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Protein

Peptidyl-prolyl cis-trans isomerase C

Gene

Ppic

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Cyclosporin A (CsA) inhibits CYPC.

GO - Molecular functioni

  1. cyclosporin A binding Source: MGI
  2. peptidyl-prolyl cis-trans isomerase activity Source: GO_Central

GO - Biological processi

  1. protein folding Source: InterPro
  2. protein peptidyl-prolyl isomerization Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase C (EC:5.2.1.8)
Short name:
PPIase C
Alternative name(s):
Cyclophilin C
Rotamase C
Gene namesi
Name:Ppic
Synonyms:Cypc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:97751. Ppic.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Peptidyl-prolyl cis-trans isomerase CPRO_0000064148Add
BLAST

Proteomic databases

MaxQBiP30412.
PaxDbiP30412.
PRIDEiP30412.

2D gel databases

REPRODUCTION-2DPAGEIPI00130240.

PTM databases

PhosphoSiteiP30412.

Expressioni

Gene expression databases

BgeeiP30412.
CleanExiMM_PPIC.
ExpressionAtlasiP30412. baseline and differential.
GenevestigatoriP30412.

Interactioni

Protein-protein interaction databases

IntActiP30412. 3 interactions.
MINTiMINT-4108440.
STRINGi10090.ENSMUSP00000025419.

Structurei

Secondary structure

1
212
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 4612Combined sources
Beta strandi49 – 5810Combined sources
Turni60 – 623Combined sources
Helixi64 – 7512Combined sources
Turni76 – 783Combined sources
Beta strandi86 – 916Combined sources
Turni92 – 943Combined sources
Beta strandi95 – 984Combined sources
Beta strandi102 – 1076Combined sources
Beta strandi131 – 1344Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi146 – 1516Combined sources
Helixi154 – 1563Combined sources
Turni157 – 1593Combined sources
Beta strandi162 – 1687Combined sources
Helixi170 – 1778Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi191 – 20616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RMCX-ray1.64A/C/E/G31-212[»]
ProteinModelPortaliP30412.
SMRiP30412. Positions 31-212.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30412.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 198158PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cyclophilin-type PPIase family.Curated
Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0652.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP30412.
KOiK09563.
OMAiDRPLTNC.
OrthoDBiEOG7RFTK4.
PhylomeDBiP30412.
TreeFamiTF354259.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPGPRLLLP AVLCLGLGAL VSSSGSSGVR KRGPSVTDKV FFDVRIGDKD
60 70 80 90 100
VGRIVIGLFG NVVPKTVENF VALATGEKGY GYKGSIFHRV IKDFMIQGGD
110 120 130 140 150
FTARDGTGGM SIYGETFPDE NFKLKHYGIG WVSMANAGPD TNGSQFFITL
160 170 180 190 200
TKPTWLDGKH VVFGKVLDGM TVVHSIELQA TDGHDRPLTD CTIVNSGKID
210
VKTPFVVEVP DW
Length:212
Mass (Da):22,794
Last modified:April 1, 1993 - v1
Checksum:iC99E7AA5D0FA04B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74227 mRNA. Translation: AAA37511.1.
BC025861 mRNA. Translation: AAH25861.1.
CCDSiCCDS29252.1.
PIRiA40047.
RefSeqiNP_032934.1. NM_008908.4.
UniGeneiMm.4587.

Genome annotation databases

EnsembliENSMUST00000025419; ENSMUSP00000025419; ENSMUSG00000024538.
GeneIDi19038.
KEGGimmu:19038.
UCSCiuc008exu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74227 mRNA. Translation: AAA37511.1.
BC025861 mRNA. Translation: AAH25861.1.
CCDSiCCDS29252.1.
PIRiA40047.
RefSeqiNP_032934.1. NM_008908.4.
UniGeneiMm.4587.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RMCX-ray1.64A/C/E/G31-212[»]
ProteinModelPortaliP30412.
SMRiP30412. Positions 31-212.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP30412. 3 interactions.
MINTiMINT-4108440.
STRINGi10090.ENSMUSP00000025419.

PTM databases

PhosphoSiteiP30412.

2D gel databases

REPRODUCTION-2DPAGEIPI00130240.

Proteomic databases

MaxQBiP30412.
PaxDbiP30412.
PRIDEiP30412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025419; ENSMUSP00000025419; ENSMUSG00000024538.
GeneIDi19038.
KEGGimmu:19038.
UCSCiuc008exu.1. mouse.

Organism-specific databases

CTDi5480.
MGIiMGI:97751. Ppic.

Phylogenomic databases

eggNOGiCOG0652.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP30412.
KOiK09563.
OMAiDRPLTNC.
OrthoDBiEOG7RFTK4.
PhylomeDBiP30412.
TreeFamiTF354259.

Miscellaneous databases

ChiTaRSiPpic. mouse.
EvolutionaryTraceiP30412.
NextBioi295481.
PROiP30412.
SOURCEiSearch...

Gene expression databases

BgeeiP30412.
CleanExiMM_PPIC.
ExpressionAtlasiP30412. baseline and differential.
GenevestigatoriP30412.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: one in the presence and one in the absence of CsA."
    Friedman J., Weissman I.L.
    Cell 66:799-806(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. "Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin A."
    Ke H., Zhao Y., Luo F., Weissman I.L., Friedman J.
    Proc. Natl. Acad. Sci. U.S.A. 90:11850-11854(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN COMPLEX WITH CSA.

Entry informationi

Entry nameiPPIC_MOUSE
AccessioniPrimary (citable) accession number: P30412
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 1, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.