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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
ProteomesiUP000006718 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 165165Peptidyl-prolyl cis-trans isomerase APRO_0000064116Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 165164Peptidyl-prolyl cis-trans isomerase A, N-terminally processedPRO_0000423244Add
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 processedBy similarity
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

PRIDEiP62940.

Expressioni

Gene expression databases

ExpressionAtlasiP62940. baseline.

Interactioni

Protein-protein interaction databases

DIPiDIP-48565N.
STRINGi9544.ENSMMUP00000021879.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Beta strandi15 – 2410Combined sources
Turni26 – 283Combined sources
Helixi30 – 4112Combined sources
Turni42 – 443Combined sources
Beta strandi55 – 573Combined sources
Turni58 – 603Combined sources
Beta strandi61 – 644Combined sources
Beta strandi72 – 743Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi112 – 1176Combined sources
Helixi120 – 1223Combined sources
Turni123 – 1253Combined sources
Beta strandi128 – 1325Combined sources
Helixi136 – 1438Combined sources
Beta strandi156 – 1638Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-165.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62940.

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

eggNOGiCOG0652.
GeneTreeiENSGT00760000119119.
HOVERGENiHBG001065.
InParanoidiP62940.
KOiK03767.
OMAiMRSAFFQ.
OrthoDBiEOG79GT7W.
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
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. Positions 2-165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48565N.
STRINGi9544.ENSMMUP00000021879.

Chemistry

BindingDBiP62940.

Proteomic databases

PRIDEiP62940.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5478.

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119119.
HOVERGENiHBG001065.
InParanoidiP62940.
KOiK03767.
OMAiMRSAFFQ.
OrthoDBiEOG79GT7W.
TreeFamiTF316719.

Miscellaneous databases

EvolutionaryTraceiP62940.
NextBioi19968106.
PROiP62940.

Gene expression databases

ExpressionAtlasiP62940. baseline.

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

  1. Luban J., Yin L.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Patterns of evolution of host proteins involved in retroviral pathogenesis."
    Ortiz M., Bleiber G., Martinez R., Kaessmann H., Telenti A.
    Retrovirology 3:11-11(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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: June 24, 2015
This is version 91 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

External Data

Dasty 3

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 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.