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Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

PPIA

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

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
Cleaved into the following chain:
Gene namesi
Name:PPIA
Synonyms:CYPA
OrganismiMacaca mulatta (Rhesus macaque)
Taxonomic identifieri9544 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
Proteomesi
  • UP000006718 Componenti: Chromosome 3

Subcellular locationi

  • Cytoplasm By similarity
  • 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000641161 – 165Peptidyl-prolyl cis-trans isomerase AAdd BLAST165
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00004232442 – 165Peptidyl-prolyl cis-trans isomerase A, N-terminally processedAdd BLAST164

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 ubiquitin); alternateBy similarity
Modified residuei44N6-acetyllysineBy similarity1
Modified residuei76N6-acetyllysineBy similarity1
Modified residuei77PhosphoserineBy similarity1
Modified residuei82N6-acetyllysineBy similarity1
Modified residuei93PhosphothreonineBy similarity1
Glycosylationi108N-linked (GlcNAc...)Sequence 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

Expressioni

Gene expression databases

BgeeiENSMMUG00000016638.
ExpressionAtlasiP62940. differential.

Interactioni

Protein-protein interaction databases

DIPiDIP-48565N.
STRINGi9544.ENSMMUP00000021879.

Structurei

Secondary structure

1165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 12Combined sources8
Beta strandi15 – 24Combined sources10
Turni26 – 28Combined sources3
Helixi30 – 41Combined sources12
Turni42 – 44Combined sources3
Beta strandi55 – 57Combined sources3
Turni58 – 60Combined sources3
Beta strandi61 – 64Combined sources4
Beta strandi72 – 74Combined sources3
Beta strandi97 – 100Combined sources4
Beta strandi102 – 104Combined sources3
Beta strandi112 – 117Combined sources6
Helixi120 – 122Combined sources3
Turni123 – 125Combined sources3
Beta strandi128 – 132Combined sources5
Helixi136 – 143Combined sources8
Beta strandi156 – 163Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WLWX-ray1.50A1-165[»]
4DGAX-ray1.90A/B1-165[»]
4DGBX-ray1.70A1-165[»]
4DGCX-ray2.65A/B/C/D/E1-165[»]
4DGDX-ray1.40A1-165[»]
4DGEX-ray2.20A/B1-165[»]
ProteinModelPortaliP62940.
SMRiP62940.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62940.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOVERGENiHBG001065.
InParanoidiP62940.
KOiK03767.
OMAiMRSAFFQ.
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.

P62940-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG
60 70 80 90 100
SCFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM
110 120 130 140 150
ANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG
160
KTSKKITIAD CGQLE
Length:165
Mass (Da):18,012
Last modified:January 23, 2007 - v2
Checksum:i9B2E637A555E4434
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023861 mRNA. Translation: AAB81961.1.
DQ251283 Genomic DNA. Translation: ABB77883.1.
RefSeqiNP_001027981.1. NM_001032809.1.
UniGeneiMmu.19758.

Genome annotation databases

EnsembliENSMMUT00000023383; ENSMMUP00000021879; ENSMMUG00000016638.
GeneIDi574102.
KEGGimcc:574102.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023861 mRNA. Translation: AAB81961.1.
DQ251283 Genomic DNA. Translation: ABB77883.1.
RefSeqiNP_001027981.1. NM_001032809.1.
UniGeneiMmu.19758.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WLWX-ray1.50A1-165[»]
4DGAX-ray1.90A/B1-165[»]
4DGBX-ray1.70A1-165[»]
4DGCX-ray2.65A/B/C/D/E1-165[»]
4DGDX-ray1.40A1-165[»]
4DGEX-ray2.20A/B1-165[»]
ProteinModelPortaliP62940.
SMRiP62940.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48565N.
STRINGi9544.ENSMMUP00000021879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMMUT00000023383; ENSMMUP00000021879; ENSMMUG00000016638.
GeneIDi574102.
KEGGimcc:574102.

Organism-specific databases

CTDi5478.

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOVERGENiHBG001065.
InParanoidiP62940.
KOiK03767.
OMAiMRSAFFQ.
TreeFamiTF316719.

Miscellaneous databases

EvolutionaryTraceiP62940.
PROiP62940.

Gene expression databases

BgeeiENSMMUG00000016638.
ExpressionAtlasiP62940. differential.

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...

Entry informationi

Entry nameiPPIA_MACMU
AccessioniPrimary (citable) accession number: P62940
Secondary accession number(s): P05092
, Q0ZQK4, Q96IX3, Q9BRU4, Q9BTY9, Q9UC61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 102 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.