P62941 · PPIA_PAPAN
- ProteinPeptidyl-prolyl cis-trans isomerase A
- GenePPIA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids165 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (By similarity).
Activates endothelial cells (ECs) in a proinflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (By similarity).
Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity).
In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (By similarity).
Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (By similarity).
Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (By similarity).
Plays an important role in platelet activation and aggregation (By similarity).
Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity).
Binds heparan sulfate glycosaminoglycans (By similarity).
Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (By similarity).
Activates endothelial cells (ECs) in a proinflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (By similarity).
Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity).
In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (By similarity).
Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (By similarity).
Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (By similarity).
Plays an important role in platelet activation and aggregation (By similarity).
Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity).
Binds heparan sulfate glycosaminoglycans (By similarity).
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Activity regulation
Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-prolyl cis-trans isomerase A
- EC number
- Short namesPPIase A
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Papio
Accessions
- Primary accessionP62941
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed; alternate | ||||
Sequence: M | ||||||
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000423248 | 1-165 | Peptidyl-prolyl cis-trans isomerase A | |||
Sequence: MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE | ||||||
Modified residue | 2 | N-acetylvaline; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed | ||||
Sequence: V | ||||||
Chain | PRO_0000064118 | 2-165 | Peptidyl-prolyl cis-trans isomerase A, N-terminally processed | |||
Sequence: VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE | ||||||
Modified residue | 28 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 28 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Cross-link | 28 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | ||||||
Modified residue | 44 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 76 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 77 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 82 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 82 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 93 | Phosphothreonine | ||||
Sequence: T | ||||||
Glycosylation | 108 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 125 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 131 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 133 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization (By similarity).
PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (By similarity).
Acetylation at Lys-125 favors the interaction with TARDBP (By similarity).
PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (By similarity).
Acetylation at Lys-125 favors the interaction with TARDBP (By similarity).
Keywords
- PTM
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with protein phosphatase PPP3CA/calcineurin A (By similarity).
Interacts with isoform 2 of BSG/CD147 (By similarity).
Interacts with FOXO1; the interaction promotes FOXO1 dephosphorylation, nuclear accumulation and transcriptional activity (By similarity).
Interacts with integrin ITGA2B:ITGB3; the interaction is ROS and peptidyl-prolyl cis-trans isomerase (PPIase) activity-dependent and is increased in the presence of thrombin (By similarity).
Interacts with MAP3K5 (By similarity).
Interacts with TARDBP; the interaction is dependent on the RNA-binding activity of TARDBP and the PPIase activity of PPIA/CYPA and the acetylation of PPIA/CYPA at Lys-125 favors the interaction (By similarity).
Interacts with HNRNPA1, HNRNPA2B1, HNRNPC, RBMX, HNRNPK and HNRNPM (By similarity).
Interacts with isoform 2 of BSG/CD147 (By similarity).
Interacts with FOXO1; the interaction promotes FOXO1 dephosphorylation, nuclear accumulation and transcriptional activity (By similarity).
Interacts with integrin ITGA2B:ITGB3; the interaction is ROS and peptidyl-prolyl cis-trans isomerase (PPIase) activity-dependent and is increased in the presence of thrombin (By similarity).
Interacts with MAP3K5 (By similarity).
Interacts with TARDBP; the interaction is dependent on the RNA-binding activity of TARDBP and the PPIase activity of PPIA/CYPA and the acetylation of PPIA/CYPA at Lys-125 favors the interaction (By similarity).
Interacts with HNRNPA1, HNRNPA2B1, HNRNPC, RBMX, HNRNPK and HNRNPM (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-163 | PPIase cyclophilin-type | ||||
Sequence: FFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQ |
Sequence similarities
Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length165
- Mass (Da)18,012
- Last updated2007-01-23 v2
- Checksum9B2E637A555E4434
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF023859 EMBL· GenBank· DDBJ | AAB81959.1 EMBL· GenBank· DDBJ | mRNA |