ID   CP4A7_RABIT             Reviewed;         511 AA.
AC   P14581;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Cytochrome P450 4A7;
DE   AltName: Full=CYPIVA7;
DE   AltName: Full=Cytochrome P450-KA-2;
DE   AltName: Full=Lauric acid omega-hydroxylase;
DE   AltName: Full=Long-chain fatty acid omega-monooxygenase;
DE            EC=1.14.14.80 {ECO:0000250|UniProtKB:Q02928};
DE   Flags: Precursor;
GN   Name=CYP4A7;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=2340280; DOI=10.1021/bi00456a004;
RA   Johnson E.F., Walker D.L., Griffin K.J., Clark J.E., Okita R.T.,
RA   Meurhoff A.S., Masters B.S.S.;
RT   "Cloning and expression of three rabbit kidney cDNAs encoding lauric acid
RT   omega-hydroxylases.";
RL   Biochemistry 29:873-879(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 5-24.
RC   TISSUE=Kidney;
RX   PubMed=2600085; DOI=10.1016/s0021-9258(20)88237-4;
RA   Yokotani N., Bernhardt R., Sogawa K., Kusunose E., Gotoh O., Kusunose M.,
RA   Fujii-Kuriyama Y.;
RT   "Two forms of omega-hydroxylase toward prostaglandin A and laurate. cDNA
RT   cloning and their expression.";
RL   J. Biol. Chem. 264:21665-21669(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 5-24.
RC   TISSUE=Kidney;
RX   PubMed=2127276; DOI=10.1093/oxfordjournals.jbchem.a123239;
RA   Yoshimura R., Kusunose E., Yokotani N., Yamamoto S., Kubota I.,
RA   Kusunose M.;
RT   "Purification and characterization of two forms of fatty acid omega-
RT   hydroxylase cytochrome P-450 from rabbit kidney cortex microsomes.";
RL   J. Biochem. 108:544-548(1990).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC       In liver microsomes, this enzyme is involved in an NADPH-dependent
CC       electron transport pathway. It oxidizes a variety of structurally
CC       unrelated compounds, including steroids, fatty acids, and xenobiotics.
CC   -!- FUNCTION: The kidney P-450 system is rather specialized for the omega-
CC       hydroxylation of fatty acids. Both P450-KA1 and P450-KA2 catalyze the
CC       omega- and (omega-1)-hydroxylation of various fatty acids with no drug-
CC       metabolizing activity, and hydroxylate prostaglandin A1 and A2 solely
CC       at the omega-position.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--
CC         hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid +
CC         H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:140991,
CC         ChEBI:CHEBI:140992; EC=1.14.14.80;
CC         Evidence={ECO:0000250|UniProtKB:Q02928};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P51869};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Liver, kidney, small intestine.
CC   -!- INDUCTION: P450 can be induced to high levels in liver and other
CC       tissues by various foreign compounds, including drugs, pesticides, and
CC       carcinogens.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M28657; AAA31231.1; -; mRNA.
DR   EMBL; M29530; AAA31233.1; -; mRNA.
DR   PIR; B34160; B34160.
DR   RefSeq; NP_001164541.1; NM_001171070.1.
DR   AlphaFoldDB; P14581; -.
DR   SMR; P14581; -.
DR   GeneID; 100328944; -.
DR   KEGG; ocu:100328944; -.
DR   CTD; 100328944; -.
DR   InParanoid; P14581; -.
DR   OrthoDB; 825914at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; IEA:UniProtKB-EC.
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; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW   Reference proteome.
FT   PROPEP          1..4
FT                   /evidence="ECO:0000269|PubMed:2127276,
FT                   ECO:0000269|PubMed:2600085"
FT                   /id="PRO_0000003577"
FT   CHAIN           5..511
FT                   /note="Cytochrome P450 4A7"
FT                   /id="PRO_0000003578"
FT   BINDING         322
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P51869"
FT   BINDING         458
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:0000250|UniProtKB:P51869"
FT   CONFLICT        99
FT                   /note="C -> V (in Ref. 2; AAA31233)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="F -> S (in Ref. 2; AAA31233)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392..393
FT                   /note="SK -> RQ (in Ref. 2; AAA31233)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        477
FT                   /note="V -> L (in Ref. 2; AAA31233)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   511 AA;  58319 MW;  21FD8215D26A4451 CRC64;
     MSVSALSSTR LPGSFSGFLQ AAALLGLLLL LLKAAQLYLR RQWLLRALQQ FPCPPSHWLL
     GHSREFPIDS ELQQVLKRVE KFPSACPRWL WGSELFLICY DPDYMKTILG RSDPKARVSY
     SFLAPWIGYG LLLLEGQTWF QHRRMLTPAF HYDILKPYVG LMVDSVQVML DKLEKLARKD
     APLEIYEHVS LMTLETIMKC AFSHQGSVQL ESRTSKSYIQ AVRELSDLAL QRVRNVFHQS
     DFLYRLSPEG RLSHRACQLA HEHTDRVIQQ RKAQLQQEGE LEKVRRKRRL DFLDVLLFAK
     MENGSSLSDQ DLRAEVDTFM FEGHDTTASG ISWIFYALAT HPEHQHRCRE EIQGLLGDGA
     SITWEHLDKM PYTTMCIKEA LRLYPPVPGV GSKLSSPVTF PDGRSLPKGI IITLSIYGLH
     HNPKVWPNPE VFDPSRFAPG SARHSHAFLP FSGGSRNCIG KQFAMNELKV AVALTLVRFE
     LLPDPTRVPI PITRLVLKSK NGIHLRLRKL H