ID A0A2K5HSF0_COLAP Unreviewed; 512 AA. AC A0A2K5HSF0; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 13-SEP-2023, entry version 28. DE RecName: Full=Cytochrome P450 1A {ECO:0000256|RuleBase:RU368045}; DE EC=1.14.14.1 {ECO:0000256|RuleBase:RU368045}; GN Name=CYP1A1 {ECO:0000313|VGNC:VGNC:103497}; 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:ENSCANP00000007272.1, ECO:0000313|Proteomes:UP000233080}; RN [1] {ECO:0000313|Ensembl:ENSCANP00000007272.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2023) to UniProtKB. CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. CC They oxidize a variety of structurally unrelated compounds, including CC steroids, fatty acids, and xenobiotics. CC {ECO:0000256|RuleBase:RU368045}. 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 ECO:0000256|PIRSR:PIRSR602401-1, ECO:0000256|RuleBase:RU368045}; 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|RuleBase:RU368045}; Peripheral membrane protein CC {ECO:0000256|RuleBase:RU368045}. Microsome membrane CC {ECO:0000256|RuleBase:RU368045}; Peripheral membrane protein CC {ECO:0000256|RuleBase:RU368045}. Membrane CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. 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 AlphaFoldDB; A0A2K5HSF0; -. DR STRING; 336983.ENSCANP00000007272; -. DR Ensembl; ENSCANT00000026987.1; ENSCANP00000007272.1; ENSCANG00000023817.1. DR GeneID; 105505165; -. DR KEGG; cang:105505165; -. DR CTD; 1543; -. DR VGNC; VGNC:103497; CYP1A1. DR OMA; WITNQSA; -. DR OrthoDB; 2900138at2759; -. DR UniPathway; UPA00912; -. DR Proteomes; UP000233080; Unplaced. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule. DR GO; GO:0106256; F:hydroperoxy icosatetraenoate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd20676; CYP1A; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24289; STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE; 1. DR PANTHER; PTHR24289:SF13; STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01683; EP450ICYP1A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, KW ECO:0000256|RuleBase:RU368045}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602401-1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602401-1}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR602401-1}; KW Microsome {ECO:0000256|ARBA:ARBA00022848, ECO:0000256|RuleBase:RU368045}; KW Monooxygenase {ECO:0000256|RuleBase:RU000461}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}; KW Reference proteome {ECO:0000313|Proteomes:UP000233080}. FT BINDING 457 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR602401-1" 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 //