FUNCTION: Implicated in promoting R protein-mediated resistance to Pseudomonas syringae pv. tomato (Pst.) DC3000 under continuous light conditions. Promotes systemic acquired resistance (SAR) and PR gene expression triggered by P. syringae. FUNCTION: Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation, and regulates other light responses, including circadian rhythms, tropic growth, stomata opening, guard cell development, root development, bacterial and viral pathogen responses, abiotic stress responses, cell cycles, programmed cell death, apical dominance, fruit and ovule development, seed dormancy, and magnetoreception. Photoexcited cryptochromes interact with signaling partner proteins to alter gene expression at both transcriptional and post-translational levels and, consequently, regulate the corresponding metabolic and developmental programs (PubMed:21841916). Blue-light absorbing flavoprotein that activates reversible flavin photoreduction via an electron transport chain comprising a tryptophan triad (W-324, W-377 and W-400), accompanied by a large conformational change upon photoexcitation, or via an alternative electron transport that involves small metabolites, including NADPH, NADH, and ATP. The half-life of the activated signaling state is about 5 minutes (PubMed:26313597, PubMed:25157750, PubMed:23398192, PubMed:21875594, PubMed:21467031). Also involved in the detection of blue/green ratio in light (shade under leaf canopies) and subsequent adaptations on plant growth and development (PubMed:20668058). In darkness, the dark reoxidation of flavin occurs and leads to inactivated state (PubMed:21467031, PubMed:23398192). Perceives low blue light (LBL) and responds by directly contacting two bHLH transcription factors, PIF4 and PIF5, at chromatin on E-box variant 5'-CA[CT]GTG-3' to promote their activity and stimulate specific gene expression to adapt global physiology (e.g. hypocotyl elongation and hyponastic growth in low blue light) (PubMed:26724867, PubMed:19558423). When activated by high-intensity blue light, catalyzes direct enzymatic conversion of molecular oxygen O(2) to reactive oxygen species (ROS) and hydrogen peroxide H(2)O(2) in vitro. ROS accumulation upon activation by blue light leads to cell death in protoplasts (PubMed:25728686). Seems essential for blue-light- triggered and singlet oxygen-mediated programmed cell death (PCD) (PubMed:17075038). Required for the induction of nuclear genes encoding photoprotective components by GATA24 and GATA28 in extreme light intensities that exceed the electron utilization capacity of the chloroplast (PubMed:22786870). Involved in shortening the circadian clock period, especially at 27 degrees Celsius, in blue light (BL) and required to maintain clock genes expression rhythm (PubMed:23511208). Mediates blue light-induced gene expression and hypocotyl elongation through the inhibition of COP1-mediated degradation of the transcription factors BIT1 and HY5 and via the activation of anion channels at the plasma membrane, probably via auxin signaling (PubMed:21511872, PubMed:21511871, PubMed:16093319, PubMed:18397371, PubMed:12324610, PubMed:8528277, PubMed:9765547, PubMed:25721730). Required for the hypocotyl hook formation in darkness (PubMed:22855128). Involved in blue light-dependent stomatal opening, CHS gene expression, transpiration, inhibition of stem growth and increase of root growth, probably by regulating abscisic acid (ABA) (PubMed:22147516, PubMed:16093319, PubMed:16703358, PubMed:7756321, PubMed:9565033). Prevents lateral roots growth by inhibiting auxin transport (PubMed:20133010). Necessary for shade avoidance syndrome (SAS), characterized by leaf hyponasty and reduced lamina/petiole ratio, when exposed to blue light attenuation (PubMed:21457375). Together with phototropins, involved in phototropism regulation by various blue light fluence; blue light attenuates phototropism in high fluence rates (100 umol.m-2.s-1) but enhances phototropism in low fluence rates (<1.0 umol.m-2.s-1) (PubMed:12857830). Required for blue/UV-A wavelengths-mediated inhibition of explants shoot regeneration in vitro (e.g. new shoot apical meristems regeneration from excised cotyledons) (PubMed:22681544). Modulates anthocyanin accumulation in a PHYA-dependent manner in far-red-light. Acts as a PHYA/PHYB-dependent modulator of chlorophyll accumulation in red light. Contributes to most blue light deetiolation responses (PubMed:9733523, PubMed:8528277). May act as a chemical magnetoreceptor, via magnetically sensitive kinetics and quantum yields of photo-induced flavin / tryptophan radical pairs (PubMed:22421133). The effect of near-null magnetic field on flowering is altered by changes of blue light cycle and intensity in a CRY1/CRY2-dependent manner (PubMed:26095447). Involved in the strigolactone signaling that regulates hypocotyl growth in response to blue light (PubMed:24126495). Modulates temperature-dependent growth and physiology maintenance, especially at warm ambient temperatures, via HFR1-dependent activity (PubMed:21265897). SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, PML body Note=The nuclear pool is involved in hypocotyl and petiole growth inhibition and anthocyanin production, while the cytoplasmic pool is involved in root growth and cotyledon expansion (PubMed:18003924). Present in nuclear bodies (NBs) (PubMed:21511872, PubMed:21765176). SIMILARITY: Belongs to the DNA photolyase class-1 family.


FUNCTION: May transport inorganic phosphate (Pi). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family.


FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (By similarity). Plays a role in the physiological regulation of the intracellular CoA concentration. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the eukaryotic CoaD family.


FUNCTION: This peptide both inhibits the activity of the angiotensin- converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-potentiating peptide family.


FUNCTION: Possible function in spermatogenesis. Enhances the degradation of MDM2 and increases the amount of p53 probably by modulating the nucleocytoplasmic transport (By similarity). SUBCELLULAR LOCATION: Nucleus matrix.


FUNCTION: Essential protein that may function as a transcription regulator. Vital for pupal development. Required for proper development of the optic lobes and wings, and abdominal pigmentation. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Putative oxidoreductase. SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA and 5- hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers (By similarity). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family. CCoAMT subfamily.


FUNCTION: Catalyzes the ATP-dependent phosphorylation of D-glucosamine (GlcN) to D-glucosamine 6-phosphate. May be involved in the phosphorylation of acquired extracellular GlcN derived from the hydrolysis of chitosan, i.e., in the incorporation of exogenous GlcN into the bacterial GlcNAc metabolism. Is unable to phosphorylate maltose. SIMILARITY: Belongs to the actinobacterial glucosamine kinase family.


FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the V-ATPase E subunit family.


FUNCTION: Inhibits urokinase-type plasminogen activator. SUBCELLULAR LOCATION: Cytoplasm Secreted, extracellular space. SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.


FUNCTION: Catalyzes the intramolecular carbocycle formation from D- glucose-6-phosphate to 2-deoxy-scyllo-inosose (DOI). SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. DOI synthase family.


FUNCTION: Catalyzes the electroneutral exchange or flux of physiologically important metabolites such as dicarboxylates (malonate, malate, succinate), inorganic sulfur-containing anions, and phosphate, across mitochondrial inner membrane (PubMed:29211846). Plays an important role in gluconeogenesis, fatty acid metabolism, urea synthesis, and sulfur metabolism, particularly in liver, by supplying the substrates for the different metabolic processes. Regulates fatty acid release from adipocytes, and contributes to systemic insulin sensitivity (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: Catalyzes the methylation of the lipid moiety of the intermediate compounds phthiotriol and glycosylated phenolphthiotriol dimycoserosates to form phthiocerol dimycocerosates (DIM A) and glycosylated phenolphthiocerol dimycocerosates (PGL). SIMILARITY: Belongs to the methyltransferase superfamily. Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase family.


FUNCTION: Involved in ATP-dependent DNA-unwinding in a 3' to 5' direction, and ATP-ase activities stimulated by the single-stranded DNA-binding protein ssb1. Essential for viability and normal growth of stationary phase cells and in the absence of either srs2 or rqh1 DNA helicase (PubMed:16135799, PubMed:9228070). Involved in DNA recombination repair of strand breaks and stalled or collapsed replication forks, on the rhp51-dependent pathway: promotes rhp51 filament dissolution from stalled forks, thereby inhibiting homologous recombination and preventing excessive recombination (PubMed:16135800, PubMed:19546232). Ubiquitination and DNA helicase activities are essential for controlling rhp51-dependent recombination in the absence of rad22. Plays a role in the processing of toxic recombination intermediates. Promotes proper chromosome segregation (PubMed:16135799, PubMed:16135800, PubMed:9228070, PubMed:19546232). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Becomes localized at discrete nuclear foci together with rhp51, in response to DNA strand breakage. SIMILARITY: Belongs to the helicase family. UvrD subfamily.


FUNCTION: Possible role in the regulation of cell death. SUBCELLULAR LOCATION: Nucleus Cytoplasm.


FUNCTION: Produces a 26-residue extracellular sporulation filling factor (SKF) that induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, providing a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation (PubMed:12817086, PubMed:20805502). Can also inhibit growth of other bacteria at high concentrations (PubMed:11851812). Addition of SKF to solid cultures induces killing, but it is much less effective than SDP (AC O34344) (PubMed:20805502). Has a role in protecting the secreted lipase LipA against proteolysis, either by modulating its folding or by acting as a protease inhibitor (PubMed:15812018). SUBCELLULAR LOCATION: Secreted Note=Probably secreted by the ABC transporter SkfEF.


FUNCTION: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. FUNCTION: In addition to cross linking of extracellular matrix proteins, it may have a direct role in tumor suppression. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the lysyl oxidase family.


FUNCTION: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecY/SEC61-alpha family.


FUNCTION: Replication initiator in the monomeric form, and autogenous repressor in the dimeric form. SIMILARITY: Belongs to the initiator RepB protein family.


FUNCTION: Binds to dsDNA in a sequence-specific manner. Also binds a DNA/RNA duplex when the recognized sequence is in the DNA strand. Each tandem core repeat recognizes a single nucleotide in the target DNA via its base-specifying residue (BSR, residue 13 of each repeat); altering this amino acid changes sequence specificity. SIMILARITY: Belongs to the transcription activator-like effector (TALE) family. Bat subfamily.


FUNCTION: Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins like phosphorylated SIC1. Participates in the attachment of chromosomes to the spindle. Acts as a regulatory component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromeres and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly. SKP1/CBF3D could retrieve cyclins or cyclin-CDK-like proteins into the kinetochore thus providing cell cycle-regulated kinetochore activity. Involved in the regulation of methionine biosynthesis genes. Facilitates association of CDC53 with CDC4 and of ROY1 with YPT52. SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome, centromere, kinetochore. SIMILARITY: Belongs to the SKP1 family.


FUNCTION: Dual O-methyltransferase/FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin (By similarity). The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the hydroxyl radical, superoxide, hydrogen peroxide or singlet oxygen upon reaction with oxygen molecules (PubMed:11701851). These reactive oxygen species cause damage to various cellular components including lipids, proteins and nucleic acids (PubMed:11701851). The first step of cercosporin biosynthesis is performed by the polyketide synthase CTB1 which catalyzes the formation of nor-toralactone (By similarity). The starter unit acyltransferase (SAT) domain of CTB1 initiates polyketide extension by the selective utilization of acetyl-CoA, which is elongated to the heptaketide in the beta-ketoacyl synthase (KS) domain by successive condensations with six malonyl units introduced by the malonyl acyltransferase (MAT) domain. The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations to a trihydroxynaphthalene, which is thought to be delivered to the thioesterase (TE) domain for product release (By similarity). The bifunctional enzyme CTB3 then methylates nor-toralactone to toralactone before conducting an unusual oxidative aromatic ring opening (By similarity). The O-methyltransferase CTB2 further methylates the nascent OH-6 of the CBT3 product, blocking further oxidation at this site before the reductase CTB6 reduces the 2- oxopropyl ketone at position C7, giving naphthalene (By similarity). The FAD-dependent monooxygenase CTB5 in concert with the multicopper oxidase CTB12 are responsible for homodimerization of naphthalene with CTB7 installing the dioxepine moiety, finally producing cercosporin (By similarity). The fasciclin domain-containing protein CTB11 might act with CTB5 and CTB12 whereas the roles of CTB9 and CTB10 have still to be elucidated (By similarity). SIMILARITY: In the N-terminal section; belongs to the class I-like SAM- binding methyltransferase superfamily. Cation-independent O- methyltransferase family. COMT subfamily. SIMILARITY: In the C-terminal section; belongs to the paxM FAD- dependent monooxygenase family.


FUNCTION: May be involved in cell wall biosynthesis. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 47 family.


FUNCTION: Probable transcription factor with a role in the retinal determination (RD) network. Regulates ato expression and is required for normal R8 induction and differentiation. Danr appears to repress Dan expression, but Dan is required for Danr expression anterior to the morphogenetic furrow (MF). Dan and Danr lie downstream of so and require dac function for highest levels of expression. Contributes to differentiation of antenna-specific characteristics; effector gene that acts downstream of homothorax (hth), Distal-less (Dll), cut (ct) and spineless (ss) genes to control differentiation of distal antennal structures. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Catalyzes the stereospecific epoxidation of squalene at the terminal double bond to form (S)-2,3-epoxysqualene, the first oxygenation step in sterol biosynthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Detected in the outer envelope of chloroplasts, which is termed the chloroplast endoplasmic reticulum and is continuous with the nuclear envelope. SIMILARITY: Belongs to the sterol desaturase family.


