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Cytochrome P450 4A2 (CYPIVA2) (Cytochrome P-450 K-2) (Cytochrome P450 K-5) (Cytochrome P450-LA-omega 2) (Lauric acid omega-hydroxylase) (Long-chain fatty acid omega-monooxygenase) (EC 1.14.13.205)

 CP4A2_RAT               Reviewed;         504 AA.
P20816; Q4G071;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 2.
28-MAR-2018, entry version 149.
RecName: Full=Cytochrome P450 4A2;
AltName: Full=CYPIVA2;
AltName: Full=Cytochrome P-450 K-2;
AltName: Full=Cytochrome P450 K-5;
AltName: Full=Cytochrome P450-LA-omega 2;
AltName: Full=Lauric acid omega-hydroxylase;
AltName: Full=Long-chain fatty acid omega-monooxygenase;
EC=1.14.13.205;
Flags: Precursor;
Name=Cyp4a2; Synonyms=Cyp4a-2, Cyp4a11;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=2766932; DOI=10.1089/dna.1.1989.8.503;
Kimura S., Hanioka N., Matsunaga E., Gonzalez F.J.;
"The rat clofibrate-inducible CYP4A gene subfamily. I. Complete intron
and exon sequence of the CYP4A1 and CYP4A2 genes, unique exon
organization, and identification of a conserved 19-bp upstream
element.";
DNA 8:503-516(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 5-34, FUNCTION, AND CATALYTIC ACTIVITY.
TISSUE=Kidney;
PubMed=1739747; DOI=10.1016/0005-2760(92)90106-6;
Kawashima H., Kusunose E., Kubota I., Maekawa M., Kusunose M.;
"Purification and NH2-terminal amino acid sequences of human and rat
kidney fatty acid omega-hydroxylases.";
Biochim. Biophys. Acta 1123:156-162(1992).
[4]
PROTEIN SEQUENCE OF 5-19.
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=2306108; DOI=10.1016/0003-9861(90)90747-M;
Imaoka S., Nagashima K., Funae Y.;
"Characterization of three cytochrome P450s purified from renal
microsomes of untreated male rats and comparison with human renal
cytochrome P450.";
Arch. Biochem. Biophys. 276:473-480(1990).
[5]
COVALENT HEME ATTACHMENT.
PubMed=11139583; DOI=10.1074/jbc.M009969200;
Hoch U., Ortiz de Montellano P.R.;
"Covalently linked heme in cytochrome P4504A fatty acid
hydroxylases.";
J. Biol. Chem. 276:11339-11346(2001).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Catalyzes the omega- and (omega-1)-hydroxylation of
various fatty acids such as laurate, myristate and palmitate. Has
little activity toward prostaglandins A1 and E1. Oxidizes
arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE).
{ECO:0000269|PubMed:1739747}.
-!- CATALYTIC ACTIVITY: A long-chain fatty acid + NADPH + O(2) = an
omega-hydroxy-long-chain fatty acid + NADP(+) + H(2)O.
{ECO:0000269|PubMed:1739747}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:11139583};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane; Peripheral membrane protein.
-!- INDUCTION: By clofibrate.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M57719; AAA41039.1; -; Genomic_DNA.
EMBL; BC078684; AAH78684.1; -; mRNA.
EMBL; BC098705; AAH98705.1; -; mRNA.
PIR; A32965; A32965.
PIR; PC4350; PC4350.
RefSeq; NP_001038235.1; NM_001044770.2.
RefSeq; XP_017448632.1; XM_017593143.1.
UniGene; Rn.214991; -.
ProteinModelPortal; P20816; -.
SMR; P20816; -.
STRING; 10116.ENSRNOP00000042072; -.
SwissLipids; SLP:000000743; -.
iPTMnet; P20816; -.
PaxDb; P20816; -.
PRIDE; P20816; -.
Ensembl; ENSRNOT00000051252; ENSRNOP00000042072; ENSRNOG00000030154.
Ensembl; ENSRNOT00000083686; ENSRNOP00000072485; ENSRNOG00000030154.
Ensembl; ENSRNOT00000088209; ENSRNOP00000074484; ENSRNOG00000030154.
GeneID; 24306; -.
KEGG; rno:24306; -.
CTD; 24306; -.
RGD; 2479; Cyp4a2.
eggNOG; KOG0157; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00900000140829; -.
HOVERGEN; HBG000182; -.
InParanoid; P20816; -.
KO; K07425; -.
OMA; LLCRETY; -.
Reactome; R-RNO-211935; Fatty acids.
Reactome; R-RNO-211958; Miscellaneous substrates.
Reactome; R-RNO-211979; Eicosanoids.
Reactome; R-RNO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-RNO-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
PRO; PR:P20816; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000030154; -.
Genevisible; P20816; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0018685; F:alkane 1-monooxygenase activity; IMP:RGD.
GO; GO:0008405; F:arachidonic acid 11,12-epoxygenase activity; TAS:RGD.
GO; GO:0050544; F:arachidonic acid binding; IDA:RGD.
GO; GO:0008391; F:arachidonic acid monooxygenase activity; IMP:RGD.
GO; GO:0005504; F:fatty acid binding; IDA:RGD.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0019369; P:arachidonic acid metabolic process; IMP:RGD.
GO; GO:0046456; P:icosanoid biosynthetic process; IMP:RGD.
GO; GO:0001822; P:kidney development; IEP:RGD.
GO; GO:0048252; P:lauric acid metabolic process; IDA:RGD.
GO; GO:0043651; P:linoleic acid metabolic process; IDA:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; NADP;
Oxidoreductase; Phosphoprotein; Reference proteome.
PROPEP 1 4 {ECO:0000269|PubMed:1739747,
ECO:0000269|PubMed:2306108}.
/FTId=PRO_0000003567.
CHAIN 5 504 Cytochrome P450 4A2.
/FTId=PRO_0000003568.
METAL 451 451 Iron (heme axial ligand).
{ECO:0000269|PubMed:11139583}.
BINDING 315 315 Heme (covalent; via 1 link).
{ECO:0000269|PubMed:11139583}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
SEQUENCE 504 AA; 57969 MW; 8A795DD454125287 CRC64;
MGFSVFSPTR SLDGVSGFFQ GAFLLSLFLV LFKAVQFYLR RQWLLKALEK FPSTPSHWLW
GHNLKDREFQ QVLTWVEKFP GACLQWLSGS TARVLLYDPD YVKVVLGRSD PKPYQSLAPW
IGYGLLLLNG KKWFQHRRML TPAFHYDILK PYVKIMADSV SIMLDKWEKL DDQDHPLEIF
HYVSLMTLDT VMKCAFSHQG SVQLDVNSRS YTKAVEDLNN LIFFRVRSAF YGNSIIYNMS
SDGRLSRRAC QIAHEHTDGV IKTRKAQLQN EEELQKARKK RHLDFLDILL FAKMEDGKSL
SDEDLRAEVD TFMFEGHDTT ASGISWVFYA LATHPEHQER CREEVQSILG DGTSVTWDHL
DQMPYTTMCI KEALRLYSPV PSVSRELSSP VTFPDGRSIP KGIRVTILIY GLHHNPSYWP
NPKVFDPSRF SPDSPRHSHA YLPFSGGARN CIGKQFAMNE LKVAVALTLL RFELLPDPTR
IPVPMPRLVL KSKNGIHLRL KKLR


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