Reviewed, UniProtKB/Swiss-Prot P14580 (CP4A6_RABIT)

Names and origin

Protein names

Recommended name:
    Cytochrome P450 4A6
Alternative name(s):
    CYPIVA6
    Lauric acid omega-hydroxylase
    EC=1.14.15.3
    P450-KA-1

Gene names

Name:

CYP4A6

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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. 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.
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alkane 1-monooxygenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 4	4	Ref.2 Ref.4		PRO_0000003575
	Chain	5 – 510	506	Cytochrome P450 4A6		PRO_0000003576
Sites
	Metal binding	457	1	Iron (heme axial ligand)
	Binding site	321	1	Heme (covalent; via 1 link) By similarity
Experimental info
	Sequence conflict	27	1	L → C Ref.3
	Sequence conflict	380	1	L → M Ref.3
	Sequence conflict	424 – 425	2	VW → CG in AAA31234. Ref.2
	Sequence conflict	434 – 435	2	FP → SR Ref.3
	Sequence conflict	434	1	F → S in AAA31234. Ref.2
	Sequence conflict	476	1	V → L in AAA31234. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P14580-1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: B7A85E1208A2B9E1	FASTA	510	58,300
	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

References

[1]	"Cloning and expression of three rabbit kidney cDNAs encoding lauric acid omega-hydroxylases." Johnson E.F., Walker D.L., Griffin K.J., Clark J.E., Okita R.T., Meurhoff A.S., Masters B.S.S. Biochemistry 29:873-879(1990) [PubMed: 2340280] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"Two forms of omega-hydroxylase toward prostaglandin A and laurate. cDNA cloning and their expression." Yokotani N., Bernhardt R., Sogawa K., Kusunose E., Gotoh O., Kusunose M., Fujii-Kuriyama Y. J. Biol. Chem. 264:21665-21669(1989) [PubMed: 2600085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-24. Tissue: Kidney.
[3]	"Characterization of a rabbit gene encoding a clofibrate-inducible fatty acid omega-hydroxylase: CYP4A6." Muerhoff A.S., Griffin K.J., Johnson E.F. Arch. Biochem. Biophys. 296:66-72(1992) [PubMed: 1605646] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Purification and characterization of two forms of cytochrome P-450 with omega-hydroxylase activities toward prostaglandin A and fatty acids from rabbit liver microsomes." Kikuta Y., Kusunose E., Okumoto T., Kubota I., Kusunose M. J. Biochem. 107:280-286(1990) [PubMed: 2361958] [Abstract] Cited for: PROTEIN SEQUENCE OF 5-24.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M28656 mRNA. Translation: AAA31230.1. M29531 mRNA. Translation: AAA31234.1.
PIR	A34160.
3D structure databases
HSSP	HSSP built from PDB template 1JPZ based on UniProtKB P14779.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P14580.
Enzyme and pathway databases
BRENDA	1.14.15.3. 255.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CP4A6_RABIT

Accession

Primary (citable) accession number: P14580

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)