FUNCTION: AAA+ ATPase enhancer-binding protein that acts as a transcription regulator and plays a role in the modulation of mucin adhesion and flagellar gene expression (PubMed:9287015, PubMed:11673434, PubMed:26362077). In addition to flagella genes, regulates also expression of biofilm-related genes (PubMed:22581773). Functions as a transcriptional repressor in the absence of c-di-GMP and as an activator when c-di-GMP is present (PubMed:22581773).


SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit family.


FUNCTION: Involved in both the histidine and tryptophan biosynthetic pathways. FUNCTION: Involved in both the histidine and tryptophan biosynthetic pathways. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family. SIMILARITY: Belongs to the HisA/HisF family.


FUNCTION: Histone acetyltransferase that acetylates histone H2B to form H2BK11ac and H2BK16ac, histone H3 to form H3K14ac, with a lower preference histone H4 to form H4K8ac and H4K16ac, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. In addition to histone acetyltransferase, can use different acyl-CoA substrates, such as (2E)- butenoyl-CoA (crotonyl-CoA) and is able to mediate histone crotonylation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.


FUNCTION: Involved in the biosynthesis of ketocarotenoids which are powerful anti-oxidative molecules (PubMed:21398427, PubMed:22526507). Catalyzes the conversion of zeaxanthin to astaxanthin via adonixanthin (PubMed:21398427, PubMed:22526507). Catalyzes the conversion of beta- carotene to canthaxanthin via echinenone (PubMed:21398427, PubMed:22526507).


FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.


FUNCTION: Minus-end microtubule-dependent motor protein. Involved in apically targeted transport (By similarity). Required for zonula adherens maintenance. SUBCELLULAR LOCATION: Cell junction, adherens junction Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasmic vesicle membrane; Peripheral membrane protein Note=Apical cell membrane. On membrane organelles immediately beneath the apical plasma membrane of renal tubular epithelial cells. Localized in the distal tubules and loops of Henle in the kidney, but not in the proximal tubules or the glomeruli, with stronger staining in the apical area of these epithelial cells (By similarity). Localizes along zonula adherens only at mature cell-cell contacts. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.


FUNCTION: Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SRP receptor beta subunit family.


FUNCTION: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)- dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity). SUBCELLULAR LOCATION: Cell membrane, sarcolemma Cytoplasmic vesicle membrane Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. SIMILARITY: Belongs to the TRIM/RBCC family.


SIMILARITY: Belongs to the UPF0349 family.


FUNCTION: Involved in tanshinone biosynthesis in hairy roots (PubMed:19905026, PubMed:21082262). Catalyzes the conversion of copalyl diphosphate (CPP) to miltiradiene (PubMed:19905026, PubMed:21082262). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family.


FUNCTION: May be involved in a redox-related process. SIMILARITY: Belongs to the SelWTH family.


SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the fibroblast growth factor-binding protein family.


FUNCTION: Required for correct biomineralization of the magnetosome; probably transports some form of iron. Partially functionally redundant with MamZ. SUBCELLULAR LOCATION: Magnetosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: Proton-coupled monocarboxylate symporter. Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L- lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate (PubMed:10417314, PubMed:20695846). Dimerization is functionally required and both subunits work cooperatively in transporting substrate (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Cytoplasm Note=Requires the ancillary protein, EMB for plasma membrane localization (PubMed:15917240, PubMed:20695846). Colocalizes with BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (By similarity). SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family.


FUNCTION: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic side. SIMILARITY: Belongs to the LpoA family.


FUNCTION: Protease-inhibitor that contains multiple distinct protease inhibitor domains. Probably has serine protease- and metalloprotease- inhibitor activity. Inhibits the biological activity of mature myostatin, but not activin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the WFIKKN family.


FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 9S-, 11- and 13R-hydroperoxy fatty acids. At the end of lipoxygenation, the intermediate product 11S-HPODE from linoleic acid is then transformed into 9S-HPODE and 13R-HPODE as the final products. The intermediate product 11R-HPOTrE from alpha-linolenic acid is transformed into 9S-HPOTrE and 13R-HPOTrE as the final products. 9S- HPOTrE is further oxidized by the enzyme to 9S,16S-DiHPOTrE as the end product. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the lipoxygenase family. Manganese lipoxygenase subfamily.