ID   CP4AA_RAT               Reviewed;         509 AA.
AC   P08516; Q5EBD8;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   16-JUN-2009, entry version 94.
DE   RecName: Full=Cytochrome P450 4A10;
DE   AltName: Full=CYPIVA10;
DE   AltName: Full=Lauric acid omega-hydroxylase;
DE            EC=1.14.15.3;
DE   AltName: Full=P450-LA-omega 1;
DE   AltName: Full=P452;
GN   Name=Cyp4a10; Synonyms=Cyp4a-1, Cyp4a1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=87109183; PubMed=3027069;
RA   Hardwick J.P., Song B.-J., Huberman E., Gonzalez F.J.;
RT   "Isolation, complementary DNA sequence, and regulation of rat hepatic
RT   lauric acid omega-hydroxylase (cytochrome P-450LA omega).
RT   Identification of a new cytochrome P-450 gene family.";
RL   J. Biol. Chem. 262:801-810(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Liver;
RX   MEDLINE=88312998; PubMed=3410047; DOI=10.1016/0014-5793(88)80055-3;
RA   Earnshaw D., Dale J.W., Goldfarb P.S., Gibson G.G.;
RT   "Differential splicing in the 3' non-coding region of rat cytochrome
RT   P-452 (P450 IVA1) mRNA.";
RL   FEBS Lett. 236:357-361(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   MEDLINE=89356271; PubMed=2766932;
RA   Kimura S., Hanioka N., Matsunaga E., Gonzalez F.J.;
RT   "The rat clofibrate-inducible CYP4A gene subfamily. I. Complete intron
RT   and exon sequence of the CYP4A1 and CYP4A2 genes, unique exon
RT   organization, and identification of a conserved 19-bp upstream
RT   element.";
RL   DNA 8:503-516(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-22.
RX   MEDLINE=92231570; PubMed=1567203; DOI=10.1016/0003-9861(92)90714-8;
RA   Okita R.T., Okita J.R.;
RT   "Characterization of a cytochrome P450 from di(2-ethylhexyl)
RT   phthalate-treated rats which hydroxylates fatty acids.";
RL   Arch. Biochem. Biophys. 294:475-481(1992).
RN   [6]
RP   COVALENT HEME ATTACHMENT.
RX   MEDLINE=21179192; PubMed=11139583; DOI=10.1074/jbc.M009969200;
RA   Hoch U., Ortiz de Montellano P.R.;
RT   "Covalently linked heme in cytochrome P4504A fatty acid
RT   hydroxylases.";
RL   J. Biol. Chem. 276:11339-11346(2001).
RN   [7]
RP   COVALENT HEME ATTACHMENT, AND MUTAGENESIS OF GLU-320.
RX   MEDLINE=21935389; PubMed=11821421; DOI=10.1074/jbc.M112155200;
RA   LeBrun L.A., Hoch U., Ortiz de Montellano P.R.;
RT   "Autocatalytic mechanism and consequences of covalent heme attachment
RT   in the cytochrome P4504A family.";
RL   J. Biol. Chem. 277:12755-12761(2002).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
CC       monooxygenases. In liver microsomes, this enzyme is involved in an
CC       NADPH-dependent electron transport pathway. It oxidizes a variety
CC       of structurally unrelated compounds, including steroids, fatty
CC       acids, and xenobiotics.
CC   -!- CATALYTIC ACTIVITY: Octane + reduced rubredoxin + O(2) = 1-octanol
CC       + oxidized rubredoxin + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- INDUCTION: By clofibrate.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; M14972; AAA41061.1; -; mRNA.
DR   EMBL; X07259; CAA30245.1; -; mRNA.
DR   EMBL; M57718; AAA41038.1; -; Genomic_DNA.
DR   EMBL; BC089761; AAH89761.1; -; mRNA.
DR   IPI; IPI00327623; -.
DR   PIR; S01336; O4RTLO.
DR   RefSeq; NP_695219.1; -.
DR   RefSeq; NP_787031.1; -.
DR   UniGene; Rn.92401; -.
DR   HSSP; P14779; 1JPZ.
DR   PRIDE; P08516; -.
DR   Ensembl; ENSRNOG00000009597; Rattus norvegicus.
DR   GeneID; 170544; -.
DR   GeneID; 50549; -.
DR   KEGG; rno:170544; -.
DR   KEGG; rno:50549; -.
DR   RGD; 68945; Cyp4a1.
DR   HOVERGEN; P08516; -.
DR   BRENDA; 1.14.15.3; 248.
DR   NextBio; 621028; -.
DR   ArrayExpress; P08516; -.
DR   GermOnline; ENSRNOG00000009597; Rattus norvegicus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IDA:RGD.
DR   GO; GO:0018685; F:alkane 1-monooxygenase activity; IEA:EC.
DR   GO; GO:0008391; F:arachidonic acid monooxygenase activity; IDA:RGD.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0008393; F:fatty acid (omega-1)-hydroxylase activity; IMP:RGD.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IMP:RGD.
DR   GO; GO:0046456; P:icosanoid biosynthetic process; IMP:RGD.
DR   GO; GO:0001822; P:kidney development; IEP:RGD.
DR   GO; GO:0048252; P:lauric acid metabolic process; IDA:RGD.
DR   GO; GO:0043651; P:linoleic acid metabolic process; IDA:RGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0001890; P:placenta development; IEP:RGD.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Heme; Iron;
KW   Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase.
FT   CHAIN         1    509       Cytochrome P450 4A10.
FT                                /FTId=PRO_0000051816.
FT   METAL       456    456       Iron (heme axial ligand).
FT   BINDING     320    320       Heme (covalent; via 1 link).
FT   MUTAGEN     320    320       E->A: Loss of heme binding.
FT   CONFLICT    341    341       E -> K (in Ref. 1; AAA41061 and 2;
FT                                CAA30245).
SQ   SEQUENCE   509 AA;  58215 MW;  E622FAB351BC40AF CRC64;
     MSVSALSSTR FTGSISGFLQ VASVLGLLLL LVKAVQFYLQ RQWLLKAFQQ FPSPPFHWFF
     GHKQFQGDKE LQQIMTCVEN FPSAFPRWFW GSKAYLIVYD PDYMKVILGR SDPKANGVYR
     LLAPWIGYGL LLLNGQPWFQ HRRMLTPAFH YDILKPYVKN MADSIRLMLD KWEQLAGQDS
     SIEIFQHISL MTLDTVMKCA FSHNGSVQVD GNYKSYIQAI GNLNDLFHSR VRNIFHQNDT
     IYNFSSNGHL FNRACQLAHD HTDGVIKLRK DQLQNAGELE KVKKKRRLDF LDILLLARME
     NGDSLSDKDL RAEVDTFMFE GHDTTASGVS WIFYALATHP EHQQRCREEV QSVLGDGSSI
     TWDHLDQIPY TTMCIKEALR LYPPVPGIVR ELSTSVTFPD GRSLPKGIQV TLSIYGLHHN
     PKVWPNPEVF DPSRFAPDSP RHSHSFLPFS GGARNCIGKQ FAMSEMKVIV ALTLLRFELL
     PDPTKVPIPL PRLVLKSKNG IYLYLKKLH
//