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P78329 (CP4F2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leukotriene-B(4) omega-hydroxylase 1

EC=1.14.13.30
Alternative name(s):
CYPIVF2
Cytochrome P450 4F2
Cytochrome P450-LTB-omega
Leukotriene-B(4) 20-monooxygenase 1
Gene names
Name:CYP4F2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.

Tissue specificity

Liver.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityPolymorphism
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Inferred from direct assay PubMed 10660572. Source: UniProtKB

drug metabolic process

Inferred from mutant phenotype PubMed 21084764PubMed 21127708. Source: UniProtKB

epoxygenase P450 pathway

Inferred from direct assay PubMed 20861217PubMed 9618440. Source: UniProtKB

icosanoid metabolic process

Traceable author statement. Source: Reactome

leukotriene B4 catabolic process

Inferred from direct assay Ref.3Ref.1PubMed 9799565. Source: UniProtKB

leukotriene metabolic process

Traceable author statement. Source: Reactome

long-chain fatty acid metabolic process

Inferred from direct assay PubMed 18433732. Source: BHF-UCL

negative regulation of blood coagulation

Inferred from mutant phenotype PubMed 19297518. Source: UniProtKB

negative regulation of icosanoid secretion

Inferred from mutant phenotype PubMed 18391101. Source: UniProtKB

omega-hydroxylase P450 pathway

Traceable author statement. Source: Reactome

oxidation-reduction process

Inferred from direct assay PubMed 20861217PubMed 9618440PubMed 9799565. Source: UniProtKB

positive regulation of icosanoid secretion

Inferred from mutant phenotype PubMed 17341693. Source: UniProtKB

pressure natriuresis

Inferred from expression pattern PubMed 10660572. Source: UniProtKB

regulation of blood pressure

Inferred from mutant phenotype PubMed 18391101. Source: UniProtKB

renal water homeostasis

Inferred from expression pattern PubMed 10660572. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

sodium ion homeostasis

Inferred from expression pattern PubMed 10660572. Source: UniProtKB

very long-chain fatty acid metabolic process

Inferred from direct assay PubMed 18433732. Source: BHF-UCL

vitamin E metabolic process

Inferred from direct assay PubMed 20861217. Source: UniProtKB

vitamin K biosynthetic process

Inferred from mutant phenotype PubMed 19297518. Source: UniProtKB

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 10660572. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 10660572. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement PubMed 20861217. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 10660572PubMed 19297518PubMed 20861217PubMed 9618440PubMed 9799565. Source: UniProtKB

   Molecular_functionalkane 1-monooxygenase activity

Inferred from direct assay PubMed 18433732. Source: BHF-UCL

alpha-tocopherol omega-hydroxylase activity

Inferred from direct assay PubMed 20861217. Source: UniProtKB

arachidonic acid epoxygenase activity

Inferred from direct assay PubMed 20861217PubMed 9618440. Source: UniProtKB

arachidonic acid omega-hydroxylase activity

Inferred from direct assay PubMed 10660572PubMed 9618440. Source: UniProtKB

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

leukotriene-B4 20-monooxygenase activity

Inferred from direct assay Ref.1PubMed 9799565. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17474147. Source: IntAct

tocotrienol omega-hydroxylase activity

Inferred from direct assay PubMed 20861217. Source: UniProtKB

vitamin-K-epoxide reductase (warfarin-sensitive) activity

Inferred from mutant phenotype PubMed 19297518. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-1752413,EBI-389883

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 520520Leukotriene-B(4) omega-hydroxylase 1
PRO_0000051850

Sites

Metal binding4681Iron (heme axial ligand) By similarity
Binding site3281Heme (covalent; via 1 link) By similarity

Natural variations

Natural variant71S → Y. Ref.5
Corresponds to variant rs3093104 [ dbSNP | Ensembl ].
VAR_013116
Natural variant121W → G. Ref.5 Ref.7
Corresponds to variant rs3093105 [ dbSNP | Ensembl ].
VAR_013117
Natural variant1851G → V. Ref.4 Ref.5
Corresponds to variant rs3093153 [ dbSNP | Ensembl ].
VAR_013118
Natural variant2691A → D.
Corresponds to variant rs1805040 [ dbSNP | Ensembl ].
VAR_020125
Natural variant4331V → M. Ref.5 Ref.7
Corresponds to variant rs2108622 [ dbSNP | Ensembl ].
VAR_013119
Natural variant5191L → M. Ref.5
Corresponds to variant rs3093200 [ dbSNP | Ensembl ].
VAR_013120

Experimental info

Sequence conflict12 – 132WP → CR in AAC50052. Ref.2
Sequence conflict12 – 132WP → CR in AAF86378. Ref.8
Sequence conflict251V → A in AAH67437. Ref.7
Sequence conflict1691E → D in AAH67440. Ref.7
Sequence conflict3361G → V in AAC50052. Ref.2
Sequence conflict3911L → V in AAC50052. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P78329 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 1791F9E6EECB59B5

