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UniProtKB/Swiss-Prot entry P00179


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CP2C5_RABIT
Primary accession number P00179
Secondary accession number Q29511
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on September 5, 2006 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 74)
Name and origin of the protein
Protein name Cytochrome P450 2C5
Synonyms EC 1.14.14.1
CYPIIC5
P450 1
Progesterone 21-hydroxylase
P450IIC5
Gene name
Name: CYP2C5
From
Oryctolagus cuniculus (Rabbit) [TaxID: 9986] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3902818 [NCBI, ExPASy, EBI, Israel, Japan]
Tukey R.H., Okino S., Barnes H.J., Griffin K.J., Johnson E.F.;
"Multiple gene-like sequences related to the rabbit hepatic progesterone 21-hydroxylase cytochrome P-450 1.";
J. Biol. Chem. 260:13347-13354(1985).
[2]
SEQUENCE REVISION TO 252.
Tukey R.H.;
Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=III/J;
TISSUE=Liver;
PubMed=2387874 [NCBI, ExPASy, EBI, Israel, Japan]
Pendurthi U.R., Lamb J.G., Nguyen N., Johnson E.F., Tukey R.H.;
"Characterization of the CYP2C5 gene in 21L III/J rabbits. Allelic variation affects the expression of P450IIC5.";
J. Biol. Chem. 265:14662-14668(1990).
[4]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
DOI=10.1016/S1097-2765(00)80408-6; PubMed=10678174 [NCBI, ExPASy, EBI, Israel, Japan]
Williams P.A., Cosme J., Sridhar V., Johnson E.F., McRee D.E.;
"Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity.";
Mol. Cell 5:121-131(2000).
[5]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
DOI=10.1021/bi0273922; PubMed=12767218 [NCBI, ExPASy, EBI, Israel, Japan]
Wester M.R., Johnson E.F., Marques-Soares C., Dansette P.M., Mansuy D., Stout C.D.;
"Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 A resolution: evidence for multiple substrate binding modes.";
Biochemistry 42:6370-6379(2003).
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.
  • SUBCELLULAR LOCATION: Endoplasmic reticulum membrane (By similarity). Microsome membrane (By 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.
  • SIMILARITY: Belongs to the cytochrome P450 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M11299; AAA31209.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55664; AAA63461.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00180; O4RBP4.
3D structure databases
PDB
1DT6; X-ray; 3.00 A; A=27-487.[ExPASy / RCSB / EBI]
1N6B; X-ray; 2.30 A; A=27-487.[ExPASy / RCSB / EBI]
1NR6; X-ray; 2.10 A; A=27-487.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DT6; -.
1N6B; -.
1NR6; -.
ModBase P00179.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005792; Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0050381; Molecular function: unspecific monooxygenase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.
Gene3D G3DSA:1.10.630.10; Cyt_P450; 1.
PANTHER PTHR19383; Cyt_P450; 1.
Pfam PF00067; p450; 1.
Pfam graphical view of domain structure.
PRINTS PR00463; EP450I.
PR00385; P450.
PROSITE PS00086; CYTOCHROME_P450; 1.
Genome annotation databases
Ensembl ENSOCUG00000014206; Oryctolagus cuniculus. [Contig view]
Phylogenomic databases
HOVERGEN P00179; -.
Other
LinkHub P00179; -.
ProtoNet P00179.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   487  487     Cytochrome P450 2C5. PRO_0000051696
METAL   432   432        Iron (heme axial ligand). 
CONFLICT   97    97        R -> T (in Ref. 1; AAA31209). 
CONFLICT   252   252        Q -> E (in Ref. 1; AAA31209). 
TURN   37    41  5      
HELIX   42    44  3      
HELIX   50    61  12      
STRAND   63    71  9      
STRAND   73    79  7      
HELIX   80    87  8      
TURN   88    90  3      
HELIX   91    94  4      
STRAND   95    97  3      
HELIX   101   106  6      
TURN   107   109  3      
STRAND   111   114  4      
HELIX   117   130  14      
STRAND   135   139  5      
HELIX   141   157  17      
TURN   158   161  4      
TURN   166   168  3      
HELIX   169   183  15      
HELIX   192   208  17      
HELIX   215   218  4      
HELIX   221   225  5      
HELIX   227   253  27      
HELIX   263   270  8      
STRAND   272   274  3      
HELIX   281   312  32      
HELIX   314   327  14      
TURN   328   331  4      
HELIX   337   340  4      
HELIX   343   356  14      
STRAND   371   373  3      
STRAND   376   378  3      
STRAND   383   387  5      
HELIX   388   392  5      
TURN   395   397  3      
STRAND   398   400  3      
HELIX   406   409  4      
HELIX   435   452  18      
STRAND   453   456  4      
HELIX   461   463  3      
STRAND   472   476  5      
STRAND   482   486  5      
Sequence information
Length: 487 AA [This is the length of the unprocessed precursor] Molecular weight: 55275 Da [This is the MW of the unprocessed precursor] CRC64: ED67B2E255DF5EA0 [This is a checksum on the sequence]
        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 

P00179 in FASTA format

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