY: Belongs to the TrbE/VirB4 family.


FUNCTION: Involved in the regulation of gene expression in the retina. It functions as a negative regulator of CRX-controlled genes. SUBCELLULAR LOCATION: Nucleus Cytoplasm.


FUNCTION: It is not clear if it plays a role in trans-translation (a process which rescues stalled ribosomes). Evidence for its role; binds to tmRNA with very high affinity, is required for binding of tmRNA to 30S subunit (PubMed:11101533, PubMed:15340139). Thought to play a role only in translation of the tmRNA in vitro (PubMed:17392345). Evidence against its role; overexpression of whole protein or various S1 fragments inhibits translation, they have no effect on trans- translation, and an in vitro system with S1-less ribosomes performs trans-translation (PubMed:15340139, PubMed:17376482). In trans- translation Ala-aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA gene; the 2 termini fold to resemble tRNA(Ala) while it encodes a short internal open reading frame (the tag peptide)) acts like a tRNA, entering the A-site of the ribosome and displacing the stalled mRNA (which is subsequently degraded). The ribosome then switches to translate the ORF on the tmRNA, the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and thus targeted for degradation. FUNCTION: In case of infection by bacteriophage T4, plays a significant role in substrate choice by viral endoribonuclease RegB. FUNCTION: In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex; this subunit is required for RNA replication initiation activity during synthesis of (-) strand RNA from the (+) strand genomic RNA but not for (+) strand synthesis from the (-) strand (PubMed:6358207, PubMed:25122749). Binds an approximately 70 nucleotide RNA internal to the viral replicase gene (the M-site) (PubMed:25122749). Others have reported it is not involved in RNA replication initiation but rather in termination of RNA synthesis and is required for termination whether it is the (+) or (-) strand that is being synthesized (PubMed:23653193). FUNCTION: Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence (By similarity). FUNCTION: Required for translation of most natural mRNAs except for leaderless mRNA (PubMed:9677288, PubMed:7003157, PubMed:12068815, PubMed:17376482, PubMed:24339747). Binds mRNA upstream of the Shine- Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated (PubMed:24339747). Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides (PubMed:22908248). Has a preference for polypyrimidine tracts (PubMed:778845). Negatively autoregulates its own translation (PubMed:2120211). FUNCTION: Required for translation of most natural mRNAs except for leaderless mRNA. Binds mRNA upstream of the Shine-Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated. Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides. Has a preference for polypyrimidine tracts. Negatively autoregulates its own translation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.


FUNCTION: May be involved in metal transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CbiM family.


FUNCTION: Mediates the export of fixed carbons from the chloroplasts into the cytosol in the form of triose phosphates. SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. Note=Located in zones of contact between the inner and outer membrane of the chloroplast. SIMILARITY: Belongs to the TPT transporter family. TPT (TC 2.A.7.9) subfamily.


FUNCTION: BCL2-like protein which disrupts the host immune response by inhibiting the TLR4 signaling pathway leading to NF-kappa-B activation. Acts close to the plasma membrane and targets several host TIR-domain containing adapter proteins including MYD88, TIRAP, TRIF and TICAM2. In turn, blocks the host NF-kappa-B and TRIF-mediated IRF3 activation. SIMILARITY: Belongs to the orthopoxvirus OPG176 family.


FUNCTION: Blocker of A-type voltage-gated potassium channels of cerebellar granular cells. May also inhibit Kv4/KCND when coexpressed with DPP6 or DPP10. The occlusion of the outer entry of the K(+) conducting pore is partially reversible and affects both open and closed channels. It shares the same target in rat brain than BmTX3 (AC Q8I0L5) and AmmTX3 (AC P60208). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 15 subfamily.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 family.


FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6- phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (PubMed:28803808). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility (PubMed:11437381). Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons (PubMed:3352745, PubMed:11004567). It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion (PubMed:3352745, PubMed:11004567). SUBCELLULAR LOCATION: Cytoplasm Secreted. SIMILARITY: Belongs to the GPI family.


FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase- dependent and -independent mechanisms. Selectively targets single- stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family.


FUNCTION: Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)- salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ferric reductase (FRE) family.


FUNCTION: Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IPI1/TEX10 family.


FUNCTION: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into several unidentified sesquiterpenes (PubMed:30254228). TPS10 also converts geranylgeranyl diphosphate (GGPP) into the diterpene beta-araneosene (PubMed:31621716). SIMILARITY: Belongs to the terpene synthase family.


FUNCTION: Probably functions in cell division and growth processes. Interacts with certain SNAREs as part of specialized membrane fusion events where vesicles from the same organelle fuse (homotypic fusion) (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, phragmoplast Note=Primarily localized to the nucleus and, during cytokinesis, to the phragmoplast, a site where membrane vesicles are targeted in the deposition of new cell wall materials. SIMILARITY: Belongs to the AAA ATPase family.


FUNCTION: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. FUNCTION: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein Note=Localizes to the division septum. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein Note=Localizes to the division septum. Localization requires FtsQ and FtsL, but not FtsW and FtsI. Localization of FtsB and FtsL is codependent. SIMILARITY: Belongs to the FtsB family.


FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6 subfamily.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TMCO5 family.


FUNCTION: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. SIMILARITY: Belongs to the protein disulfide isomerase family.


FUNCTION: Involved in maintenance of centrosome cohesion, probably as part of a linker structure which prevents centrosome splitting. Required for localization of CDK5RAP2 to the centrosome during interphase. Contributes to CROCC/rootletin filament formation. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes to thin fibers protruding away from the proximal ends of the two centrioles. Dissociates from interphase centrosomes at the onset of mitosis.


FUNCTION: Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon- exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as an EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus, nucleoplasm Note=Shuttles between the nucleus and the cytoplasm. Nuclear export is mediated by XPO1/CRM1. SIMILARITY: Belongs to the pym family.


FUNCTION: Involved in assembly and/or maintenance of motile cilia. Required during spermatogenesis for axoneme elongation. Necessary for optimal function of the chordotonal (hearing) organs. SUBCELLULAR LOCATION: Cell projection, cilium Perikaryon Cytoplasm. SIMILARITY: Belongs to the CFAP97 family.


FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. SIMILARITY: Belongs to the HAUS3 family.


FUNCTION: Required for efficient RNA interference (RNAi) of pop-1 indicating a role in the germline development. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.


FUNCTION: Peripheral membrane component of the cis-Golgi stack that acts as a membrane skeleton that maintains the structure of the Golgi apparatus, and as a vesicle thether that facilitates vesicle fusion to the Golgi membrane (PubMed:9150144, PubMed:20197635). Required for normal protein transport from the endoplasmic reticulum to the Golgi apparatus and the cell membrane (By similarity). Together with p115/USO1 and STX5, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus (PubMed:10679020, PubMed:11035033, PubMed:18167358). Plays a central role in mitotic Golgi disassembly: phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the interaction with p115/USO1, preventing tethering of COPI vesicles and thereby inhibiting transport through the Golgi apparatus during mitosis (PubMed:9753325). Also plays a key role in spindle pole assembly and centrosome organization (PubMed:26165940). Promotes the mitotic spindle pole assembly by activating the spindle assembly factor TPX2 to nucleate microtubules around the Golgi and capture them to couple mitotic membranes to the spindle: upon phosphorylation at the onset of mitosis, GOLGA2 interacts with importin-alpha via the nuclear localization signal region, leading to recruit importin-alpha to the Golgi membranes and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2 then activates AURKA kinase and stimulates local microtubule nucleation. Upon filament assembly, nascent microtubules are further captured by GOLGA2, thus linking Golgi membranes to the spindle (By similarity). Regulates the meiotic spindle pole assembly, probably via the same mechanism (By similarity). Also regulates the centrosome organization (By similarity). Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum-Golgi intermediate compartment membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton, spindle pole Note=Associates with the mitotic spindle during mitosis. SIMILARITY: Belongs to the GOLGA2 family.


FUNCTION: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase GPI14 (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type III membrane protein. SIMILARITY: Belongs to the PIGX family.


