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P00185 (CP1A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 137. 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 1A1

Short name=CYP1A1
EC=1.14.14.1
Alternative name(s):
CYPIA1
Cytochrome P450-C
Cytochrome P450MT2

Cleaved into the following 2 chains:

  1. Cytochrome P450MT2A
  2. Cytochrome P450MT2B
Gene names
Name:Cyp1a1
Synonyms:Cyp1a-1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length524 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

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

Cofactor

Heme group By similarity.

Subcellular location

Cytochrome P450 1A1: Cytoplasm Ref.7.

Cytochrome P450MT2A: Endoplasmic reticulum membrane. Mitochondrion membrane. Microsome membrane Ref.7.

Cytochrome P450MT2B: Endoplasmic reticulum. Mitochondrion Ref.7.

Tissue specificity

Liver.

Induction

By 3-methylcholanthrene (3MC) and beta-naphthoflavone (BNF).

Domain

Contains a chimeric signal that facilitates targeting of the protein to both the endoplasmic reticulum and mitochondria. A 12 amino acid sequence between 33 and 44 functions as a putative mitochondrial-targeting signal. The removal of the first 4- or 32-amino acid residues from the intact protein positions the mitochondrial targeting signal for efficient binding to the mitochondrial import receptors. The membrane-free P4501A1 seems to be more sensitive to proteolysis.

Post-translational modification

Two forms; MT2A (long form) and MT2B (short form); are produced by NH2-terminal proteolytic cleavage. This cleavage activates a cryptic mitochondrial targeting signal.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
Microsome
Mitochondrion
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process9-cis-retinoic acid biosynthetic process

Inferred from direct assay PubMed 8765131. Source: RGD

aging

Inferred from expression pattern PubMed 21769602. Source: RGD

amine metabolic process

Inferred from electronic annotation. Source: Ensembl

camera-type eye development

Inferred from expression pattern PubMed 15967433. Source: RGD

cell proliferation

Inferred from expression pattern PubMed 17560764. Source: RGD

coumarin metabolic process

Inferred from direct assay PubMed 11780761. Source: RGD

demethylation

Inferred from direct assay PubMed 10915793PubMed 11370669. Source: GOC

developmental process

Inferred from expression pattern PubMed 18926897. Source: RGD

dibenzo-p-dioxin catabolic process

Inferred from direct assay PubMed 15812643. Source: RGD

dibenzo-p-dioxin metabolic process

Inferred from direct assay PubMed 12464257. Source: RGD

digestive tract development

Inferred from expression pattern PubMed 12162855. Source: RGD

drug metabolic process

Inferred from electronic annotation. Source: Ensembl

embryo development ending in birth or egg hatching

Inferred from expression pattern PubMed 16225763. Source: RGD

flavonoid metabolic process

Inferred from direct assay PubMed 18057719. Source: RGD

hepatocyte differentiation

Inferred from expression pattern PubMed 17574236. Source: RGD

hydrogen peroxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

insecticide metabolic process

Inferred from direct assay PubMed 16169030. Source: RGD

liver development

Inferred from expression pattern PubMed 12162855. Source: RGD

maternal process involved in parturition

Inferred from expression pattern PubMed 16226747. Source: RGD

porphyrin-containing compound metabolic process

Inferred from direct assay PubMed 12907239. Source: RGD

positive regulation of G1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 14742689. Source: RGD

response to antibiotic

Inferred from expression pattern PubMed 10037757. Source: RGD

response to arsenic-containing substance

Inferred from expression pattern PubMed 10329507. Source: RGD

response to drug

Inferred from expression pattern PubMed 19122336. Source: RGD

response to food

Inferred from expression pattern PubMed 15740081PubMed 17673347. Source: RGD

response to herbicide

Inferred from expression pattern PubMed 12907239. Source: RGD

response to hyperoxia

Inferred from expression pattern PubMed 16497785. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 11589108. Source: RGD

response to immobilization stress

Inferred from expression pattern PubMed 14726153. Source: RGD

response to iron(III) ion

Inferred from expression pattern PubMed 15211619. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 18308837. Source: RGD

response to nematode

Inferred from expression pattern PubMed 12621079. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 10413312PubMed 10640292PubMed 10772642PubMed 16937917PubMed 18678235PubMed 18827444PubMed 18978342PubMed 19373505. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 16901763PubMed 16918313PubMed 16966090PubMed 17624648PubMed 18098063PubMed 19100306. Source: RGD

response to virus

Inferred from expression pattern PubMed 15061698. Source: RGD

response to vitamin A

Inferred from expression pattern PubMed 10381141. Source: RGD

response to wounding

Inferred from expression pattern PubMed 14723344. Source: RGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15716480. Source: RGD

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 19219745. Source: RGD

mitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay Ref.7. Source: RGD

   Molecular_functionaromatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

catalytic activity

Inferred from direct assay PubMed 10381141. Source: RGD

demethylase activity

Inferred from direct assay PubMed 10915793PubMed 11370669. Source: RGD

enzyme binding

Inferred from direct assay PubMed 10891369. Source: RGD

flavonoid 3'-monooxygenase activity

Inferred from direct assay PubMed 18057719. Source: RGD

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

monooxygenase activity

Inferred from direct assay PubMed 12054491PubMed 12464257PubMed 12907239PubMed 8765131. Source: RGD

oxidoreductase activity

Inferred from direct assay PubMed 11339718PubMed 11370669. Source: RGD

oxidoreductase activity, acting on diphenols and related substances as donors

Inferred from direct assay PubMed 12054491. Source: RGD

protein binding

Inferred from physical interaction PubMed 11350928PubMed 9454608. Source: RGD

steroid hydroxylase activity

Inferred from direct assay PubMed 11370669. Source: RGD

vitamin D 24-hydroxylase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain2 – 524523Cytochrome P450 1A1
PRO_0000003564
Chain5 – 524520Cytochrome P450MT2A
PRO_0000003565
Chain33 – 524492Cytochrome P450MT2B
PRO_0000003566

Regions

Region33 – 4412Mitochondrial targeting signal

Sites

Metal binding4611Iron (heme axial ligand)
Binding site2281Substrate By similarity

Experimental info

Mutagenesis32 – 332VT → AI: No proteolytic cleavage. Ref.7
Sequence conflict21 – 222TT → VV AA sequence Ref.5
Sequence conflict531I → M in CAA25153. Ref.2
Sequence conflict4941M → S in AAA41025. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P00185 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: C766DF8044D598C5

FASTA52459,393
        10         20         30         40         50         60 
MPSVYGFPAF TSATELLLAV TTFCLGFWVV RVTRTWVPKG LKSPPGPWGL PFIGHVLTLG 

        70         80         90        100        110        120 
KNPHLSLTKL SQQYGDVLQI RIGSTPVVVL SGLNTIKQAL VKQGDDFKGR PDLYSFTLIA 

       130        140        150        160        170        180 
NGQSMTFNPD SGPLWAARRR LAQNALKSFS IASDPTLASS CYLEEHVSKE AEYLISKFQK 

       190        200        210        220        230        240 
LMAEVGHFDP FKYLVVSVAN VICAICFGRR YDHDDQELLS IVNLSNEFGE VTGSGYPADF 

       250        260        270        280        290        300 
IPILRYLPNS SLDAFKDLNK KFYSFMKKLI KEHYRTFEKG HIRDITDSLI EHCQDRRLDE 

       310        320        330        340        350        360 
NANVQLSDDK VITIVFDLFG AGFDTITTAI SWSLMYLVTN PRIQRKIQEE LDTVIGRDRQ 

       370        380        390        400        410        420 
PRLSDRPQLP YLEAFILETF RHSSFVPFTI PHSTIRDTSL NGFYIPKGHC VFVNQWQVNH 

       430        440        450        460        470        480 
DQELWGDPNE FRPERFLTSS GTLDKHLSEK VILFGLGKRK CIGETIGRLE VFLFLAILLQ 

       490        500        510        520 
QMEFNVSPGE KVDMTPAYGL TLKHARCEHF QVQMRSSGPQ HLQA 

« Hide

References

[1]"Distinct organization of methylcholanthrene- and phenobarbital-inducible cytochrome P-450 genes in the rat."
Sogawa K., Gotoh O., Kawajiri K., Fujii-Kuriyama Y.
Proc. Natl. Acad. Sci. U.S.A. 81:5066-5070(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-induced rat liver cytochrome P-450MC."
Yabusaki Y., Shimizu M., Murakami H., Nakamura K., Oeda K., Ohkawa H.
Nucleic Acids Res. 12:2929-2938(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Gene structure and nucleotide sequence for rat cytochrome P-450c."
Hines R.N., Levy J.B., Conrad R.D., Iversen P.L., Shen M.-L., Renli A.M., Bresnick E.
Arch. Biochem. Biophys. 237:465-476(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Amino-terminal sequence and structure of monoclonal antibody immunopurified cytochromes P-450."
Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V., Friedman F.K.
Biochemistry 25:2397-2402(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26.
[5]"Effect of nutritional imbalances on cytochrome P-450 isozymes in rat liver."
Amelizad Z., Narbonne J.F., Wolf C.R., Robertson L.W., Oesch F.
Biochem. Pharmacol. 37:3245-3249(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-22.
[6]"Identification and characterization of cytochrome P4501A1 amino acid residues interacting with a radiolabeled photoaffinity diazido-benzphetamine analogue."
Cvrk T., Hodek P., Strobel H.W.
Arch. Biochem. Biophys. 330:142-152(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[7]"Targeting of NH2-terminal-processed microsomal protein to mitochondria: a novel pathway for the biogenesis of hepatic mitochondrial P450MT2."
Addya S., Anandatheerthavarada H.K., Biswas G., Bhagwat S.V., Mullick J., Avadhani N.G.
J. Cell Biol. 139:589-599(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 32-VAL-THR-33.
Strain: Sprague-Dawley.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02246 Genomic DNA. Translation: AAA41027.1.
X00469 mRNA. Translation: CAA25153.1.
M26129 Genomic DNA. Translation: AAA41025.1.
PIRO4RTMC. A00185.
RefSeqNP_036672.2. NM_012540.2.
XP_006243212.1. XM_006243150.1.
UniGeneRn.10352.

3D structure databases

ProteinModelPortalP00185.
SMRP00185. Positions 37-513.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246477. 2 interactions.
STRING10116.ENSRNOP00000026473.

Chemistry

ChEMBLCHEMBL2922.

Proteomic databases

PaxDbP00185.
PRIDEP00185.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026473; ENSRNOP00000026473; ENSRNOG00000019500.
GeneID24296.
KEGGrno:24296.
UCSCRGD:2458. rat.

Organism-specific databases

CTD1543.
RGD2458. Cyp1a1.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00750000117317.
HOVERGENHBG106944.
InParanoidP00185.
KOK07408.
OMAKVITIVF.
OrthoDBEOG7RBZ85.
PhylomeDBP00185.
TreeFamTF105095.

Enzyme and pathway databases

SABIO-RKP00185.

Gene expression databases

GenevestigatorP00185.

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...

Other

NextBio602902.
PROP00185.

Entry information

Entry nameCP1A1_RAT
AccessionPrimary (citable) accession number: P00185
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 137 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