Cytochrome P450 1A1 - Oryctolagus cuniculus (Rabbit)

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P05176 (CP1A1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytochrome P450 1A1
EC=1.14.14.1

Alternative name(s):
CYPIA1
Cytochrome P-450 PHPAH1
Cytochrome P450 isozyme 6
Short name=Cytochrome P450 LM6

Gene names

Name:

CYP1A1

Organism

Oryctolagus cuniculus (Rabbit) [Reference proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	518 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and by 3-methylcholanthrene (3MC).
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	amine metabolic process Inferred from electronic annotation. Source: Compara drug metabolic process Inferred from electronic annotation. Source: Compara heterocycle metabolic process Inferred from electronic annotation. Source: Compara hydrogen peroxide biosynthetic process Inferred from electronic annotation. Source: Compara response to toxin Inferred from electronic annotation. Source: Compara toxin metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 iron ion binding Inferred from electronic annotation. Source: InterPro vitamin D 24-hydroxylase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 518

518

Cytochrome P450 1A1

PRO_0000051632

Sites

Metal binding

461

Iron (heme axial ligand)

Experimental info

Sequence conflict

R → P in AAA31431. Ref.2

Sequence conflict

146

L → R in AAA31431. Ref.2

Sequence conflict

176 – 177

SK → GR in AAA31431. Ref.2

Sequence conflict

341 – 345

PRIQR → RQHTRE in AAA31431. Ref.2

Sequence conflict

422

P → R in AAA31431. Ref.2

Sequence conflict

427

D → V in AAA31431. Ref.2

Sequence conflict

429 – 430

EA → RS in AAA31431. Ref.2

Sequence conflict

442 – 443

AV → TL in AAA31431. Ref.2

Sequence conflict

446 – 449

ALTE → GPDD in AAA31431. Ref.2

Sequence conflict

463

G → A in AAA31431. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P05176 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: A9D382C5DF122A5A
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FASTA

518

58,278

        10         20         30         40         50         60 
MVSDFGLPTF ISATELLLAS AVFCLVFWVA GASKPRVPKG LKRLPGPWGW PLLGHVLTLG 

        70         80         90        100        110        120 
KNPHVALARL SRRYGDVFQI RLGSTPVVVL SGLDTIKQAL VRQGDDFKGR PDLYSFSFVT 

       130        140        150        160        170        180 
KGQSMIFGSD SGPVWAARRR LAQNALNSFS VASDPASSSS CYLEEHVSQE AENLISKFQE 

       190        200        210        220        230        240 
LMAAVGHFDP YRYVVMSVAN VICAMCFGRR YDHDDQELLS LVNLNDEFGK VAASGSPADF 

       250        260        270        280        290        300 
FLILRYLPNP ALDTFKDLNE RFYSFTQERV KEHCRSFEKG HIRDITDSLI KHYRVDRLDE 

       310        320        330        340        350        360 
NANVQVSDEK TVGIVLDLFG AGFDTVTTAI SWSLMYLVTK PRIQRKIQEE LDAVVGRARR 

       370        380        390        400        410        420 
PRFSDRPQLP YLEAVIMETF RHTSFLPFTI PHSTTRDTSL GGFYIPKGRC VFVNQWQNNH 

       430        440        450        460        470        480 
DPELWGDPEA FRPERFLTPS GAVDKALTEK VLLFGLGKRK CIGETIGRLE VFLFLATLLQ 

       490        500        510 
QVEFSVSPGT TVDMTPIYGL TMKHARCEHF QAKLRFEA

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References

[1]	"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.
[2]	"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 73-518.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X05685 mRNA. Translation: CAA29170.1. M11727 mRNA. Translation: AAA31431.1.
PIR	A27821.
RefSeq	NP_001164543.1. NM_001171072.1.
UniGene	Ocu.2041.
3D structure databases
ProteinModelPortal	P05176.
SMR	P05176. Positions 36-516.
ModBase	Search...
Protein-protein interaction databases
STRING	9986.ENSOCUP00000015239.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSOCUT00000017743; ENSOCUP00000015239; ENSOCUG00000017744.
GeneID	100328613.
Phylogenomic databases
eggNOG	COG2124.
GeneTree	ENSGT00680000099714.
HOGENOM	HOG000036991.
HOVERGEN	HBG106944.
OrthoDB	EOG4WSW9D.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. IPR008066. Cyt_P450_E_grp-I_CYP1. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR01683. EP450ICYP1A. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CP1A1_RABIT

Accession

Primary (citable) accession number: P05176

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 1, 1988
Last modified:	April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents