CP4A5_RABIT
ID CP4A5_RABIT Reviewed; 511 AA.
AC P14579;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cytochrome P450 4A5;
DE AltName: Full=CYPIVA5;
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=CYP4A5;
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].
RC TISSUE=Kidney;
RX PubMed=2013275; DOI=10.1111/j.1432-1033.1991.tb15846.x;
RA Yokotani N., Kusunose E., Sogawa K., Kawashima H., Kinosaki M.,
RA Kusunose M., Fujii-Kuriyama Y.;
RT "cDNA cloning and expression of the mRNA for cytochrome P-450kd which shows
RT a fatty acid omega-hydroxylating activity.";
RL Eur. J. Biochem. 196:531-536(1991).
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 -!- 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; 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}.
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DR EMBL; M28655; AAA31229.1; -; mRNA.
DR EMBL; X57209; CAA40493.1; -; mRNA.
DR PIR; A34260; A34260.
DR RefSeq; NP_001164448.1; NM_001170977.1.
DR AlphaFoldDB; P14579; -.
DR SMR; P14579; -.
DR PRIDE; P14579; -.
DR GeneID; 100328576; -.
DR KEGG; ocu:100328576; -.
DR CTD; 100328576; -.
DR InParanoid; P14579; -.
DR OrthoDB; 1247045at2759; -.
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: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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT PROPEP 1..4
FT /evidence="ECO:0000305"
FT /id="PRO_0000003573"
FT CHAIN 5..511
FT /note="Cytochrome P450 4A5"
FT /id="PRO_0000003574"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
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 435
FT /note="G -> S (in Ref. 2; CAA40493)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="V -> L (in Ref. 2; CAA40493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 58357 MW; 11D174BFC8BFA268 CRC64;
MSVSALSPTR LPGSLSGLLQ VAALLGLLLL LLKAAQLYLR RQWLLRALQQ FPCPPFHWLL
GHSREFQMNQ ELQQILKWVE KFPRACPHWI GGNKVRVQLY DPDYMKVILG RSDPKSRGSY
TFVAPWIGYG LLLLNGQPWF QHRRMLTPAF HYDILKPYVG LMVDSVQIML DKWEQLVSQD
SSLEVFQDIS LMTLDTIMKC AFSYQGSVQL DSRNSQSYIQ AVGDLNNLVF ARVRNIFHQS
DTIYRLSPEG RLSHRACQLA HEHTDRVIQQ RKAQLQQEGE LEKVRRKRRL DFLDVLLFAK
MENGSSLSDQ DLRAEVDTFM FEGHDTTASG VSWIFYALAT HPEHQHRCRE EIQGLLGDGA
SITWEHLDQM PYTTMCIKEA MRLYPPVPAI SRDLSSPVTF PDGRSLPKGF TVTLSIYGLH
HNPNVWPNPE VFDPGRFTPG SARHSHAFLP FSGGARNCIG KQFAMNELKV AVALTLVRFE
LLPDPTRIPK PTARLVLKSN NGIHLRLRKL Q
