[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-269. TISSUE=Leukocyte; PubMed=8486631 [NCBI, ExPASy, EBI, Israel, Japan] Kikuta Y., Kusunose E., Endo K., Yamamoto S., Sogawa K., Fujii-Kuriyama Y., Kusunose M.; "A novel form of cytochrome P-450 family 4 in human polymorphonuclear leukocytes. cDNA cloning and expression of leukotriene B4 omega-hydroxylase."; J. Biol. Chem. 268:9376-9380(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ASP-269. PubMed=9539102 [NCBI, ExPASy, EBI, Israel, Japan] Kikuta Y., Kato M., Yamashita Y., Miyauchi Y., Tanaka K., Kamada N., Kusunose M.; "Human leukotriene B4 omega-hydroxylase (CYP4F3) gene: molecular cloning and chromosomal localization."; DNA Cell Biol. 17:221-230(1998).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Fetal liver; Peng X., Morgan K., Morgan T.R.; "A novel form of cytochrome P-450 family 4 in human fetal liver."; Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-269; ILE-270 AND THR-271. SeattleSNPs program for genomic applications; Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. This enzyme requires molecular oxygen and NADPH for the omega-hydroxylation of LTB4, a potent chemoattractant for polymorphonuclear leukocytes.
CATALYTIC ACTIVITY: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + NADPH + O₂ = (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + NADP⁺ + H₂O.
COFACTOR: Heme group (By similarity).
ENZYME REGULATION: Inhibited by carbon monoxide (CO).
PATHWAY: Lipid metabolism; leukotriene B4 degradation .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein (By similarity). Microsome membrane; Single-pass membrane protein (By similarity).
TISSUE SPECIFICITY: Expressed in the polymorphonuclear leukocytes as well as leukocytes.
SIMILARITY: Belongs to the cytochrome P450 family.
SEQUENCE CAUTION:
- Sequence=AAC08589.1; Type=Frameshift; Positions=67, 114;
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cyp4f3/";.

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

D12620; BAA02144.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D12621; BAA02145.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB002454; BAA25990.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB002461; BAA25991.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF054821; AAC08589.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY792513; AAV40834.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A46661; A46661.

NP_000887.2; -.

3D structure databases

HSSP

P14779; 1JME. [HSSP ENTRY / PDB]

ModBase

Q08477.

Organism-specific databases

GC19P015612; -.

HIX0058774; -.

HGNC:2646; CYP4F3.

601270; gene. [NCBI / EBI]

PharmGKB

PA234; -.

GeneCards

Q08477.

Gene expression databases

ArrayExpress

Q08477; -.

CleanEx

HS_CYP4F3; -.

GermOnline

ENSG00000186529; Homo sapiens.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0050051;	Molecular function: leukotriene-B4 20-monooxygenase activity (inferred from electronic annotation from EC).
GO:0006691;	Biological process: leukotriene metabolic process (traceable author statement from ProtInc).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

Proteomics databases

PRIDE

Q08477; -.

Genome annotation databases

Ensembl

ENSG00000186529; Homo sapiens. [Contig view]

GeneID

4051; -.

KEGG

hsa:4051; -.

NMPDR

fig|9606.3.peg.15898; -.

Phylogenomic databases

HOGENOM

Q08477; -.

HOVERGEN

Q08477; -.

Other

LinkHub

Q08477; -.

NextBio

15870; -.

SOURCE

CYP4F3; Homo sapiens.

ProtoNet

Q08477.

UniRef

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

Keywords

Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase; Polymorphism; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 520`	`520`	`Cytochrome P450 4F3.`	`PRO_0000051851`
`TRANSMEM`	`11 31`	`21`	`Potential.`
`METAL`	`468 468`		`Iron (heme axial ligand) (By similarity).`
`BINDING`	`328 328`		`Heme (covalent; via 1 link) (By similarity).`
`VARIANT`	`96 96`	`1`	`H -> Q (in dbSNP:rs34923393 [NCBI]).`	`VAR_048457`
`VARIANT`	`106 106`	`1`	`Y -> C (in dbSNP:rs35888783 [NCBI]).`	`VAR_048458`
`VARIANT`	`269 269`	`1`	`A -> D (in dbSNP:rs1805040 [NCBI]).`	`VAR_001258`
`VARIANT`	`270 270`	`1`	`V -> I.`	`VAR_020664`
`VARIANT`	`271 271`	`1`	`I -> T.`	`VAR_020665`
`CONFLICT`	`184 186`		`EGS -> KGY (in Ref. 3; AAC08589).`
`CONFLICT`	`488 488`		`R -> A (in Ref. 1 and 2).`
`CONFLICT`	`512 512`		`L -> I (in Ref. 3; AAC08589).`

Sequence information

Length: 520 AA [This is the length of the unprocessed precursor]

Molecular weight: 59847 Da [This is the MW of the unprocessed precursor]

CRC64: 2519D875280CF9DC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPQLSLSSLG LWPMAASPWL LLLLVGASWL LARILAWTYT FYDNCCRLRC FPQPPKRNWF 

        70         80         90        100        110        120 
LGHLGLIHSS EEGLLYTQSL ACTFGDMCCW WVGPWHAIVR IFHPTYIKPV LFAPAAIVPK 

       130        140        150        160        170        180 
DKVFYSFLKP WLGDGLLLSA GEKWSRHRRM LTPAFHFNIL KPYMKIFNES VNIMHAKWQL 

       190        200        210        220        230        240 
LASEGSARLD MFEHISLMTL DSLQKCVFSF DSHCQEKPSE YIAAILELSA LVTKRHQQIL 

       250        260        270        280        290        300 
LYIDFLYYLT PDGQRFRRAC RLVHDFTDAV IQERRRTLPS QGVDDFLQAK AKSKTLDFID 

       310        320        330        340        350        360 
VLLLSKDEDG KKLSDEDIRA EADTFMFEGH DTTASGLSWV LYHLAKHPEY QERCRQEVQE 

       370        380        390        400        410        420 
LLKDREPKEI EWDDLAQLPF LTMCIKESLR LHPPVPAVSR CCTQDIVLPD GRVIPKGIIC 

       430        440        450        460        470        480 
LISVFGTHHN PAVWPDPEVY DPFRFDPKNI KERSPLAFIP FSAGPRNCIG QAFAMAEMKV 

       490        500        510        520 
VLGLTLLRFR VLPDHTEPRR KPELVLRAEG GLWLRVEPLS

Q08477 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