ID   CP4A4_RABIT             Reviewed;         510 AA.
AC   P10611; Q02927;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 3.
DT   03-MAY-2023, entry version 135.
DE   RecName: Full=Cytochrome P450 4A4;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIVA4;
DE   AltName: Full=Cytochrome P450-P-2;
DE   AltName: Full=Prostaglandin omega-hydroxylase;
DE   Flags: Precursor;
GN   Name=CYP4A4;
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 [GENOMIC DNA] OF 1-65.
RC   STRAIN=III/J;
RX   PubMed=8434947; DOI=10.1006/abbi.1993.1093;
RA   Palmer C.N., Griffin K.J., Johnson E.F.;
RT   "Rabbit prostaglandin omega-hydroxylase (CYP4A4): gene structure and
RT   expression.";
RL   Arch. Biochem. Biophys. 300:670-676(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 21-510, AND PROTEIN SEQUENCE OF 5-29.
RX   PubMed=3654614; DOI=10.1016/s0021-9258(18)45210-6;
RA   Matsubara S., Yamamoto S., Sogawa K., Yokotani N., Fujii-Kuriyama Y.,
RA   Haniu M., Shively J.E., Gotoh O., Kusunose E., Kusunose M.;
RT   "cDNA cloning and inducible expression during pregnancy of the mRNA for
RT   rabbit pulmonary prostaglandin omega-hydroxylase (cytochrome P-450p-2).";
RL   J. Biol. Chem. 262:13366-13371(1987).
RN   [3]
RP   FUNCTION.
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       Catalyzes the omega- and (omega-1)-hydroxylation of fatty acids.
CC       {ECO:0000269|PubMed:2127276}.
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P51869};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein. Microsome membrane; Single-pass membrane protein.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA31228.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L04758; AAA31228.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; J02818; AAA31232.1; -; mRNA.
DR   PIR; S32315; A29368.
DR   AlphaFoldDB; P10611; -.
DR   SMR; P10611; -.
DR   BindingDB; P10611; -.
DR   ChEMBL; CHEMBL4743; -.
DR   InParanoid; P10611; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   CDD; cd20678; CYP4B-like; 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; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24291:SF39; CYTOCHROME P450 4A11-RELATED; 1.
DR   PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   PROPEP          1..4
FT                   /evidence="ECO:0000269|PubMed:3654614"
FT                   /id="PRO_0000003571"
FT   CHAIN           5..510
FT                   /note="Cytochrome P450 4A4"
FT                   /id="PRO_0000003572"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         321
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P51869"
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:0000250|UniProtKB:P51869"
SQ   SEQUENCE   510 AA;  58930 MW;  50CB1DE9D9D7FD5D CRC64;
     MSVSALSPTR LPGSLSGLLQ VAALLGLLLL LLKAAQLYLH RQWLLRALQQ FPCPPFHWLL
     GHSREFQNDQ ELERIQKWVE KFPGACPWWL SGNKARLLVY DPDYLKVILG RSDPKAPRNY
     KLMTPWIGYG LLLLDGQTWF QHRRMLTPAF HYDILKPYVG LMVDSVQIML DRWEQLISQD
     SSLEIFQHVS LMTLDTIMKC AFSYQGSVQL DRNSHSYIQA INDLNNLVFY RARNVFHQSD
     FLYRLSPEGR LFHRACQLAH EHTDRVIQQR KAQLQQEGEL EKVRRKRRLD FLDVLLFAKM
     ENGSSLSDQD LRAEVDTFMF EGHDTTASGV SWIFYALATH PEHQHRCREE IQGLLGDGAS
     ITWEHLDQMP YTTMCIKEAL RLYPPVPSVT RQLSKPVTFP DGRSLPKGVI LFLSIYGLHY
     NPKVWQNPEV FDPFRFAPDS AYHSHAFLPF SGGARNCIGK QFAMRELKVA VALTLVRFEL
     LPDPTRIPIP IARVVLKSKN GIHLRLRKLH
//