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P24455 (CP2A9_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 2A9

EC=1.14.14.1
Alternative name(s):
CYPIIA9
Cytochrome P450-MC1-R
Testosterone 7-alpha-hydroxylase
Gene names
Name:CYP2A9
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Tissue specificity

Liver.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Cytochrome P450 2A9
PRO_0000051672

Sites

Metal binding4381Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict3671L → C in AAA37069. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P24455 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: E7376475D21AEC10

FASTA49356,418
        10         20         30         40         50         60 
MLGSGLILVA ILAYLSVMVL VFVWKQKFRG KLPPGPTPLP YIGNYLQLNT KDIYSSITEL 

        70         80         90        100        110        120 
SERYGPVFTI YLGPRPVVVL YGYDAVKEAL VDQAEEFSGR GEQATYNTLF KDYGVAFSSG 

       130        140        150        160        170        180 
ERAKQLRRFS IATLRDFGVG KRGVEERIQE EAAYLIKMLR STRGAPIDPN DYLSQTVSNV 

       190        200        210        220        230        240 
ISSVVFGDAF DYEDKEFLEL LHMMNEMNKF AASPVGQLYD MFHSVMKYLP GPQQQIIKNT 

       250        260        270        280        290        300 
KELEDFMIRK VKQNQSTLDL NSARNFIDSF LIHMHEEKKN PTSEFNIKNL VMTSLNLFFA 

       310        320        330        340        350        360 
GSETVSSTIR YGFLLLMKYP EVEAKVHEEI DRVIGRNRQP QFEDRMKMPY TEAVINEIQR 

       370        380        390        400        410        420 
FANLAPLGIP RKTIKNTTFR GFFLPKDTDV YPILGSLLTD PKFFTSPKHF NPQNFLDDRG 

       430        440        450        460        470        480 
QLKKIAAFVP FSVGKRFCLG DGLARMELFL FLTTILQNFR LKFPKKLEDI DASPKPLGFS 

       490 
RIIPRYTMSF LPI 

« Hide

References

[1]"Cloning and characterization of Syrian hamster testosterone 7 alpha-hydroxylase, CYP2A9."
Kurose K., Tohkin M., Ushio F., Fukuhara M.
Arch. Biochem. Biophys. 351:60-65(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Cloning and characterization of two major 3-methylcholanthrene inducible hamster liver cytochrome P450s."
Lai T.S., Chiang J.Y.L.
Arch. Biochem. Biophys. 283:429-439(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 208-493.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D86953 mRNA. Translation: BAA25259.1.
M63789 mRNA. Translation: AAA37069.1.
RefSeqNP_001268294.1. NM_001281365.1.

3D structure databases

ProteinModelPortalP24455.
SMRP24455. Positions 30-492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4996550.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101826326.

Phylogenomic databases

HOVERGENHBG015789.

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...

Entry information

Entry nameCP2A9_MESAU
AccessionPrimary (citable) accession number: P24455
Secondary accession number(s): O70538
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: December 15, 1998
Last modified: December 11, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families