P30412 (PPIC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › 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

1

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212

Helix Strand Turn

Details...

Beta strand

35 – 46

12

Beta strand

49 – 58

10

Turn

60 – 62

3

Helix

64 – 75

12

Turn

76 – 78

3

Beta strand

86 – 91

6

Turn

92 – 94

3

Beta strand

95 – 98

4

Beta strand

102 – 107

6

Beta strand

131 – 134

4

Beta strand

136 – 138

3

Beta strand

146 – 151

6

Helix

154 – 156

3

Turn

157 – 159

3

Beta strand

162 – 168

7

Helix

170 – 177

8

Beta strand

187 – 189

3

Beta strand

191 – 206

16

Sequences

	Sequence		Length	Mass (Da)
	P30412 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: C99E7AA5D0FA04B6	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

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.

IPI

IPI00130240.

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...

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.

KO

K09563.

OMA

YGYKGSR.

OrthoDB

EOG7RFTK4.

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:	November 13, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program