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P00187 (CP1A2_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 122. 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
Cytochrome P450 isozyme 4
Short name=Cytochrome P450 LM4
Cytochrome P450-PM4
Gene names
Name:CYP1A2
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length516 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. Most active in catalyzing 2-hydroxylation.

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

By beta-naphthoflavone and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD).

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 516515Cytochrome P450 1A2
PRO_0000051655

Regions

Region361 – 3655Substrate binding

Sites

Metal binding4581Iron (heme axial ligand)
Binding site2261Substrate By similarity
Site4031Involved in electron transfer with reductase

Natural variations

Natural variant1741G → S. Ref.1
Natural variant2331G → S. Ref.1
Natural variant2991S → G. Ref.1

Experimental info

Sequence conflict221C → S AA sequence Ref.3
Sequence conflict671R → P in AAA31437. Ref.1
Sequence conflict701R → Q AA sequence Ref.3
Sequence conflict921D → N AA sequence Ref.3
Sequence conflict931T → H in AAA31433. Ref.4
Sequence conflict1211Q → H in CAA29171. Ref.2
Sequence conflict1721L → F AA sequence Ref.3
Sequence conflict1941V → S AA sequence Ref.3
Sequence conflict208 – 2125RFPQG → FPQGM AA sequence Ref.3
Sequence conflict2081R → H in AAA31437. Ref.1
Sequence conflict2081R → H in CAA32066. Ref.1
Sequence conflict2081R → H in AAA31433. Ref.4
Sequence conflict247 – 2515NRPLQ → QPNLR AA sequence Ref.3
Sequence conflict2881F → I in AAA31433. Ref.4
Sequence conflict291 – 30212SEKNS…NSGLI → NEMDSMDDGAHV in AAA31433. Ref.4
Sequence conflict3091N → T in AAA31433. Ref.4
Sequence conflict354 – 3552AR → PG in AAA31437. Ref.1
Sequence conflict354 – 3552AR → PG in CAA32066. Ref.1
Sequence conflict3581R → L in AAA31433. Ref.4
Sequence conflict3591L → I AA sequence Ref.3
Sequence conflict3591L → I in AAA31433. Ref.4
Sequence conflict4621T → I in AAA31433. Ref.4
Sequence conflict4941I → T AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P00187 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3FD074D74A47C3EF

FASTA51658,334
        10         20         30         40         50         60 
MAMSPAAPLS VTELLLVSAV FCLVFWAVRA SRPKVPKGLK RLPGPWGWPL LGHLLTLGKN 

        70         80         90        100        110        120 
PHVALARLSR RYGDVFQIRL GSTPVVVLSG LDTIKQALVR QGDDFKGRPD LYSSSFITEG 

       130        140        150        160        170        180 
QSMTFSPDSG PVWAARRRLA QDSLKSFSIA SNPASSSSCY LEEHVSQEAE NLIGRFQELM 

       190        200        210        220        230        240 
AAVGRFDPYS QLVVSAARVI GAMCFGRRFP QGSEEMLDVV RNSSKFVETA SSGSPVDFFP 

       250        260        270        280        290        300 
ILRYLPNRPL QRFKDFNQRF LRFLQKTVRE HYEDFDRNSI QDITGALFKH SEKNSKANSG 

       310        320        330        340        350        360 
LIPQEKIVNL VNDIFGAGFD TITTALSWSL MYLVTNPRRQ RKIQEELDAV VGRARQPRLS 

       370        380        390        400        410        420 
DRPQLPYLEA FILELFRHTS FVPFTIPHST TRDTTLNGFH IPKECCIFIN QWQINHDPQL 

       430        440        450        460        470        480 
WGDPEEFRPE RFLTADGAAI NKPLSEKVTL FGLGKRRCIG ETLARWEVFL FLAILLQRLE 

       490        500        510 
FSVPPGVPVD LTPIYGLTMK HPRCEHVQAR PRFSDQ 

« Hide

References

[1]"cDNA cloning and functional expression in yeast Saccharomyces cerevisiae of beta-naphthoflavone-induced rabbit liver P-450 LM4 and LM6."
Pompon D.
Eur. J. Biochem. 177:285-293(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-174; SER-233 AND GLY-299.
Strain: New Zealand white.
[2]"Structural analysis of cloned cDNAs for polycyclic hydrocarbon-inducible forms of rabbit liver microsomal cytochrome P-450."
Kagawa N., Mihara K., Sato R.
J. Biochem. 101:1471-1479(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Complete amino acid sequence of a cytochrome P-450 isolated from beta-naphthoflavone-induced rabbit liver microsomes. Comparison with phenobarbital-induced and constitutive isozymes and identification of invariant residues."
Ozols J.
J. Biol. Chem. 261:3965-3979(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-516.
[4]"Cloning and characterization of cDNAs encoding 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible rabbit mRNAs for cytochrome P-450 isozymes 4 and 6."
Okino S.T., Quattrochi L.C., Barnes H.J., Osanto S., Griffin K.J., Johnson E.F., Tukey R.H.
Proc. Natl. Acad. Sci. U.S.A. 82:5310-5314(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 92-515.
[5]"Modification of cytochrome P450 1A2 enzymes by the mechanism-based inactivator 2-ethynylnaphthalene and the photoaffinity label 4-azidobiphenyl."
Yun C.H., Hammons G.J., Jones G., Martin M.V., Hopkins N.E., Alworth W.L., Guengerich F.P.
Biochemistry 31:10556-10563(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 176-185.
[6]"On the amino acid sequence of cytochrome P-450 isozyme 4 from rabbit liver microsomes."
Fujita V.S., Black S.D., Tarr G.E., Koop D.R., Coon M.J.
Proc. Natl. Acad. Sci. U.S.A. 81:4260-4264(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36538 mRNA. Translation: AAA31437.1.
X13853 mRNA. Translation: CAA32066.1.
X05686 mRNA. Translation: CAA29171.1.
M11728 mRNA. Translation: AAA31433.1.
PIRO4RBBN. B27821.
RefSeqNP_001164592.1. NM_001171121.1.
UniGeneOcu.1943.

3D structure databases

ProteinModelPortalP00187.
SMRP00187. Positions 34-514.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000008665.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100328937.

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000036991.
HOVERGENHBG106944.

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_RABIT
AccessionPrimary (citable) accession number: P00187
Secondary accession number(s): Q29526
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 122 of the entry and version 3 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