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Q9HCS2 (CP4FC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome P450 4F12

EC=1.14.14.1
Alternative name(s):
CYPIVF12
Gene names
Name:CYP4F12
ORF Names:UNQ568/PRO1129
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes leukotriene B4 omega-hydroxylation and arachidonic acid omega-hydroxylation but with an activity much lower than that of CYP4F2. Catalyzes the hydroxylation of the antihistamine ebastine.

Catalytic activity

RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.

Cofactor

Heme group By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Microsome membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Expressed in small intestine, liver, colon and heart. Ref.1 Ref.2

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence caution

The sequence EAW84492.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

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

Inferred from sequence or structural similarity. Source: UniProtKB

drug metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

epoxygenase P450 pathway

Inferred from sequence or structural similarity. Source: UniProtKB

leukotriene B4 catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

long-chain fatty acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of blood coagulation

Inferred from sequence or structural similarity. Source: UniProtKB

oxidation-reduction process

Inferred from sequence or structural similarity. Source: UniProtKB

pressure natriuresis

Inferred from sequence or structural similarity. Source: UniProtKB

renal water homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

sodium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

very long-chain fatty acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

vitamin E metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

vitamin K biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionalkane 1-monooxygenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

arachidonic acid epoxygenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

aromatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

leukotriene-B4 20-monooxygenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

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

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 524524Cytochrome P450 4F12
PRO_0000051857

Regions

Transmembrane19 – 3921Helical; Potential
Transmembrane87 – 10721Helical; Potential

Sites

Metal binding4681Iron (heme axial ligand) By similarity

Natural variations

Natural variant131P → L. Ref.2
Corresponds to variant rs16995376 [ dbSNP | Ensembl ].
VAR_013244
Natural variant161T → M. Ref.1 Ref.2 Ref.3
Corresponds to variant rs16995378 [ dbSNP | Ensembl ].
VAR_048459
Natural variant761N → D. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs609636 [ dbSNP | Ensembl ].
VAR_013245
Natural variant901I → V. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs609290 [ dbSNP | Ensembl ].
VAR_013246
Natural variant1881C → R. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs2285888 [ dbSNP | Ensembl ].
VAR_013247
Natural variant5221S → G. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs593818 [ dbSNP | Ensembl ].
VAR_048460

Sequences

Sequence LengthMass (Da)Tools
Q9HCS2 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: F29C29BA8DB880FE

FASTA52460,270
        10         20         30         40         50         60 
MSLLSLPWLG LRPVATSPWL LLLLVVGSWL LARILAWTYA FYNNCRRLQC FPQPPKRNWF 

        70         80         90        100        110        120 
WGHLGLITPT EEGLKNSTQM SATYSQGFTI WLGPIIPFIV LCHPDTIRSI TNASAAIAPK 

       130        140        150        160        170        180 
DNLFIRFLKP WLGEGILLSG GDKWSRHRRM LTPAFHFNIL KSYITIFNKS ANIMLDKWQH 

       190        200        210        220        230        240 
LASEGSSCLD MFEHISLMTL DSLQKCIFSF DSHCQERPSE YIATILELSA LVEKRSQHIL 

       250        260        270        280        290        300 
QHMDFLYYLS HDGRRFHRAC RLVHDFTDAV IRERRRTLPT QGIDDFFKDK AKSKTLDFID 

       310        320        330        340        350        360 
VLLLSKDEDG KALSDEDIRA EADTFMFGGH DTTASGLSWV LYNLARHPEY QERCRQEVQE 

       370        380        390        400        410        420 
LLKDRDPKEI EWDDLAQLPF LTMCVKESLR LHPPAPFISR CCTQDIVLPD GRVIPKGITC 

       430        440        450        460        470        480 
LIDIIGVHHN PTVWPDPEVY DPFRFDPENS KGRSPLAFIP FSAGPRNCIG QAFAMAEMKV 

       490        500        510        520 
VLALMLLHFR FLPDHTEPRR KLELIMRAEG GLWLRVEPLN VSLQ 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and expression of CYP4F12, a novel human cytochrome P450."
Bylund J., Bylund M., Oliw E.H.
Biochem. Biophys. Res. Commun. 280:892-897(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CHARACTERIZATION, VARIANTS MET-16; ASP-76; VAL-90; ARG-188 AND GLY-522.
Tissue: Liver.
[2]"cDNA cloning and expression of a novel cytochrome p450 (cyp4f12) from human small intestine."
Hashizume T., Imaoka S., Hiroi T., Terauchi Y., Fujii T., Miyazaki H., Kamataki T., Funae Y.
Biochem. Biophys. Res. Commun. 280:1135-1141(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CHARACTERIZATION, VARIANTS LEU-13; MET-16; ASP-76; VAL-90; ARG-188 AND GLY-522.
Tissue: Small intestine.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS MET-16; ASP-76; VAL-90; ARG-188 AND GLY-522.
[4]"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].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ASP-76; VAL-90; ARG-188 AND GLY-522.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY008841 mRNA. Translation: AAG33247.1.
AB035130 mRNA. Translation: BAB18269.1.
AB035131 mRNA. Translation: BAB18270.1.
AY358977 mRNA. Translation: AAQ89336.1.
AC004523 Genomic DNA. Translation: AAC11543.1.
AC122702 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84492.1. Different initiation.
CCDSCCDS42517.1.
PIRJC7594.
JC7598.
RefSeqNP_076433.3. NM_023944.3.
UniGeneHs.131459.

3D structure databases

ProteinModelPortalQ9HCS2.
SMRQ9HCS2. Positions 97-524.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122449. 3 interactions.
IntActQ9HCS2. 2 interactions.
STRING9606.ENSP00000321821.

PTM databases

PhosphoSiteQ9HCS2.

Polymorphism databases

DMDM313104094.

Proteomic databases

MaxQBQ9HCS2.
PaxDbQ9HCS2.
PRIDEQ9HCS2.

Protocols and materials databases

DNASU66002.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324632; ENSP00000321821; ENSG00000186204.
ENST00000550308; ENSP00000448998; ENSG00000186204.
GeneID66002.
KEGGhsa:66002.
UCSCuc002nbl.3. human.

Organism-specific databases

CTD66002.
GeneCardsGC19P015783.
HGNCHGNC:18857. CYP4F12.
MIM611485. gene.
neXtProtNX_Q9HCS2.
PharmGKBPA38717.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000233833.
HOVERGENHBG000182.
InParanoidQ9HCS2.
KOK17730.
OMAIICVINI.
OrthoDBEOG7CNZFK.
PhylomeDBQ9HCS2.
TreeFamTF105088.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9HCS2.
BgeeQ9HCS2.
CleanExHS_CYP4F12.
GenevestigatorQ9HCS2.

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

GeneWikiCYP4F12.
GenomeRNAi66002.
NextBio67510.
PROQ9HCS2.
SOURCESearch...

Entry information

Entry nameCP4FC_HUMAN
AccessionPrimary (citable) accession number: Q9HCS2
Secondary accession number(s): O60389, Q9HCS1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 120 of the entry and version 2 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