FASTA52059,853
        10         20         30         40         50         60 
MSQLSLSWLG LWPVAASPWL LLLLVGASWL LAHVLAWTYA FYDNCRRLRC FPQPPRRNWF 

        70         80         90        100        110        120 
WGHQGMVNPT EEGMRVLTQL VATYPQGFKV WMGPISPLLS LCHPDIIRSV INASAAIAPK 

       130        140        150        160        170        180 
DKFFYSFLEP WLGDGLLLSA GDKWSRHRRM LTPAFHFNIL KPYMKIFNES VNIMHAKWQL 

       190        200        210        220        230        240 
LASEGSACLD MFEHISLMTL DSLQKCVFSF DSHCQEKPSE YIAAILELSA LVSKRHHEIL 

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

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

       370        380        390        400        410        420 
LLKDREPKEI EWDDLAHLPF LTMCMKESLR LHPPVPVISR HVTQDIVLPD GRVIPKGIIC 

       430        440        450        460        470        480 
LISVFGTHHN PAVWPDPEVY DPFRFDPENI KERSPLAFIP FSAGPRNCIG QTFAMAEMKV 

       490        500        510        520 
VLALTLLRFR VLPDHTEPRR KPELVLRAEG GLWLRVEPLS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a novel form of leukotriene B4 omega-hydroxylase from human liver."
Kikuta Y., Kusunose E., Kondo T., Yamamoto S., Kinoshita H., Kusunose M.
FEBS Lett. 348:70-74(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"The human liver CYP4F2 cDNA sequence and expression in baculovirus-infected insect cells."
Chen L., Hardwick J.P.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Expression and molecular cloning of human liver leukotriene B4 omega-hydroxylase (CYP4F2) gene."
Kikuta Y., Miyauchi Y., Kusunose E., Kusunose M.
DNA Cell Biol. 18:723-730(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-185.
Tissue: Kidney.
[5]SeattleSNPs variation discovery resource
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TYR-7; GLY-12; VAL-185; MET-433 AND MET-519.
[6]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLY-12 AND MET-433.
[8]"Promoter activity and regulation of the CYP4F2 leukotriene B4 omega hydroxylase gene by peroxisomal proliferators and retinoic acid in HepG2 cells."
Zhang X., Chen L., Hardwick J.P.
Arch. Biochem. Biophys. 378:364-376(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-175.
Tissue: Liver.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D26480 mRNA. Translation: BAA05490.1.
U02388 mRNA. Translation: AAC50052.2.
AB015306 Genomic DNA. Translation: BAA75823.1.
AK290790 mRNA. Translation: BAF83479.1.
AF467894 Genomic DNA. Translation: AAL67578.1.
AC005336 Genomic DNA. Translation: AAC27730.1.
BC067437 mRNA. Translation: AAH67437.1.
BC067439 mRNA. Translation: AAH67439.1.
BC067440 mRNA. Translation: AAH67440.1.
AF221943 Genomic DNA. Translation: AAF86378.1.
CCDSCCDS12336.1.
PIRS45702.
RefSeqNP_001073.3. NM_001082.4.
UniGeneHs.558423.

3D structure databases

ProteinModelPortalP78329.
SMRP78329. Positions 71-520.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114099. 3 interactions.
IntActP78329. 5 interactions.
STRING9606.ENSP00000221700.

Chemistry

BindingDBP78329.
ChEMBLCHEMBL3379.

PTM databases

PhosphoSiteP78329.

Polymorphism databases

DMDM6166044.

Proteomic databases

PaxDbP78329.
PRIDEP78329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221700; ENSP00000221700; ENSG00000186115.
GeneID8529.
KEGGhsa:8529.
UCSCuc002nbs.1. human.

Organism-specific databases

CTD8529.
GeneCardsGC19M015988.
HGNCHGNC:2645. CYP4F2.
HPAHPA014048.
HPA017265.
MIM604426. gene.
neXtProtNX_P78329.
Orphanet240997. Susceptibility to bleeding due to warfarine treatment.
240923. Warfarine toxicity.
PharmGKBPA27121.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2124.
HOVERGENHBG000182.
KOK17726.
OMAQGMVNPT.
OrthoDBEOG7CNZFK.
PhylomeDBP78329.
TreeFamTF105088.

Enzyme and pathway databases

BioCycMetaCyc:HS02675-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP78329.
BgeeP78329.
CleanExHS_CYP4F2.
GenevestigatorP78329.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCYP4F2.
GenomeRNAi8529.
NextBio31940.
PROP78329.
SOURCESearch...

Entry information

Entry nameCP4F2_HUMAN
AccessionPrimary (citable) accession number: P78329
Secondary accession number(s): A8K425 expand/collapse secondary AC list , Q16677, Q6NWT4, Q6NWT6, Q9NNZ0, Q9UIU8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM