CP4A4_RABIT
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-AUG-2022, entry version 132.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; 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
