Cytochrome P450 1A2 - Oryctolagus cuniculus (Rabbit)

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Reviewed, UniProtKB/Swiss-Prot P00187 (CP1A2_RABIT)

Last modified January 19, 2010. Version 96. History...

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

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Names and origin

Protein names

Recommended 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

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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Protein attributes

Sequence length	516 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aromatase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 516

515

Cytochrome P450 1A2

PRO_0000051655

Regions

Region

361 – 365

Substrate binding

Sites

Metal binding

458

Iron (heme axial ligand)

Site

403

Involved in electron transfer with reductase

Amino acid modifications

Modified residue

289

N6-acetyllysine By similarity

Natural variations

Natural variant

174

G → S

Natural variant

233

G → S

Natural variant

299

S → G

Experimental info

Sequence conflict

C → S AA sequence Ref.3

Sequence conflict

R → P in AAA31437. Ref.1

Sequence conflict

R → Q AA sequence Ref.3

Sequence conflict

D → N AA sequence Ref.3

Sequence conflict

D → N Ref.4

Sequence conflict

121

Q → H in CAA29171. Ref.2

Sequence conflict

172

L → F AA sequence Ref.3

Sequence conflict

194

V → S AA sequence Ref.3

Sequence conflict

208 – 212

RFPQG → FPQGM AA sequence Ref.3

Sequence conflict

208

R → H in AAA31437. Ref.1

Sequence conflict

247 – 251

NRPLQ → QPNLR AA sequence Ref.3

Sequence conflict

289 – 302

KHSEK…NSGLI → IKHNEMDSMDDGAHV Ref.4

Sequence conflict

354 – 355

AR → PG in CAA32066. Ref.1

Sequence conflict

354 – 355

AR → PG in AAA31437. Ref.1

Sequence conflict

358

R → L in AAA31433. Ref.4

Sequence conflict

359

L → I AA sequence Ref.3

Sequence conflict

359

L → I in AAA31433. Ref.4

Sequence conflict

462

T → I in AAA31433. Ref.4

Sequence conflict

494

I → T AA sequence Ref.3

Sequence conflict

494

I → T in AAA31433. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P00187-1 [UniParc].

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

516

58,334

        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

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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: 2847925] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 3667560] [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: 3949797] [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: 2991917] [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: 1420171] [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: 6589592] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	X13853 mRNA. Translation: CAA32066.1. M36538 mRNA. Translation: AAA31437.1. X05686 mRNA. Translation: CAA29171.1. M11728 mRNA. Translation: AAA31433.1. Sequence problems.
PIR	O4RBBN. B27821.
3D structure databases
SMR	P00187. Positions 34-514.
ModBase	Search...
Genome annotation databases
Ensembl	ENSOCUT00000010056; ENSOCUP00000008665; ENSOCUG00000010056; Oryctolagus cuniculus. [Genome view]
Phylogenomic databases
eggNOG	maNOG17048.
HOVERGEN	P00187.
Enzyme and pathway databases
BRENDA	1.14.14.1. 255.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. IPR008066. Cyt_P450_E_grp-I_CYP1. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit. PTHR19383:SF63. Cyt_P450_E_grp-I_CYP1. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR01683. EP450ICYP1A. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

CP1A2_RABIT

Accession

Primary (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:	January 19, 2010
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents