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P00179

- CP2C5_RABIT

UniProt

P00179 - CP2C5_RABIT

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Protein

Cytochrome P450 2C5

Gene

CYP2C5

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.

Cofactori

Heme group.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi432 – 4321Iron (heme axial ligand)

GO - Molecular functioni

  1. aromatase activity Source: UniProtKB-EC
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

SABIO-RKP00179.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 2C5 (EC:1.14.14.1)
Alternative name(s):
CYPIIC5
Cytochrome P450 1
Cytochrome P450IIC5
Progesterone 21-hydroxylase
Gene namesi
Name:CYP2C5
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Chromosome 18

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 487487Cytochrome P450 2C5PRO_0000051696Add
BLAST

Expressioni

Inductioni

P450 can be induced to high levels in liver and other tissues by various foreign compounds, including drugs, pesticides, and carcinogens.

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000020892.

Structurei

Secondary structure

1
487
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni37 – 393
Helixi42 – 443
Helixi50 – 6112
Beta strandi63 – 7715
Helixi80 – 878
Turni88 – 947
Beta strandi95 – 973
Helixi103 – 1075
Beta strandi111 – 1144
Helixi117 – 13014
Turni133 – 1364
Beta strandi137 – 1393
Helixi141 – 15717
Turni158 – 1614
Helixi167 – 18317
Helixi192 – 20716
Helixi214 – 2174
Helixi220 – 2256
Helixi227 – 25428
Helixi263 – 27210
Beta strandi273 – 2753
Helixi281 – 31232
Helixi314 – 32714
Beta strandi330 – 3323
Helixi336 – 3416
Helixi343 – 35614
Beta strandi371 – 3733
Beta strandi376 – 3783
Beta strandi383 – 3864
Helixi388 – 3925
Turni395 – 3973
Beta strandi398 – 4003
Helixi406 – 4094
Beta strandi412 – 4154
Helixi428 – 4303
Helixi435 – 45218
Beta strandi453 – 4597
Helixi461 – 4633
Beta strandi472 – 4765
Beta strandi482 – 4865

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DT6X-ray3.00A22-487[»]
1N6BX-ray2.30A19-487[»]
1NR6X-ray2.10A19-487[»]
ProteinModelPortaliP00179.
SMRiP00179. Positions 27-487.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00179.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000118775.
HOGENOMiHOG000036992.
HOVERGENiHBG015789.
InParanoidiP00179.
OMAiHDNTEFP.
OrthoDBiEOG7RBZ85.
TreeFamiTF352043.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00179-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDPVVVLVLG LCCLLLLSIW KQNSGRGKLP PGPTPFPIIG NILQIDAKDI
60 70 80 90 100
SKSLTKFSEC YGPVFTVYLG MKPTVVLHGY EAVKEALVDL GEEFAGRGSV
110 120 130 140 150
PILEKVSKGL GIAFSNAKTW KEMRRFSLMT LRNFGMGKRS IEDRIQEEAR
160 170 180 190 200
CLVEELRKTN ASPCDPTFIL GCAPCNVICS VIFHNRFDYK DEEFLKLMES
210 220 230 240 250
LNENVRILSS PWLQVYNNFP ALLDYFPGIH KTLLKNADYI KNFIMEKVKE
260 270 280 290 300
HQKLLDVNNP RDFIDCFLIK MEQENNLEFT LESLVIAVSD LFGAGTETTS
310 320 330 340 350
TTLRYSLLLL LKHPEVAARV QEEIERVIGR HRSPCMQDRS RMPYTDAVIH
360 370 380 390 400
EIQRFIDLLP TNLPHAVTRD VRFRNYFIPK GTDIITSLTS VLHDEKAFPN
410 420 430 440 450
PKVFDPGHFL DESGNFKKSD YFMPFSAGKR MCVGEGLARM ELFLFLTSIL
460 470 480
QNFKLQSLVE PKDLDITAVV NGFVSVPPSY QLCFIPI
Length:487
Mass (Da):55,275
Last modified:September 5, 2006 - v2
Checksum:iED67B2E255DF5EA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971R → T in AAA31209. (PubMed:3902818)Curated
Sequence conflicti252 – 2521Q → E in AAA31209. (PubMed:3902818)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11299 mRNA. Translation: AAA31209.1.
M55664 mRNA. Translation: AAA63461.1.
PIRiA00180. O4RBP4.
RefSeqiNP_001164397.1. NM_001170926.1.
UniGeneiOcu.1857.

Genome annotation databases

EnsembliENSOCUT00000021366; ENSOCUP00000020892; ENSOCUG00000021501.
GeneIDi100328549.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11299 mRNA. Translation: AAA31209.1 .
M55664 mRNA. Translation: AAA63461.1 .
PIRi A00180. O4RBP4.
RefSeqi NP_001164397.1. NM_001170926.1.
UniGenei Ocu.1857.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DT6 X-ray 3.00 A 22-487 [» ]
1N6B X-ray 2.30 A 19-487 [» ]
1NR6 X-ray 2.10 A 19-487 [» ]
ProteinModelPortali P00179.
SMRi P00179. Positions 27-487.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000020892.

Chemistry

ChEMBLi CHEMBL1907985.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSOCUT00000021366 ; ENSOCUP00000020892 ; ENSOCUG00000021501 .
GeneIDi 100328549.

Organism-specific databases

CTDi 100328549.

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00760000118775.
HOGENOMi HOG000036992.
HOVERGENi HBG015789.
InParanoidi P00179.
OMAi HDNTEFP.
OrthoDBi EOG7RBZ85.
TreeFami TF352043.

Enzyme and pathway databases

SABIO-RK P00179.

Miscellaneous databases

EvolutionaryTracei P00179.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00463. EP450I.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.

Entry informationi

Entry nameiCP2C5_RABIT
AccessioniPrimary (citable) accession number: P00179
Secondary accession number(s): Q29511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 5, 2006
Last modified: October 29, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3