[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Kidney; DOI=10.1021/bi00456a004; PubMed=2340280 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1016/0003-9861(92)90545-8; PubMed=1605646 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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: Octane + reduced rubredoxin + O₂ = 1-octanol + oxidized rubredoxin + H₂O.
COFACTOR: Heme group (By similarity).
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.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M28656; AAA31230.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M29531; AAA31234.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A34160; A34160.

3D structure databases

HSSP

P14779; 1JPZ. [HSSP ENTRY / PDB]

ModBase

P14580.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

BLOCKS

P14580.

Phylogenomic databases

HOVERGEN

P14580; -.

Other

ProtoNet

P14580.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 4`	`4`		`PRO_0000003575`
`CHAIN`	`5 510`	`506`	`Cytochrome P450 4A6.`	`PRO_0000003576`
`METAL`	`457 457`		`Iron (heme axial ligand).`
`BINDING`	`321 321`		`Heme (covalent; via 1 link) (By similarity).`
`CONFLICT`	`27 27`		`L -> C (in Ref. 3).`
`CONFLICT`	`380 380`		`L -> M (in Ref. 3).`
`CONFLICT`	`424 425`		`VW -> CG (in Ref. 2; AAA31234).`
`CONFLICT`	`434 435`		`FP -> SR (in Ref. 3).`
`CONFLICT`	`434 434`		`F -> S (in Ref. 2; AAA31234).`
`CONFLICT`	`476 476`		`V -> L (in Ref. 2; AAA31234).`

Sequence information

Length: 510 AA [This is the length of the unprocessed precursor]

Molecular weight: 58300 Da [This is the MW of the unprocessed precursor]

CRC64: B7A85E1208A2B9E1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVSALNPTR LPGSLSGLLQ VAGLLGLLLL LLKAAQLYLH RQWLLRALQQ FPCPPFHWLL 

        70         80         90        100        110        120 
GHSREFQNGH ELQVMLKWVE KFPSACPRWL WGSRAHLLIY DPDYMKVILG RSDPKAQGSY 

       130        140        150        160        170        180 
RFLAPWIGYG LLLLNGQTWF QHRRMLTPAF HYDILKPYVG LMADSVQIML DKWEQLVSQD 

       190        200        210        220        230        240 
SSLEVFQDIS LMTLDTIMKC AFSHQGSVQL DRNSQSYIQA VGDLNNLFFS RVRNVFHQSD 

       250        260        270        280        290        300 
TIYRLSPEGR LSHRACQLAH EHTDRVIQQR KAQLQQEGEL EKVRRKRRLD FLDVLLFAKM 

       310        320        330        340        350        360 
ENGSSLSDQD LRAEVDTFMF EGHDTTASGI SWIFYALATH PEHQHRCREE IQGLLGDGAS 

       370        380        390        400        410        420 
ITWEHLDQMP YTTMCIKEAL RLYPPVPGVG RQLSSPVTFP DGRSLPKGVI VTLSIYALHH 

       430        440        450        460        470        480 
NPKVWPNPEV FDPFPFAPGS ARHSHAFLPF SGGPRNCIGK QFAMNELKVA VALTLVRFEL 

       490        500        510 
LPDPKRVPDQ KPRLVLKSSN GIHLRLRKLR

P14580 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools