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P20853 (CP2A7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. 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 2A7

EC=1.14.14.1
Alternative name(s):
CYPIIA7
Cytochrome P450 IIA4
Gene names
Name:CYP2A7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length494 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

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

Cofactor

Heme group By similarity.

Subcellular location

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

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 componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityPolymorphism
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaromatase 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

oxygen binding

Traceable author statement PubMed 7864805. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Cytochrome P450 2A7
PRO_0000051669

Sites

Metal binding4391Iron (heme axial ligand) By similarity

Natural variations

Natural variant611F → I.
Corresponds to variant rs10425176 [ dbSNP | Ensembl ].
VAR_047815
Natural variant641C → R.
Corresponds to variant rs10425169 [ dbSNP | Ensembl ].
VAR_047816
Natural variant1691D → E.
Corresponds to variant rs4142867 [ dbSNP | Ensembl ].
VAR_061043
Natural variant2741H → R.
Corresponds to variant rs4079366 [ dbSNP | Ensembl ].
VAR_047817
Natural variant3011A → G.
Corresponds to variant rs2545754 [ dbSNP | Ensembl ].
VAR_047818
Natural variant3111R → C.
Corresponds to variant rs3869579 [ dbSNP | Ensembl ].
VAR_047819
Natural variant3681M → T.
Corresponds to variant rs2261144 [ dbSNP | Ensembl ].
VAR_047820
Natural variant4791V → G. Ref.1
Corresponds to variant rs12460590 [ dbSNP | Ensembl ].
VAR_061044

Experimental info

Sequence conflict1081D → E in AAB40520. Ref.2
Sequence conflict1631T → S in AAA52138. Ref.1
Sequence conflict2261V → L in AAB40520. Ref.2
Sequence conflict2421Q → L in AAB40520. Ref.2
Sequence conflict402 – 4032PS → LR in AAB40520. Ref.2
Sequence conflict4091Q → R in AAB40520. Ref.2
Sequence conflict418 – 4192DD → GE in AAB40520. Ref.2
Sequence conflict4261S → R in AAB40520. Ref.2
Sequence conflict4351G → R in AAB40520. Ref.2
Sequence conflict4381N → Y in AAA52138. Ref.1
Sequence conflict4751P → S in AAA52138. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P20853 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 4DA10D0C2714E6AA

FASTA49456,425
        10         20         30         40         50         60 
MLASGLLLVA LLACLTVMVL MSVWQQRKSR GKLPPGPTPL PFIGNYLQLN TEHICDSIMK 

        70         80         90        100        110        120 
FSECYGPVFT IHLGPRRVVV LCGHDAVREA LVDQAEEFSG RGEQATFDWV FKGYGVAFSN 

       130        140        150        160        170        180 
GERAKQLLRF AIATLRDFGV GKRGIEERIQ EESGFLIEAI RSTHGANIDP TFFLSRTVSN 

       190        200        210        220        230        240 
VISSIVFGDR FDYEDKEFLS LLSMMLGIFQ FTSTSTGQLY EMFSSVMKHL PGPQQQAFKL 

       250        260        270        280        290        300 
LQGLEDFIAK KVEHNQRTLD PNSPQDFIDS FLIHMQEEEK NPNTEFYLKN LMMSTLNLFI 

       310        320        330        340        350        360 
AGTETVSTTL RYGFLLLMKH PEVEAKVHEE IDRVIGKNRQ PKFEDRTKMP YMEAVIHEIQ 

       370        380        390        400        410        420 
RFGDVIPMSL ARRVKKDTKF RDFFLPKGTE VFPMLGSVLR DPSFFSNPQD FNPQHFLDDK 

       430        440        450        460        470        480 
GQFKKSDAFV PFSIGKRNCF GEGLARMELF LFFTTVMQNF RLKSSQSPKD IDVSPKHVVF 

       490 
ATIPRNYTMS FLPR 

« Hide

References

« Hide 'large scale' references
[1]"The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes."
Yamano S., Tatsuno J., Gonzalez F.J.
Biochemistry 29:1322-1329(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-479.
Tissue: Liver.
[2]"A genetic polymorphism in coumarin 7-hydroxylation: sequence of the human CYP2A genes and identification of variant CYP2A6 alleles."
Fernandez-Salguero P., Hoffman S.M., Cholerton S., Mohrenweiser H., Raunio H., Rautio A., Pelkonen O., Huang J.D., Evans W.E., Idle J.R.
Am. J. Hum. Genet. 57:651-660(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33317 mRNA. Translation: AAA52138.1.
U22029 mRNA. Translation: AAB40520.1.
AC008537 Genomic DNA. No translation available.
PIRC34271.
I38967.
RefSeqNP_000755.2. NM_000764.2.
NP_085079.2. NM_030589.2.
UniGeneHs.719890.

3D structure databases

ProteinModelPortalP20853.
SMRP20853. Positions 31-494.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP20853.

Polymorphism databases

DMDM215273959.

Proteomic databases

PRIDEP20853.

Protocols and materials databases

DNASU1549.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301146; ENSP00000301146; ENSG00000198077.
GeneID1549.
KEGGhsa:1549.
UCSCuc002opm.3. human.

Organism-specific databases

CTD1549.
GeneCardsGC19M041381.
H-InvDBHIX0137215.
HGNCHGNC:2611. CYP2A7.
HPACAB033510.
MIM608054. gene.
neXtProtNX_P20853.
PharmGKBPA27102.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000036992.
HOVERGENHBG015789.
InParanoidP20853.
KOK17684.
OMALNTEHIC.
OrthoDBEOG7RBZ85.
PhylomeDBP20853.
TreeFamTF352043.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP20853.
GenevestigatorP20853.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008067. Cyt_P450_E_grp-I_CYP2A-like.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR01684. EP450ICYP2A.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCYP2A7.
GenomeRNAi1549.
NextBio6405.
PROP20853.
SOURCESearch...

Entry information

Entry nameCP2A7_HUMAN
AccessionPrimary (citable) accession number: P20853
Secondary accession number(s): Q13121
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 132 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