ID A0A2K5HSF0_COLAP Unreviewed; 512 AA. AC A0A2K5HSF0; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 16-JAN-2019, entry version 7. DE RecName: Full=Cytochrome P450 {ECO:0000256|RuleBase:RU000461}; DE EC=1.14.14.1 {ECO:0000256|RuleBase:RU000461}; GN Name=CYP1A1 {ECO:0000313|Ensembl:ENSCANP00000007272}; OS Colobus angolensis palliatus (Peters' Angolan colobus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; 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., RA Doddapaneni H., Gnanaolivu R., Gross S., Jayaseelan J., Jones J., RA Khan Z., Kovar C., Kurapati P., Le B., Lee S., Mathew T., RA Narasimhan A., Okwuonu G., Ongeri F., Osuji N., Qu C., Quiroz J., RA Rajbhandari K., Reid J.G., Santibanez J., Skinner E., Wang Y., Xin Y., RA Han Y., Muzny D.M., 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 -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate CC monooxygenases. {ECO:0000256|RuleBase:RU000461}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an alkane + O2 + reduced [NADPH--hemoprotein reductase] = CC a primary alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15734, ChEBI:CHEBI:18310, CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.1; CC Evidence={ECO:0000256|RuleBase:RU000461}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|RuleBase:RU000461}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|RuleBase:RU000461}. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC {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; ENSGT00940000153539; -. DR OrthoDB; 702827at2759; -. DR Proteomes; UP000233080; Whole Genome Shotgun Assembly. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0101020; F:estrogen 16-alpha-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: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: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:0008202; P:steroid 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 Complete proteome {ECO:0000313|Proteomes:UP000233080}; KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU000461}; KW Heme {ECO:0000256|RuleBase:RU000461}; KW Iron {ECO:0000256|RuleBase:RU000461}; KW Metal-binding {ECO:0000256|RuleBase:RU000461}; KW Microsome {ECO:0000256|RuleBase:RU000461}; 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 //