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P45877 (PPIC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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
   Coding sequence diversityPolymorphism
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction

Traceable author statement PubMed 1652374. Source: ProtInc

   Cellular_componentcytoplasm

Traceable author statement PubMed 1652374. Source: ProtInc

   Molecular_functioncyclosporin A binding

Traceable author statement PubMed 1652374. Source: ProtInc

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

unfolded protein binding

Traceable author statement PubMed 1652374. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Peptidyl-prolyl cis-trans isomerase C
PRO_0000064147

Regions

Domain41 – 198158PPIase cyclophilin-type

Natural variations

Natural variant861K → R. Ref.2
Corresponds to variant rs34341374 [ dbSNP | Ensembl ].
VAR_051770
Natural variant1601H → L. Ref.2
VAR_060712
Natural variant1901N → S. Ref.2
Corresponds to variant rs451195 [ dbSNP | Ensembl ].
VAR_024319

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P45877 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 6F3DB547A2AE581B

FASTA21222,763
        10         20         30         40         50         60 
MGPGPRLLLP LVLCVGLGAL VFSSGAEGFR KRGPSVTAKV FFDVRIGDKD VGRIVIGLFG 

        70         80         90        100        110        120 
KVVPKTVENF VALATGEKGY GYKGSKFHRV IKDFMIQGGD ITTGDGTGGV SIYGETFPDE 

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

       190        200        210 
TDGHDRPLTN CSIINSGKID VKTPFVVEIA DW 

« Hide

References

« Hide 'large scale' references
[1]"Human cyclophilin C: primary structure, tissue distribution, and determination of binding specificity for cyclosporins."
Schneider H., Charara N., Schmitz R., Wehrli S., Mikol V., Zurini M.G., Quesniaux V.F., Movva N.R.
Biochemistry 33:8218-8224(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIEHS SNPs program
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-86; LEU-160 AND SER-190.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Uterus.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S71018 mRNA. Translation: AAB31350.1.
EF506885 Genomic DNA. Translation: ABO43038.1.
CH471086 Genomic DNA. Translation: EAW48878.1.
BC002678 mRNA. Translation: AAH02678.1.
PIRA54204.
RefSeqNP_000934.1. NM_000943.4.
UniGeneHs.110364.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ESLX-ray1.90A/B/C/D/E/F24-212[»]
ProteinModelPortalP45877.
SMRP45877. Positions 32-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111476. 5 interactions.
IntActP45877. 2 interactions.
MINTMINT-2861873.
STRING9606.ENSP00000303057.

Chemistry

DrugBankDB00172. L-Proline.

PTM databases

PhosphoSiteP45877.

Polymorphism databases

DMDM1169178.

Proteomic databases

PaxDbP45877.
PRIDEP45877.

Protocols and materials databases

DNASU5480.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306442; ENSP00000303057; ENSG00000168938.
GeneID5480.
KEGGhsa:5480.
UCSCuc003kth.3. human.

Organism-specific databases

CTD5480.
GeneCardsGC05M122363.
HGNCHGNC:9256. PPIC.
HPAHPA039163.
MIM123842. gene.
neXtProtNX_P45877.
PharmGKBPA33581.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065981.
HOVERGENHBG001065.
InParanoidP45877.
KOK09563.
OMALTDCVIT.
OrthoDBEOG7RFTK4.
PhylomeDBP45877.
TreeFamTF354259.

Gene expression databases

BgeeP45877.
CleanExHS_PPIC.
GenevestigatorP45877.

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. human.
EvolutionaryTraceP45877.
GeneWikiPPIC.
GenomeRNAi5480.
NextBio21214.
PROP45877.
SOURCESearch...

Entry information

Entry namePPIC_HUMAN
AccessionPrimary (citable) accession number: P45877
Secondary accession number(s): A4LBB5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM