ID U6DU47_NEOVI Unreviewed; 486 AA. AC U6DU47; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 02-OCT-2024, entry version 32. DE RecName: Full=Cytochrome P450 {ECO:0000256|RuleBase:RU368053}; DE EC=1.14.14.1 {ECO:0000256|RuleBase:RU368053}; GN Name=CP2AD {ECO:0000313|EMBL:CCP86490.1}; OS Neovison vison (American mink) (Mustela vison). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae; OC Mustelinae; Neogale. OX NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP86490.1}; RN [1] {ECO:0000313|EMBL:CCP86490.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Pool of brain {ECO:0000313|EMBL:CCP86490.1}; RA Anistoroaei R., Christensen K.; RT "An American mink transcriptome."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. CC {ECO:0000256|RuleBase:RU368053}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:142491; EC=1.14.14.1; CC Evidence={ECO:0000256|RuleBase:RU368053}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971, CC ECO:0000256|PIRSR:PIRSR602401-1, ECO:0000256|RuleBase:RU368053}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|RuleBase:RU368053}. Microsome membrane CC {ECO:0000256|RuleBase:RU368053}. 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 EMBL; HAAF01014668; CCP86490.1; -; mRNA. DR AlphaFoldDB; U6DU47; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; IEA:TreeGrafter. DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. 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:InterPro. DR GO; GO:0009804; P:coumarin metabolic process; IEA:TreeGrafter. DR GO; GO:0019373; P:epoxygenase P450 pathway; IEA:TreeGrafter. DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:TreeGrafter. DR CDD; cd20668; CYP2A; 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; IPR008067; Cyt_P450_E_grp-I_CYP2A-like. DR InterPro; IPR036396; Cyt_P450_sf. DR InterPro; IPR050182; Cytochrome_P450_fam2. DR PANTHER; PTHR24300:SF180; CYTOCHROME P450 2A13; 1. DR PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR01684; EP450ICYP2A. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, KW ECO:0000256|RuleBase:RU368053}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602401-1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602401-1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR602401-1}; KW Microsome {ECO:0000256|ARBA:ARBA00022848, ECO:0000256|RuleBase:RU368053}; KW Monooxygenase {ECO:0000256|RuleBase:RU000461}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..17 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 18..486 FT /note="Cytochrome P450" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004669297" FT BINDING 431 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 486 AA; 56240 MW; 9750F7DF76187F70 CRC64; MALLACLTIM VLMSVWRQRK LWGKLPPGPT PLPFIGNYLQ LNTEQMYNSL MKISERYGPV FTVHLGPRRI VVLCGHEAVK EALVDQAEEF SGRGEQATFD WLFKGYGVAF SNGERAKQLR RFSITTLRDF GVGKRGIEER IQEEAGFLIE TLRSTQGAFI DPTFFLSRTV SNVISSIVFG DRFDYEDKEF LSLLRMMLGS FQFTATSTGQ LYEMFYSVMK HLPGPQQQAF KELQGLEDFI AKKVEQNQRT LDPNSPRDFI DSFLIRMREE QNNPNTEFYM KNLVLTTLNL FFAGTETVST TLRYGFLLLM KHPHVEAQLH EEIDRVIGKN RQPKFEDRAK MPYTEAVIHE IQRFGDMIPM GLARRVTKDT KFRKFFLPKG TEVFPMLGSV LRDPKFFSNP RDFHPEHFLD ENGQFKKSDA FVPFSIGKRY CFGEGLARME LFLFLTNILQ NFRFKSPQLP QDIDVSPKHV GFATIPRSYT MSFQPR //