Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

Ppia

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

  • cyclosporin A binding Source: RGD
  • peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Rotamase

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
p1B15
p31
Cleaved into the following chain:
Gene namesi
Name:Ppia
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi3372 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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2780

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004232521 – 164Peptidyl-prolyl cis-trans isomerase AAdd BLAST164
Initiator methionineiRemoved; alternate3 Publications
ChainiPRO_00000641212 – 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 processed1 Publication1
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 residuei76N6-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 residuei93PhosphothreonineBy similarity1
Glycosylationi108N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei125N6-acetyllysineBy similarity1
Modified residuei131N6-acetyllysineBy similarity1
Modified residuei133N6-acetyllysineBy similarity1

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

PaxDbiP10111
PRIDEiP10111

2D gel databases

World-2DPAGEi0004:P10111

PTM databases

iPTMnetiP10111
PhosphoSitePlusiP10111

Expressioni

Gene expression databases

BgeeiENSRNOG00000027864
ExpressionAtlasiP10111 baseline and differential
GenevisibleiP10111 RN

Interactioni

Subunit structurei

Interacts with protein phosphatase PPP3CA/calcineurin A.By similarity

Protein-protein interaction databases

BioGridi247550, 2 interactors
IntActiP10111, 1 interactor
STRINGi10116.ENSRNOP00000009407

Chemistry databases

BindingDBiP10111

Structurei

3D structure databases

ProteinModelPortaliP10111
SMRiP10111
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
HOGENOMiHOG000065981
HOVERGENiHBG001065
InParanoidiP10111
KOiK03767
OMAiFFINFKD
OrthoDBiEOG091G0BGL
PhylomeDBiP10111
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.

P10111-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNPTVFFDI TADGEPLGRV CFELFADKVP KTAENFRALS TGEKGFGYKG
60 70 80 90 100
SSFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM
110 120 130 140 150
ANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMSIVE AMERFGSRNG
160
KTSKKITISD CGQL
Length:164
Mass (Da):17,874
Last modified:January 23, 2007 - v2
Checksum:i444C1ECF7F12841D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19533 mRNA Translation: AAA41009.1
M25637 mRNA Translation: AAB59719.1
BC059141 mRNA Translation: AAH59141.1
BC091153 mRNA Translation: AAH91153.1
PIRiA29819 CSRTA
RefSeqiNP_058797.1, NM_017101.1
XP_006250863.1, XM_006250801.3
UniGeneiRn.118772
Rn.1463

Genome annotation databases

EnsembliENSRNOT00000088798; ENSRNOP00000071404; ENSRNOG00000055068
ENSRNOT00000091873; ENSRNOP00000073930; ENSRNOG00000027864
GeneIDi100360977
25518
KEGGirno:100360977
rno:25518
UCSCiRGD:3372 rat

Similar proteinsi

Entry informationi

Entry nameiPPIA_RAT
AccessioniPrimary (citable) accession number: P10111
Secondary accession number(s): P18303, Q5BK98
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 166 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health