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Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

Ppia

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Rotamase

Enzyme and pathway databases

ReactomeiR-MMU-210991. Basigin interactions.
R-MMU-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase A (EC:5.2.1.8)
Short name:
PPIase A
Alternative name(s):
Cyclophilin A
Cyclosporin A-binding protein
Rotamase A
SP18
Cleaved into the following chain:
Gene namesi
Name:Ppia
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:97749. Ppia.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004232451 – 164Peptidyl-prolyl cis-trans isomerase AAdd BLAST164
Initiator methionineiRemoved; alternateBy similarity3 Publications
ChainiPRO_00000641172 – 164Peptidyl-prolyl cis-trans isomerase A, N-terminally processedAdd BLAST163

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylvaline; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processedBy similarity1
Modified residuei28N6-acetyllysine; alternateBy similarity1
Cross-linki28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei44N6-acetyllysineBy similarity1
Modified residuei77PhosphoserineBy similarity1
Modified residuei82N6-acetyllysine; alternateBy similarity1
Cross-linki82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei93PhosphothreonineCombined sources1
Glycosylationi108N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei125N6-acetyllysineBy similarity1
Modified residuei131N6-acetyllysineBy similarity1
Modified residuei133N6-acetyllysineCombined sources1

Post-translational modificationi

Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP17742.
PaxDbiP17742.
PeptideAtlasiP17742.
PRIDEiP17742.

2D gel databases

REPRODUCTION-2DPAGEiP17742.
SWISS-2DPAGEiP17742.
UCD-2DPAGEiP17742.

PTM databases

iPTMnetiP17742.
PhosphoSitePlusiP17742.
SwissPalmiP17742.

Expressioni

Gene expression databases

BgeeiENSMUSG00000071866.
CleanExiMM_PPIA.
ExpressionAtlasiP17742. baseline and differential.
GenevisibleiP17742. MM.

Interactioni

Subunit structurei

Interacts with PRPF19 isoform 2 (via N-terminus).1 Publication

Protein-protein interaction databases

BioGridi234487. 8 interactors.
IntActiP17742. 6 interactors.
MINTiMINT-1856608.
STRINGi10090.ENSMUSP00000117987.

Structurei

3D structure databases

ProteinModelPortaliP17742.
SMRiP17742.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 163PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST157

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOVERGENiHBG001065.
InParanoidiP17742.
KOiK03767.
OMAiVPVEPVF.
OrthoDBiEOG091G0BGL.
TreeFamiTF316719.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiView protein in InterPro
IPR029000. Cyclophilin-like_dom_sf.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiView protein in Pfam
PF00160. Pro_isomerase. 1 hit.
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiView protein in PROSITE
PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNPTVFFDI TADDEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG
60 70 80 90 100
SSFHRIIPGF MCQGGDFTRH NGTGGRSIYG EKFEDENFIL KHTGPGILSM
110 120 130 140 150
ANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG
160
KTSKKITISD CGQL
Length:164
Mass (Da):17,971
Last modified:January 23, 2007 - v2
Checksum:i3528824224EA8849
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13 – 14DD → NE in BAB27089 (PubMed:16141072).Curated2
Sequence conflicti18 – 20GRV → TXP AA sequence (PubMed:1565646).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52803 mRNA. Translation: CAA36989.1.
AK002236 mRNA. Translation: BAB21954.1.
AK007981 mRNA. Translation: BAB25387.1.
AK010649 mRNA. Translation: BAB27089.1.
AK012531 mRNA. Translation: BAB28300.1.
AK012663 mRNA. Translation: BAB28392.1.
AK028210 mRNA. Translation: BAC25817.1.
BC083076 mRNA. Translation: AAH83076.1.
AF171073 Genomic DNA. Translation: AAD50996.1.
CCDSiCCDS24419.1.
PIRiS10327. CSMSA.
RefSeqiNP_032933.1. NM_008907.1.
UniGeneiMm.5246.

Genome annotation databases

EnsembliENSMUST00000132846; ENSMUSP00000117987; ENSMUSG00000071866.
GeneIDi268373.
KEGGimmu:268373.
UCSCiuc007hyn.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiPPIA_MOUSE
AccessioniPrimary (citable) accession number: P17742
Secondary accession number(s): Q9CWJ5, Q9R137
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 182 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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