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Reviewed, UniProtKB/Swiss-Prot P20816 (CP4A2_RAT)

Last modified January 19, 2010. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cytochrome P450 4A2
Alternative name(s):
    CYPIVA2
    Lauric acid omega-hydroxylase
    EC=1.14.15.3
    Cytochrome P450-LA-omega 2
    Cytochrome P450 K-5
    Cytochrome P-450 K-2
Gene names
Name: Cyp4a2
Synonyms: Cyp4a-2, Cyp4a11
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Octane + reduced rubredoxin + O2 = 1-octanol + oxidized rubredoxin + H2O.

Cofactor

Heme group By similarity.

Subcellular location

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

Induction

By clofibrate.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processarachidonic acid metabolic process

Inferred from mutant phenotype. Source: RGD

icosanoid biosynthetic process

Inferred from mutant phenotype. Source: RGD

kidney development

Inferred from expression pattern. Source: RGD

lauric acid metabolic process

Inferred from direct assay. Source: RGD

linoleic acid metabolic process

Inferred from direct assay. Source: RGD

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

response to drug

Inferred from expression pattern. Source: RGD

response to hormone stimulus

Inferred from expression pattern. Source: RGD

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

extrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microsome

Inferred from direct assay. Source: RGD

   Molecular functionalkane 1-monooxygenase activity

Inferred from electronic annotation. Source: EC

arachidonic acid 11,12-epoxygenase activity

Traceable author statement. Source: RGD

arachidonic acid binding

Inferred from direct assay. Source: RGD

electron carrier activity

Inferred from electronic annotation. Source: InterPro

fatty acid (omega-1)-hydroxylase activity

Inferred from mutant phenotype. Source: RGD

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 44
PRO_0000003567
Chain5 – 504500Cytochrome P450 4A2
PRO_0000003568

Sites

Metal binding4511Iron (heme axial ligand)
Binding site3151Heme (covalent; via 1 link)

Sequences

Sequence LengthMass (Da)Tools
P20816-1 [UniParc].

Last modified August 1, 1991. Version 2.
Checksum: 8A795DD454125287

FASTA50457,969
        10         20         30         40         50         60 
MGFSVFSPTR SLDGVSGFFQ GAFLLSLFLV LFKAVQFYLR RQWLLKALEK FPSTPSHWLW 

        70         80         90        100        110        120 
GHNLKDREFQ QVLTWVEKFP GACLQWLSGS TARVLLYDPD YVKVVLGRSD PKPYQSLAPW 

       130        140        150        160        170        180 
IGYGLLLLNG KKWFQHRRML TPAFHYDILK PYVKIMADSV SIMLDKWEKL DDQDHPLEIF 

       190        200        210        220        230        240 
HYVSLMTLDT VMKCAFSHQG SVQLDVNSRS YTKAVEDLNN LIFFRVRSAF YGNSIIYNMS 

       250        260        270        280        290        300 
SDGRLSRRAC QIAHEHTDGV IKTRKAQLQN EEELQKARKK RHLDFLDILL FAKMEDGKSL 

       310        320        330        340        350        360 
SDEDLRAEVD TFMFEGHDTT ASGISWVFYA LATHPEHQER CREEVQSILG DGTSVTWDHL 

       370        380        390        400        410        420 
DQMPYTTMCI KEALRLYSPV PSVSRELSSP VTFPDGRSIP KGIRVTILIY GLHHNPSYWP 

       430        440        450        460        470        480 
NPKVFDPSRF SPDSPRHSHA YLPFSGGARN CIGKQFAMNE LKVAVALTLL RFELLPDPTR 

       490        500 
IPVPMPRLVL KSKNGIHLRL KKLR 

« Hide

References

« Hide 'large scale' references
[1]"The rat clofibrate-inducible CYP4A gene subfamily. I. Complete intron and exon sequence of the CYP4A1 and CYP4A2 genes, unique exon organization, and identification of a conserved 19-bp upstream element."
Kimura S., Hanioka N., Matsunaga E., Gonzalez F.J.
DNA 8:503-516(1989) [PubMed: 2766932] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]"Purification and NH2-terminal amino acid sequences of human and rat kidney fatty acid omega-hydroxylases."
Kawashima H., Kusunose E., Kubota I., Maekawa M., Kusunose M.
Biochim. Biophys. Acta 1123:156-162(1992) [PubMed: 1739747] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE OF 5-34.
Tissue: Kidney.
[4]"Characterization of three cytochrome P450s purified from renal microsomes of untreated male rats and comparison with human renal cytochrome P450."
Imaoka S., Nagashima K., Funae Y.
Arch. Biochem. Biophys. 276:473-480(1990) [PubMed: 2306108] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE OF 5-19.
Strain: Sprague-Dawley.
Tissue: Kidney.
[5]"Covalently linked heme in cytochrome P4504A fatty acid hydroxylases."
Hoch U., Ortiz de Montellano P.R.
J. Biol. Chem. 276:11339-11346(2001) [PubMed: 11139583] [Abstract]
Cited for: COVALENT HEME ATTACHMENT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57719 Genomic DNA. Translation: AAA41039.1.
BC078684 mRNA. Translation: AAH78684.1.
BC098705 mRNA. Translation: AAH98705.1.
IPIIPI00203317.
PIRA32965.
PC4350.
RefSeqNP_001038235.1.
UniGeneRn.33492

3D structure databases

SMRP20816. Positions 74-502.
ModBaseSearch...

Protein-protein interaction databases

STRINGP20816.

Proteomic databases

PRIDEP20816.

Genome annotation databases

EnsemblENSRNOT00000045571; ENSRNOP00000045567; ENSRNOG00000030154; Rattus norvegicus. [Genome view]
GeneID24306.
KEGGrno:24306.

Organism-specific databases

CTD24306.
RGD2479. Cyp4a2.

Phylogenomic databases

eggNOGmaNOG05356.
HOVERGENP20816.

Enzyme and pathway databases

BRENDA1.14.15.3. 248.

Gene expression databases

ArrayExpressP20816.
GenevestigatorP20816.
GermOnlineENSRNOG00000030154. Rattus norvegicus.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio602929.

Entry information

Entry nameCP4A2_RAT
AccessionPrimary (citable) accession number: P20816
Secondary accession number(s): Q4G071
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: August 1, 1991
Last modified: January 19, 2010
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents