Reviewed, UniProtKB/Swiss-Prot P14581 (CP4A7_RABIT)

Names and origin

Protein names

Recommended name:
    Cytochrome P450 4A7
Alternative name(s):
    CYPIVA7
    Lauric acid omega-hydroxylase
    EC=1.14.15.3
    P450-KA-2

Gene names

Name:

CYP4A7

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	511 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, small intestine.
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.3		PRO_0000003577
	Chain	5 – 511	507	Cytochrome P450 4A7		PRO_0000003578
Sites
	Metal binding	458	1	Iron (heme axial ligand)
	Binding site	322	1	Heme (covalent; via 1 link) By similarity
Experimental info
	Sequence conflict	99	1	C → V in AAA31233. Ref.2
	Sequence conflict	150	1	F → S in AAA31233. Ref.2
	Sequence conflict	392 – 393	2	SK → RQ in AAA31233. Ref.2
	Sequence conflict	477	1	V → L in AAA31233. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P14581-1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 21FD8215D26A4451	FASTA	511	58,319
	10 20 30 40 50 60 MSVSALSSTR LPGSFSGFLQ AAALLGLLLL LLKAAQLYLR RQWLLRALQQ FPCPPSHWLL 70 80 90 100 110 120 GHSREFPIDS ELQQVLKRVE KFPSACPRWL WGSELFLICY DPDYMKTILG RSDPKARVSY 130 140 150 160 170 180 SFLAPWIGYG LLLLEGQTWF QHRRMLTPAF HYDILKPYVG LMVDSVQVML DKLEKLARKD 190 200 210 220 230 240 APLEIYEHVS LMTLETIMKC AFSHQGSVQL ESRTSKSYIQ AVRELSDLAL QRVRNVFHQS 250 260 270 280 290 300 DFLYRLSPEG RLSHRACQLA HEHTDRVIQQ RKAQLQQEGE LEKVRRKRRL DFLDVLLFAK 310 320 330 340 350 360 MENGSSLSDQ DLRAEVDTFM FEGHDTTASG ISWIFYALAT HPEHQHRCRE EIQGLLGDGA 370 380 390 400 410 420 SITWEHLDKM PYTTMCIKEA LRLYPPVPGV GSKLSSPVTF PDGRSLPKGI IITLSIYGLH 430 440 450 460 470 480 HNPKVWPNPE VFDPSRFAPG SARHSHAFLP FSGGSRNCIG KQFAMNELKV AVALTLVRFE 490 500 510 LLPDPTRVPI PITRLVLKSK NGIHLRLRKL H

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]	"Purification and characterization of two forms of fatty acid omega-hydroxylase cytochrome P-450 from rabbit kidney cortex microsomes." Yoshimura R., Kusunose E., Yokotani N., Yamamoto S., Kubota I., Kusunose M. J. Biochem. 108:544-548(1990) [PubMed: 2127276] [Abstract] Cited for: PROTEIN SEQUENCE OF 5-24. Tissue: Kidney.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M28657 mRNA. Translation: AAA31231.1. M29530 mRNA. Translation: AAA31233.1.
PIR	B34160.
3D structure databases
HSSP	HSSP built from PDB template 1JPZ based on UniProtKB P14779.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P14581.
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

CP4A7_RABIT

Accession

Primary (citable) accession number: P14581

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)