Cytochrome P450 2C5 - Oryctolagus cuniculus (Rabbit)

Contribute

Send feedback

Reviewed, UniProtKB/Swiss-Prot P00179 (CP2C5_RABIT)

Last modified November 25, 2008. Version 74. History...

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

Documents (2) |

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

Hide | Top

Names and origin

Protein names

Recommended name:
    Cytochrome P450 2C5
    EC=1.14.14.1
Alternative name(s):
    CYPIIC5
    P450 1
    Progesterone 21-hydroxylase
    P450IIC5

Gene names

Name:

CYP2C5

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

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

Hide | Top

Protein attributes

Sequence length	487 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

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 + O(2) = ROH + oxidized flavoprotein + H(2)O.
Cofactor	Heme group.
Subcellular location	Endoplasmic reticulum membraneBy similarity. Microsome membraneBy similarity.
Induction	P450 can be induced to high levels in liver and other tissues by various foreign compounds, including drugs, pesticides, and carcinogens.
Miscellaneous	This protein differs from other forms of cytochrome P450 in that it catalyzes the 21-hydroxylation of progesterone, resulting in the formation of deoxycorticosterone.
Sequence similarities	Belongs to the cytochrome P450 family.

Hide | Top

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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 unspecific monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 487

487

Cytochrome P450 2C5

PRO_0000051696

Sites

Metal binding

432

Iron (heme axial ligand)

Experimental info

Sequence conflict

R → T in AAA31209. Ref.1

Sequence conflict

252

Q → E in AAA31209. Ref.1

Secondary structure

487

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P00179-1 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: ED67B2E255DF5EA0
Show »

FASTA

487

55,275

        10         20         30         40         50         60 
MDPVVVLVLG LCCLLLLSIW KQNSGRGKLP PGPTPFPIIG NILQIDAKDI SKSLTKFSEC 

        70         80         90        100        110        120 
YGPVFTVYLG MKPTVVLHGY EAVKEALVDL GEEFAGRGSV PILEKVSKGL GIAFSNAKTW 

       130        140        150        160        170        180 
KEMRRFSLMT LRNFGMGKRS IEDRIQEEAR CLVEELRKTN ASPCDPTFIL GCAPCNVICS 

       190        200        210        220        230        240 
VIFHNRFDYK DEEFLKLMES LNENVRILSS PWLQVYNNFP ALLDYFPGIH KTLLKNADYI 

       250        260        270        280        290        300 
KNFIMEKVKE HQKLLDVNNP RDFIDCFLIK MEQENNLEFT LESLVIAVSD LFGAGTETTS 

       310        320        330        340        350        360 
TTLRYSLLLL LKHPEVAARV QEEIERVIGR HRSPCMQDRS RMPYTDAVIH EIQRFIDLLP 

       370        380        390        400        410        420 
TNLPHAVTRD VRFRNYFIPK GTDIITSLTS VLHDEKAFPN PKVFDPGHFL DESGNFKKSD 

       430        440        450        460        470        480 
YFMPFSAGKR MCVGEGLARM ELFLFLTSIL QNFKLQSLVE PKDLDITAVV NGFVSVPPSY 


QLCFIPI

« Hide

Hide | Top

References

[1]	"Multiple gene-like sequences related to the rabbit hepatic progesterone 21-hydroxylase cytochrome P-450 1." Tukey R.H., Okino S., Barnes H.J., Griffin K.J., Johnson E.F. J. Biol. Chem. 260:13347-13354(1985) [PubMed: 3902818] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Tukey R.H. Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 252.
[3]	"Characterization of the CYP2C5 gene in 21L III/J rabbits. Allelic variation affects the expression of P450IIC5." Pendurthi U.R., Lamb J.G., Nguyen N., Johnson E.F., Tukey R.H. J. Biol. Chem. 265:14662-14668(1990) [PubMed: 2387874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: III/J. Tissue: Liver.
[4]	"Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity." Williams P.A., Cosme J., Sridhar V., Johnson E.F., McRee D.E. Mol. Cell 5:121-131(2000) [PubMed: 10678174] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[5]	"Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 A resolution: evidence for multiple substrate binding modes." Wester M.R., Johnson E.F., Marques-Soares C., Dansette P.M., Mansuy D., Stout C.D. Biochemistry 42:6370-6379(2003) [PubMed: 12767218] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

M11299 mRNA. Translation: AAA31209.1.
M55664 mRNA. Translation: AAA63461.1.

PIR

O4RBP4. A00180.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DT6	X-ray	3.00	A	27-487	[»]
1N6B	X-ray	2.30	A	27-487	[»]
1NR6	X-ray	2.10	A	27-487	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSOCUG00000014206. Oryctolagus cuniculus. [Contig view]

Phylogenomic databases

HOVERGEN

P00179.

Family and domain databases

InterPro

IPR001128. Cyt_P450.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]

Gene3D

G3DSA:1.10.630.10. Cyt_P450. 1 hit.

PANTHER

PTHR19383. Cyt_P450. 1 hit.

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00463. EP450I.
PR00385. P450.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P00179.

Hide | Top

Entry information

Entry name

CP2C5_RABIT

Accession

Primary (citable) accession number: P00179
Secondary accession number(s): Q29511

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	September 5, 2006
Last modified:	November 25, 2008
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other Resources

Entry information

Relevant documents