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Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

Ppia

Organism
Rattus norvegicus (Rat)
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

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

ReactomeiR-RNO-210991. Basigin interactions.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi3372. Ppia.

Subcellular locationi

  • Cytoplasm
  • Secreted By similarity

  • Note: Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, and mediates ERK1/2 activation.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2780.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Peptidyl-prolyl cis-trans isomerase APRO_0000423252Add
BLAST
Initiator methionineiRemoved; alternate3 Publications
Chaini2 – 164163Peptidyl-prolyl cis-trans isomerase A, N-terminally processedPRO_0000064121Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylvaline; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed1 Publication
Modified residuei28 – 281N6-acetyllysine; alternateBy similarity
Cross-linki28 – 28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei44 – 441N6-acetyllysineBy similarity
Modified residuei76 – 761N6-acetyllysineBy similarity
Modified residuei82 – 821N6-acetyllysineBy similarity
Modified residuei93 – 931PhosphothreonineBy similarity
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence analysis
Modified residuei125 – 1251N6-acetyllysineBy similarity
Modified residuei131 – 1311N6-acetyllysineBy similarity
Modified residuei133 – 1331N6-acetyllysineBy similarity

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-2DPAGE0004:P10111.

PTM databases

iPTMnetiP10111.
PhosphoSiteiP10111.

Expressioni

Gene expression databases

ExpressionAtlasiP10111. baseline.
GenevisibleiP10111. RN.

Interactioni

Protein-protein interaction databases

BioGridi247550. 2 interactions.
IntActiP10111. 1 interaction.
MINTiMINT-4566039.
STRINGi10116.ENSRNOP00000009407.

Chemistry

BindingDBiP10111.

Structurei

3D structure databases

ProteinModelPortaliP10111.
SMRiP10111. Positions 1-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 163157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP10111.
KOiK03767.
OMAiQGVPLHF.
OrthoDBiEOG79GT7W.
PhylomeDBiP10111.
TreeFamiTF316719.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

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_006250801.2.
UniGeneiRn.1463.

Genome annotation databases

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

Cross-referencesi

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_006250801.2.
UniGeneiRn.1463.

3D structure databases

ProteinModelPortaliP10111.
SMRiP10111. Positions 1-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247550. 2 interactions.
IntActiP10111. 1 interaction.
MINTiMINT-4566039.
STRINGi10116.ENSRNOP00000009407.

Chemistry

BindingDBiP10111.
ChEMBLiCHEMBL2780.

PTM databases

iPTMnetiP10111.
PhosphoSiteiP10111.

2D gel databases

World-2DPAGE0004:P10111.

Proteomic databases

PaxDbiP10111.
PRIDEiP10111.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5478.
RGDi3372. Ppia.

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP10111.
KOiK03767.
OMAiQGVPLHF.
OrthoDBiEOG79GT7W.
PhylomeDBiP10111.
TreeFamiTF316719.

Enzyme and pathway databases

ReactomeiR-RNO-210991. Basigin interactions.

Miscellaneous databases

PROiP10111.

Gene expression databases

ExpressionAtlasiP10111. baseline.
GenevisibleiP10111. RN.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Molecular cloning and regional distribution of rat brain cyclophilin."
    Lad R.P., Smith M.A., Hilt D.C.
    Brain Res. Mol. Brain Res. 9:239-244(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "P31, a mammalian housekeeping protein encoded by a multigene family containing a high proportion of pseudogenes."
    Theodor L., Peleg D., Meyuhas O.
    Biochim. Biophys. Acta 826:137-146(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sabra.
  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: Ovary and Pituitary.
  5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-31; 56-69; 77-125; 132-144 AND 155-164, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  6. "Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin."
    Connern C.P., Halestrap A.P.
    Biochem. J. 284:381-385(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-29.
    Tissue: Liver.
  7. Lubec G., Chen W.-Q.
    Submitted (FEB-2007) to UniProtKB
    Cited for: ACETYLATION AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPPIA_RAT
AccessioniPrimary (citable) accession number: P10111
Secondary accession number(s): P18303, Q5BK98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 149 of the entry and version 2 of the sequence. [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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.