Peptidyl-prolyl cis-trans isomerase C

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P30412 (PPIC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 112. History...

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

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	212 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	peptide 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 212

212

Peptidyl-prolyl cis-trans isomerase C

PRO_0000064148

Regions

Domain

41 – 198

158

PPIase cyclophilin-type

Secondary structure

212

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P30412 [UniParc].

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

FASTA

212

22,794

        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' referencesShow '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.

PIR

A40047.

RefSeq

NP_032934.1. NM_008908.4.

UniGene

Mm.4587.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RMC	X-ray	1.64	A/C/E/G	31-212	[»]

ProteinModelPortal

P30412.

SMR

P30412. Positions 31-212.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

IntAct

P30412. 3 interactions.

MINT

MINT-4108440.

STRING

10090.ENSMUSP00000025419.

PTM databases

PhosphoSite

P30412.

2D gel databases

REPRODUCTION-2DPAGE

IPI00130240.

Proteomic databases

PaxDb

P30412.

PRIDE

P30412.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000025419; ENSMUSP00000025419; ENSMUSG00000024538.

GeneID

19038.

KEGG

mmu:19038.

UCSC

uc008exu.1. mouse.

Organism-specific databases

CTD

5480.

MGI

MGI:97751. Ppic.

Phylogenomic databases

eggNOG

COG0652.

HOGENOM

HOG000065981.

HOVERGEN

HBG001065.

InParanoid

P30412.

K09563.

OMA

YGYKGSR.

OrthoDB

EOG7RFTK4.

TreeFam

TF354259.

Gene expression databases

ArrayExpress

P30412.

Bgee

P30412.

CleanEx

MM_PPIC.

Genevestigator

P30412.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PIRSF

PIRSF001467. Peptidylpro_ismrse. 1 hit.

PRINTS

PR00153. CSAPPISMRASE.

SUPFAM

SSF50891. SSF50891. 1 hit.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PPIC. mouse.

EvolutionaryTrace

P30412.

NextBio

295481.

PRO

P30412.

SOURCE

Search...

Entry information

Entry name

PPIC_MOUSE

Accession

Primary (citable) accession number: P30412

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	February 19, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents