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Cytochrome P450 4A6 (CYPIVA6) (Cytochrome P450-KA-1) (Lauric acid omega-hydroxylase) (Long-chain fatty acid omega-monooxygenase) (EC 1.14.13.205)

 CP4A6_RABIT             Reviewed;         510 AA.
P14580;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
25-OCT-2017, entry version 123.
RecName: Full=Cytochrome P450 4A6;
AltName: Full=CYPIVA6;
AltName: Full=Cytochrome P450-KA-1;
AltName: Full=Lauric acid omega-hydroxylase;
AltName: Full=Long-chain fatty acid omega-monooxygenase;
EC=1.14.13.205;
Flags: Precursor;
Name=CYP4A6;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=2340280; DOI=10.1021/bi00456a004;
Johnson E.F., Walker D.L., Griffin K.J., Clark J.E., Okita R.T.,
Meurhoff A.S., Masters B.S.S.;
"Cloning and expression of three rabbit kidney cDNAs encoding lauric
acid omega-hydroxylases.";
Biochemistry 29:873-879(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 5-24.
TISSUE=Kidney;
PubMed=2600085;
Yokotani N., Bernhardt R., Sogawa K., Kusunose E., Gotoh O.,
Kusunose M., Fujii-Kuriyama Y.;
"Two forms of omega-hydroxylase toward prostaglandin A and laurate.
cDNA cloning and their expression.";
J. Biol. Chem. 264:21665-21669(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1605646; DOI=10.1016/0003-9861(92)90545-8;
Muerhoff A.S., Griffin K.J., Johnson E.F.;
"Characterization of a rabbit gene encoding a clofibrate-inducible
fatty acid omega-hydroxylase: CYP4A6.";
Arch. Biochem. Biophys. 296:66-72(1992).
[4]
PROTEIN SEQUENCE OF 5-24.
PubMed=2361958;
Kikuta Y., Kusunose E., Okumoto T., Kubota I., Kusunose M.;
"Purification and characterization of two forms of cytochrome P-450
with omega-hydroxylase activities toward prostaglandin A and fatty
acids from rabbit liver microsomes.";
J. Biochem. 107:280-286(1990).
-!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
monooxygenases. In liver microsomes, this enzyme is involved in an
NADPH-dependent electron transport pathway. It oxidizes a variety
of structurally unrelated compounds, including steroids, fatty
acids, and xenobiotics.
-!- FUNCTION: The kidney P-450 system is rather specialized for the
omega-hydroxylation of fatty acids. Both P450-KA1 and P450-KA2
catalyze the omega- and (omega-1)-hydroxylation of various fatty
acids with no drug-metabolizing activity, and hydroxylate
prostaglandin A1 and A2 solely at the omega-position.
-!- CATALYTIC ACTIVITY: A long-chain fatty acid + NADPH + O(2) = an
omega-hydroxy-long-chain fatty acid + NADP(+) + H(2)O.
{ECO:0000250|UniProtKB:Q02928}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:P51869};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane; Peripheral membrane protein.
-!- TISSUE SPECIFICITY: Liver; kidney.
-!- INDUCTION: P450 can be induced to high levels in liver and other
tissues by various foreign compounds, including drugs, pesticides,
and carcinogens.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; M28656; AAA31230.1; -; mRNA.
EMBL; M29531; AAA31234.1; -; mRNA.
PIR; A34160; A34160.
RefSeq; NP_001164542.1; NM_001171071.1.
RefSeq; NP_001164599.1; NM_001171128.1.
UniGene; Ocu.1861; -.
UniGene; Ocu.7478; -.
ProteinModelPortal; P14580; -.
SMR; P14580; -.
STRING; 9986.ENSOCUP00000004037; -.
GeneID; 100328612; -.
GeneID; 100328946; -.
KEGG; ocu:100328612; -.
KEGG; ocu:100328946; -.
CTD; 100328946; -.
eggNOG; KOG0157; Eukaryota.
eggNOG; COG2124; LUCA.
HOGENOM; HOG000233833; -.
HOVERGEN; HBG000182; -.
InParanoid; P14580; -.
KO; K17687; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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; Reference proteome.
PROPEP 1 4 {ECO:0000269|PubMed:2361958,
ECO:0000269|PubMed:2600085}.
/FTId=PRO_0000003575.
CHAIN 5 510 Cytochrome P450 4A6.
/FTId=PRO_0000003576.
METAL 457 457 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P51869}.
BINDING 321 321 Heme (covalent; via 1 link).
{ECO:0000250|UniProtKB:P51869}.
CONFLICT 27 27 L -> C (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
CONFLICT 380 380 L -> M (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
CONFLICT 424 425 VW -> CG (in Ref. 2; AAA31234).
{ECO:0000305}.
CONFLICT 434 435 FP -> SR (in Ref. 3; no nucleotide
entry). {ECO:0000305}.
CONFLICT 434 434 F -> S (in Ref. 2; AAA31234).
{ECO:0000305}.
CONFLICT 476 476 V -> L (in Ref. 2; AAA31234).
{ECO:0000305}.
SEQUENCE 510 AA; 58300 MW; B7A85E1208A2B9E1 CRC64;
MSVSALNPTR LPGSLSGLLQ VAGLLGLLLL LLKAAQLYLH RQWLLRALQQ FPCPPFHWLL
GHSREFQNGH ELQVMLKWVE KFPSACPRWL WGSRAHLLIY DPDYMKVILG RSDPKAQGSY
RFLAPWIGYG LLLLNGQTWF QHRRMLTPAF HYDILKPYVG LMADSVQIML DKWEQLVSQD
SSLEVFQDIS LMTLDTIMKC AFSHQGSVQL DRNSQSYIQA VGDLNNLFFS RVRNVFHQSD
TIYRLSPEGR LSHRACQLAH EHTDRVIQQR KAQLQQEGEL EKVRRKRRLD FLDVLLFAKM
ENGSSLSDQD LRAEVDTFMF EGHDTTASGI SWIFYALATH PEHQHRCREE IQGLLGDGAS
ITWEHLDQMP YTTMCIKEAL RLYPPVPGVG RQLSSPVTFP DGRSLPKGVI VTLSIYALHH
NPKVWPNPEV FDPFPFAPGS ARHSHAFLPF SGGPRNCIGK QFAMNELKVA VALTLVRFEL
LPDPKRVPDQ KPRLVLKSSN GIHLRLRKLR


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