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P30412 (PPIC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase C

Short name=PPIase C
EC=5.2.1.8
Alternative name(s):
Cyclophilin C
Rotamase C
Gene names
Name:Ppic
Synonyms:Cypc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Cyclosporin A (CsA) inhibits CYPC.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Peptidyl-prolyl cis-trans isomerase C
PRO_0000064148

Regions

Domain41 – 198158PPIase cyclophilin-type

Secondary structure

................................. 212
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30412 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: C99E7AA5D0FA04B6

FASTA21222,794
        10         20         30         40         50         60 
MSPGPRLLLP AVLCLGLGAL VSSSGSSGVR KRGPSVTDKV FFDVRIGDKD VGRIVIGLFG 

        70         80         90        100        110        120 
NVVPKTVENF VALATGEKGY GYKGSIFHRV IKDFMIQGGD FTARDGTGGM SIYGETFPDE 

       130        140        150        160        170        180 
NFKLKHYGIG WVSMANAGPD TNGSQFFITL TKPTWLDGKH VVFGKVLDGM TVVHSIELQA 

       190        200        210 
TDGHDRPLTD CTIVNSGKID VKTPFVVEVP DW 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74227 mRNA. Translation: AAA37511.1.
BC025861 mRNA. Translation: AAH25861.1.
PIRA40047.
RefSeqNP_032934.1. NM_008908.4.
UniGeneMm.4587.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RMCX-ray1.64A/C/E/G31-212[»]
ProteinModelPortalP30412.
SMRP30412. Positions 31-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP30412. 3 interactions.
MINTMINT-4108440.
STRING10090.ENSMUSP00000025419.

PTM databases

PhosphoSiteP30412.

2D gel databases

REPRODUCTION-2DPAGEIPI00130240.

Proteomic databases

PaxDbP30412.
PRIDEP30412.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025419; ENSMUSP00000025419; ENSMUSG00000024538.
GeneID19038.
KEGGmmu:19038.
UCSCuc008exu.1. mouse.

Organism-specific databases

CTD5480.
MGIMGI:97751. Ppic.

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065981.
HOVERGENHBG001065.
InParanoidP30412.
KOK09563.
OMAYGYKGSR.
OrthoDBEOG7RFTK4.
PhylomeDBP30412.
TreeFamTF354259.

Gene expression databases

ArrayExpressP30412.
BgeeP30412.
CleanExMM_PPIC.
GenevestigatorP30412.

Family and domain databases

InterProIPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPIC. mouse.
EvolutionaryTraceP30412.
NextBio295481.
PROP30412.
SOURCESearch...

Entry information

Entry namePPIC_MOUSE
AccessionPrimary (citable) accession number: P30412
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot