ID A0A2K5HSF0_COLAP Unreviewed; 512 AA. AC A0A2K5HSF0; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 12-AUG-2020, entry version 15. DE RecName: Full=Hydroperoxy icosatetraenoate dehydratase {ECO:0000256|ARBA:ARBA00017048}; DE EC=1.14.14.1 {ECO:0000256|ARBA:ARBA00012109}; DE EC=4.2.1.152 {ECO:0000256|ARBA:ARBA00013084}; GN Name=CYP1A1 {ECO:0000313|Ensembl:ENSCANP00000007272}; OS Colobus angolensis palliatus (Peters' Angolan colobus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Colobinae; Colobus. OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000007272, ECO:0000313|Proteomes:UP000233080}; RN [1] {ECO:0000313|Ensembl:ENSCANP00000007272, ECO:0000313|Proteomes:UP000233080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Hughes D.S., Murali S., Raveendran M., Korchina V., Bandaranaike D., RA Bellair M., Blankenburg K., Chao H., Dahdouli M., Dinh H., Doddapaneni H., RA Gnanaolivu R., Gross S., Jayaseelan J., Jones J., Khan Z., Kovar C., RA Kurapati P., Le B., Lee S., Mathew T., Narasimhan A., Okwuonu G., RA Ongeri F., Osuji N., Qu C., Quiroz J., Rajbhandari K., Reid J.G., RA Santibanez J., Skinner E., Wang Y., Xin Y., Han Y., Muzny D.M., RA Richards S., Worley K.C., Rogers J., Gibbs R.A.; RT "Black and white colobus reference genome project."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCANP00000007272} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2018) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo- CC (5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231; CC EC=4.2.1.152; Evidence={ECO:0000256|ARBA:ARBA00001395}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948; CC Evidence={ECO:0000256|ARBA:ARBA00001395}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)- CC octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:57466, ChEBI:CHEBI:90781; CC Evidence={ECO:0000256|ARBA:ARBA00000408}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717; CC Evidence={ECO:0000256|ARBA:ARBA00000408}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo- CC (5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446; CC Evidence={ECO:0000256|ARBA:ARBA00001143}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637; CC Evidence={ECO:0000256|ARBA:ARBA00001143}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced CC [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)- CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:52120, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016, CC ChEBI:CHEBI:136410; Evidence={ECO:0000256|ARBA:ARBA00001204}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121; CC Evidence={ECO:0000256|ARBA:ARBA00001204}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo- CC (6E,8Z,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48632, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:65342; CC Evidence={ECO:0000256|ARBA:ARBA00001867}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633; CC Evidence={ECO:0000256|ARBA:ARBA00001867}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced CC [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)- CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:131965; Evidence={ECO:0000256|ARBA:ARBA00001225}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861; CC Evidence={ECO:0000256|ARBA:ARBA00001225}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced CC [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)- CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:131964; Evidence={ECO:0000256|ARBA:ARBA00001108}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857; CC Evidence={ECO:0000256|ARBA:ARBA00001108}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced CC [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)- CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:76627; Evidence={ECO:0000256|ARBA:ARBA00000525}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760; CC Evidence={ECO:0000256|ARBA:ARBA00000525}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced CC [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)- CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, CC ChEBI:CHEBI:76634; Evidence={ECO:0000256|ARBA:ARBA00000543}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780; CC Evidence={ECO:0000256|ARBA:ARBA00000543}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] CC = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, CC ChEBI:CHEBI:28744, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|ARBA:ARBA00000499}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213; CC Evidence={ECO:0000256|ARBA:ARBA00000499}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] CC = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:62845; CC Evidence={ECO:0000256|ARBA:ARBA00001681}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281; CC Evidence={ECO:0000256|ARBA:ARBA00001681}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-retinal + O2 + reduced [NADPH--hemoprotein CC reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17898, CC ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|ARBA:ARBA00000119}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089; CC Evidence={ECO:0000256|ARBA:ARBA00000119}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-retinol + O2 + reduced [NADPH--hemoprotein CC reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17336, CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|ARBA:ARBA00000340}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093; CC Evidence={ECO:0000256|ARBA:ARBA00000340}; CC -!- CATALYTIC ACTIVITY: CC Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2- CC hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:47208, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:1156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, CC ChEBI:CHEBI:58210; Evidence={ECO:0000256|ARBA:ARBA00000504}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209; CC Evidence={ECO:0000256|ARBA:ARBA00000504}; CC -!- CATALYTIC ACTIVITY: CC Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4- CC hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:47292, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:87602; Evidence={ECO:0000256|ARBA:ARBA00001752}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293; CC Evidence={ECO:0000256|ARBA:ARBA00001752}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC {ECO:0000256|ARBA:ARBA00004891}. CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004406}. Membrane CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. Microsome membrane CC {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004174}. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_011788288.1; XM_011932898.1. DR Ensembl; ENSCANT00000026987; ENSCANP00000007272; ENSCANG00000023817. DR GeneID; 105505165; -. DR GeneTree; ENSGT00950000183037; -. DR OMA; DLTPEYG; -. DR OrthoDB; 702827at2759; -. DR UniPathway; UPA00912; -. DR Proteomes; UP000233080; Whole Genome Shotgun Assembly. DR GO; GO:0008391; F:arachidonic acid monooxygenase activity; IEA:Ensembl. DR GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; IEA:Ensembl. DR GO; GO:0101021; F:estrogen 2-hydroxylase activity; IEA:Ensembl. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:Ensembl. DR GO; GO:0070576; F:vitamin D 24-hydroxylase activity; IEA:Ensembl. DR GO; GO:0009308; P:amine metabolic process; IEA:Ensembl. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl. DR GO; GO:0046483; P:heterocycle metabolic process; IEA:Ensembl. DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl. DR GO; GO:0002933; P:lipid hydroxylation; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR GO; GO:0042572; P:retinol metabolic process; IEA:Ensembl. DR GO; GO:0009404; P:toxin metabolic process; IEA:Ensembl. DR Gene3D; 1.10.630.10; -; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1. DR InterPro; IPR036396; Cyt_P450_sf. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01683; EP450ICYP1A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; SSF48264; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU000461}; Microsome {ECO:0000256|ARBA:ARBA00022848}; KW Monooxygenase {ECO:0000256|RuleBase:RU000461}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}; KW Reference proteome {ECO:0000313|Proteomes:UP000233080}. SQ SEQUENCE 512 AA; 58017 MW; 17E3E16D37CD8D7E CRC64; MLFPISMSAT AFLLASVIFC LVFWVIRASR PRVPKGLKNP PGPWGWPLIG HMLTLGKNPH LALSRMSQRY GDVLQIRIGS TPVLVLSGLD TIRQALVQQG DDFKGRPNLY SFTLVSNGQS MSFGPDSGPV WAARRRLAQN GLKSFSIASD PASSSSCYLE EHVSKEAEVL ISKLQEQMAG PGHFNPYRYV VVSVANVICA ICFGQRYDHD HQELLSLVLL NNNFAEVVGS GNPADFIPIL RYLPNRSLNG FKDLNEKFHS FIQKMIKEHY KTFEKGHIRD ITDSLIEHCQ EKQLDENANI QLSDEKIINV VLDLFGAGFD TVTTAISWSL MYLVTNPRVQ RKIQEELDTV IGRSRPPRLS DRPHLPYLEA FILETFRHSS FVPFTIPHST TRDTSLKGFY IPKGRCVFVN QWQINHDQKL WVNPSEFLPE RFITPDGAIN KVLSEKMILF GLGKRKCIGE TIARWEVFLF LAILLQRVEF SVPPGVKVDM TPIYGLTMKH ACCEHFRMQL RS //