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Q64391 (CP1A2_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. 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 1A2

EC=1.14.14.1
Alternative name(s):
CYPIA2
Gene names
Name:CYP1A2
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Most active in catalyzing 2-hydroxylation By similarity.

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.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processalkaloid metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular respiration

Inferred from electronic annotation. Source: Ensembl

cellular response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

dibenzo-p-dioxin metabolic process

Inferred from electronic annotation. Source: Ensembl

exogenous drug catabolic process

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

monocarboxylic acid metabolic process

Inferred from electronic annotation. Source: Ensembl

monoterpenoid metabolic process

Inferred from electronic annotation. Source: Ensembl

oxidative deethylation

Inferred from electronic annotation. Source: Ensembl

oxidative demethylation

Inferred from electronic annotation. Source: Ensembl

porphyrin-containing compound metabolic process

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

steroid catabolic process

Inferred from electronic annotation. Source: Ensembl

toxin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaromatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

caffeine oxidase activity

Inferred from electronic annotation. Source: Ensembl

demethylase activity

Inferred from electronic annotation. Source: Ensembl

heme binding

Inferred from sequence or structural similarity. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 515514Cytochrome P450 1A2
PRO_0000051650

Sites

Metal binding4581Iron (heme axial ligand) By similarity
Binding site2261Substrate By similarity

Experimental info

Sequence conflict1491V → L in AAB70866. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q64391 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E5EDF0B9D33151A8

FASTA51558,423
        10         20         30         40         50         60 
MPLSWLLPFS AMELLLTATI FYLVLWVVKA FRLQVPKGLK SPPGPWGWPL IGHVLTLGKN 

        70         80         90        100        110        120 
PHLALTRLSA RYGDVLQIRI GSTPVVVLSG LDTIRQALVR QSDDFKGRPD LYSSTFISDG 

       130        140        150        160        170        180 
QSMIFNPDSG PVWAARRRLA QSALQSFSVA SDPASVSSCY LEEHVSREAE HLVTKLLDLM 

       190        200        210        220        230        240 
AGPGCFEPSS QIVGSVANVI GAMCFGKNFP QTSEEMLQIV NTSKEFTEFA SSGNPVDFFP 

       250        260        270        280        290        300 
ILRYLPNPML QQFKDFNKRF LQFLQKTVQE HYQDFDKNHV QDIASALFKH SEESPHVNGD 

       310        320        330        340        350        360 
LIPRKKIVNL VNDIFGAGFD TVTTAISWSL LYLVTKPEIQ KKIHKELDAV IGRDRKPRLA 

       370        380        390        400        410        420 
DRPQLPYMEA FILEVFRYSS FLPFTIPHCT TRDTILNGFY IPKDRCVFIN QWQVNHDPKQ 

       430        440        450        460        470        480 
WEDPFEFRPE RFLLANNTAV DKTLSDKILL FGLGKRRCIG ETLGRWEVFL FLAILLQQLE 

       490        500        510 
FSVPPGVKVD LTPVYGLTMK PPHCQHVQAR PRFSK 

« Hide

References

[1]"Regulation of CYP1A and CYP3A mRNAs by ascorbic acid in guinea pigs."
Mori T., Itoh S., Ohgiya S., Ishizaki K., Kamataki T.
Arch. Biochem. Biophys. 348:268-277(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Hartley.
Tissue: Liver.
[2]Black V.H.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Hartley.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50457 mRNA. Translation: BAA09048.1.
U23501 mRNA. Translation: AAB70866.1.
RefSeqNP_001166165.1. NM_001172694.1.

3D structure databases

ProteinModelPortalQ64391.
SMRQ64391. Positions 34-514.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000017610.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCPOT00000001250; ENSCPOP00000017610; ENSCPOG00000001235.
GeneID100135513.

Organism-specific databases

CTD1544.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00750000117317.
HOGENOMHOG000036991.
HOVERGENHBG106944.
InParanoidQ64391.
OrthoDBEOG7RBZ85.
TreeFamTF105095.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008066. Cyt_P450_E_grp-I_CYP1.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR01683. EP450ICYP1A.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCP1A2_CAVPO
AccessionPrimary (citable) accession number: Q64391
Secondary accession number(s): Q64404
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 98 of the entry and version 1 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