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Database: UniProt
Entry: G3VB36_SARHA
LinkDB: G3VB36_SARHA
Original site: G3VB36_SARHA 
ID   G3VB36_SARHA            Unreviewed;       665 AA.
AC   G3VB36;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 2.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Arachidonate 12-lipoxygenase, 12S type {ECO:0008006|Google:ProtNLM};
GN   Name=LOC100933073 {ECO:0000313|Ensembl:ENSSHAP00000000390.2};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000000390.2, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000000390.2, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000000390.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601885-1};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000256|PIRSR:PIRSR601885-1};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR   AlphaFoldDB; G3VB36; -.
DR   STRING; 9305.ENSSHAP00000000390; -.
DR   Ensembl; ENSSHAT00000000395.2; ENSSHAP00000000390.2; ENSSHAG00000000343.2.
DR   eggNOG; ENOG502QQSP; Eukaryota.
DR   GeneTree; ENSGT00940000155191; -.
DR   HOGENOM; CLU_004282_3_3_1; -.
DR   InParanoid; G3VB36; -.
DR   TreeFam; TF105320; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR   GO; GO:0004052; F:arachidonate 12(S)-lipoxygenase activity; IEA:Ensembl.
DR   GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; IEA:Ensembl.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:Ensembl.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR   GO; GO:0019395; P:fatty acid oxidation; IEA:Ensembl.
DR   GO; GO:1901751; P:leukotriene A4 metabolic process; IEA:Ensembl.
DR   GO; GO:0043651; P:linoleic acid metabolic process; IEA:Ensembl.
DR   GO; GO:2001303; P:lipoxin A4 biosynthetic process; IEA:Ensembl.
DR   GO; GO:2001306; P:lipoxin B4 biosynthetic process; IEA:Ensembl.
DR   GO; GO:0019372; P:lipoxygenase pathway; IEA:Ensembl.
DR   GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl.
DR   Gene3D; 3.10.450.60; -; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR000907; LipOase.
DR   InterPro; IPR013819; LipOase_C.
DR   InterPro; IPR036226; LipOase_C_sf.
DR   InterPro; IPR020834; LipOase_CS.
DR   InterPro; IPR001885; LipOase_mml.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR   PANTHER; PTHR11771:SF4; POLYUNSATURATED FATTY ACID LIPOXYGENASE ALOX12; 1.
DR   Pfam; PF00305; Lipoxygenase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PRINTS; PR00087; LIPOXYGENASE.
DR   PRINTS; PR00467; MAMLPOXGNASE.
DR   SMART; SM00308; LH2; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   SUPFAM; SSF48484; Lipoxigenase; 1.
DR   PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR   PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR601885-2};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|PIRSR:PIRSR601885-1};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601885-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007648}.
FT   DOMAIN          2..117
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          117..665
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
FT   BINDING         17
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT   BINDING         74
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT   BINDING         75
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT   BINDING         363
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT   BINDING         368
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT   BINDING         543
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT   BINDING         665
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT   SITE            102
FT                   /note="Essential for stabilizing binding to COTL1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601885-3"
SQ   SEQUENCE   665 AA;  75883 MW;  457FC21467D8496C CRC64;
     MGRYRVRVAT GNSAFSGSNN QVQLWLVGLR AEVELGLRLR PARGQMEDFE VDVSEDLGPL
     QFVKLRKIHL LIKDAWFCNH ITVWVFEQSM EEKEIVFPCY RWVEGDGIIC LPETTAWMIR
     NESQGLFQKH QEEELKARRT LYGWVSWKKG IPLSVAAASE KDLPLDARFH EEKKVDFERT
     RVVGVTEIAL KRLYTLLSSW NSLEDFDQIF WGGKSALAKR VRLSWKDDDF FGYQFLNGVN
     PTLLRKSSSL PTRLVIPPGT EDLKAQLERK LQEGCLFEVD FSLLAGIQAN VIQGERQHLA
     APLLMLKMEP DGKLLPMVIQ LQLPGSDSPV PPLFLPSDPS LTWLLAKAWV KNSDFQLHEL
     QAHLLKTHLM AEVFAVATMR CLPGMHPIFK LLIPHLRYTL EINTRARTKL ISNGGFFDQA
     VNTGGGGHLD VLRRATTCLT YRSLCPPDDL ADRGLLGVPS AFYAHDAVRL WDIISRYVQG
     IVQLHYLEDE VVRSDPELQA WCREITEIGL CKAQERGFPV SFQSRDELCH FVTMCIFTCT
     AQHSAVNQGQ LDWYTWVPNA PCTMRQPPPT TKDVTLEMVM ATMPNVHQAC IQMTISWHLG
     RFQPDMVPLG HHKEQYFSGP GPQAVLNRFQ EDLYTLEREI VARNESLDLP YEYLKPSRIE
     NSITI
//
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