FUNCTION: Antimicrobial peptide with potent activity against Gram- positive and Gram-negative bacteria. Activity against E.coli and B.subtilis. Weaker activity against L.mucor, s.marcescens and P.aeruginosa. May play a role in innate host defense. SUBCELLULAR LOCATION: Secreted Membrane; Peripheral membrane protein Note=Associates with phospholipid membranes via its amphipathic helix and can insert into the lipid bilayer. SIMILARITY: Belongs to the pleurocidin family.


FUNCTION: Acts as a translational repressor of SRE-containing messengers. SUBCELLULAR LOCATION: Cytoplasm Cell projection, dendrite Synapse, synaptosome Note=Colocalizes throughout the cytoplasm in granules with polyadenylated RNAs, PABPC1 and STAU1. Also frequently colocalizes in cytoplasmic stress granule-like foci with ELAVL1, TIA1 and TIAL1. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner (By similarity). Enriched in synaptoneurosomes. SIMILARITY: Belongs to the SMAUG family.


FUNCTION: Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules (PubMed:29967381). ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. Also implicated in recombination and chromatin maintenance pathways. May protect cells from apoptosis. Associates with mitochondrial DNA. SUBCELLULAR LOCATION: Nucleus Mitochondrion matrix Mitochondrion matrix, mitochondrion nucleoid. SIMILARITY: Belongs to the helicase family.


FUNCTION: Dehydrogenase that converts trans-4-L-hydroxyproline to delta-1-pyrroline-3-hydroxy-5-carboxylate (Hyp) using a quinone as the terminal electron acceptor. Can also use proline as a substrate but with a very much lower efficiency. Does not react with other diastereomers of Hyp: trans-4-D-hydroxyproline and cis-4-L- hydroxyproline. SIMILARITY: Belongs to the proline oxidase family.


FUNCTION: Ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs). Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA. Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen Secreted Nucleus, nucleolus Note=Rapidly endocytosed by target cells and translocated to the nucleus where it accumulates in the nucleolus and binds to DNA (By similarity). SIMILARITY: Belongs to the pancreatic ribonuclease family.


FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uS5 is important for the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Plays a role in the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS5 family.


FUNCTION: Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein (By similarity). Binds free fatty acids and reduces their intracellular esterification (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein C1 family.


FUNCTION: Essential component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Essential for the SPC catalytic activity, possibly by stabilizing and positioning the active center of the complex close to the lumenal surface. Essential for viability. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the SPCS3 family.


FUNCTION: Key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3- phospho-D-glyceroyl phosphate. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.


FUNCTION: Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit (PubMed:21127204). Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Postsynaptic density membrane. SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.


FUNCTION: Involved in the isomerization of 5-deoxy-glucuronate (5DG) to 5-dehydro-2-deoxy-D-gluconate (DKG or 2-deoxy-5-keto-D-gluconate). SIMILARITY: Belongs to the isomerase IolB family.


FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system (By similarity). FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-2-microglobulin family.


FUNCTION: Probable transporter. Confers resistance to cycloheximide. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.


FUNCTION: Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta- catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins. Promotes adipocyte and cardiomyocyte differentiation. SUBCELLULAR LOCATION: Nucleus speckle Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Golgi apparatus. Golgi apparatus, trans- Golgi network. SIMILARITY: Belongs to the chibby family.


FUNCTION: Transcriptional activator that binds specifically to the DNA sequence 5'-TGACG-3'. Recognizes ocs elements like the as-1 motif of the cauliflower mosaic virus 35S promoter. Binding to the as-1-like cis elements mediate auxin- and salicylic acid-inducible transcription. Binds to the hexamer motif 5'-ACGTCA-3' of histone gene promoters. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family.


FUNCTION: Member of the two-component regulatory system SaeR/SaeS involved in the regulation of staphylococcal virulence factors in a strain-dependent fashion. Probably functions as a membrane-associated protein kinase that upon sensing the appropriate signal, autophosphorylates and in turn activates the cytosolic response regulator SaeR (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: In cyliated cells, dynein axonemal particle-specific protein required for deployment of ODA to the axoneme. Interacts with outer dynein arm (ODA) subunits. SUBCELLULAR LOCATION: Dynein axonemal particle.


FUNCTION: 5'->3' double-stranded DNA exonuclease which may also contain a cryptic 3'->5' double-stranded DNA exonuclease activity. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for DNA mismatch repair (MMR) (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1 subfamily.


SUBCELLULAR LOCATION: Glycosome. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.


FUNCTION: Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1- diphosphate (PRPP) to the N9 position of the 6-oxopurines hypoxanthine and guanine to form the corresponding ribonucleotides IMP (inosine 5'- monophosphate) and GMP (guanosine 5'-monophosphate), with the release of PPi. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family.


FUNCTION: Plays a role in melanin biosynthesis. Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6- quinone-2-carboxylic acid. May regulate or influence the type of melanin synthesized. Also to a lower extent, capable of hydroxylating tyrosine and producing melanin. SUBCELLULAR LOCATION: Melanosome membrane; Single-pass type I membrane protein Note=Located to mature stage III and IV melanosomes and apposed endosomal tubular membranes. Transported to pigmented melanosomes by the BLOC-1 complex. Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. SIMILARITY: Belongs to the tyrosinase family.


FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily.


FUNCTION: Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the small heat shock protein (HSP20) family.


SIMILARITY: Belongs to the cornifelin family.


FUNCTION: One of the integral membrane subunits of multisubunit membrane-bound [NiFe]-hydrogenase eha. Eha is predicted to form large electron transfer complex and might catalyze energy-driven reduction of low-potential redox carriers (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EhaA family.


FUNCTION: Involved in the regulation of root growth (PubMed:35637390). May regulate sorting and/or transportation of trans-Golgi network (TGN) vesicles in root cap peripheral cells, thus influencing the extracellular secretion of mucilage components in the root cap (PubMed:35637390). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. SIMILARITY: Belongs to the formiminotransferase family.


FUNCTION: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK4 and CDPK5 (PubMed:32866196). In the mosquito midgut and during the last stage of male gamete exflagellation, may play a role in the rupture of the host erythrocyte membrane (PubMed:22817984). In the mosquito midgut, required for the differentiation of the zygote into the ookinete by promoting the translational activation of a subset of repressed mRNAs; these mRNAs are kept repressed in the zygote by the DOZI- or CITH-containing mRNP complexes (PubMed:22817984, PubMed:24265753). Dispensable during the asexual blood stage (PubMed:24265753). SUBCELLULAR LOCATION: Membrane; Lipid- anchor Cell membrane; Lipid-anchor; Cytoplasmic side Parasitophorous vacuole membrane; Lipid-anchor Cytoplasm Cell projection, cilium, flagellum Host cell membrane; Lipid-anchor Note=Calcium and/or autophosphorylation does not affect membrane localization. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily.


FUNCTION: DNA-binding protein which plays an essential role in nuclear envelope formation (PubMed:17170708). Required for normal chromosome segregation during mitosis (PubMed:12684533). Associates with the nuclear lamina via its interaction with LEM domain containing proteins emr-1 and lem-2 (PubMed:12684533). In association with lem-3, plays a role in radiation-induced DNA damage repair response (PubMed:22383942). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BAF family.


FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Sarcoplasmic reticulum membrane; Multi-pass membrane protein Note=Colocalizes with SclA and SclB at the sarcoplasmic reticulum and the diad, a structure composed of a single t-tubule paired with a terminal cisterna of the sarcoplasmic reticulum. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.


FUNCTION: Mannose-specific lectin. Also binds alpha-methyl-D-mannoside, D-glucose, N-acetyl-D-glucosamine and sucrose but not D-galactose, D- arabinose, D-fructose, D-xylose, lactose or glycoproteins fetiun, PSM and ovalbumin. Shows agglutinating activity towards rabbit erythrocytes. SIMILARITY: Belongs to the leguminous lectin family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the BCLAF1/THRAP3 family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0056 (MarC) family.