Ppia
entrez
268373
canonical
uniprot
P17742
canonical
ensembl
ENSMUSG00000071866
resolver
ensp
ENSMUSP00000117987
resolver
enst
ENSMUST00000132846
resolver
genesymbol
Ppia
resolver
uniprot
Q5SVY2
resolver
uniprot
Q9CWJ5
resolver
uniprot
Q9R137
resolver
uniprot_entry
PPIA_MOUSE
resolver
uniprot_entry
Q5SVY2_MOUSE
resolver
uniprot_sec
Q9CWJ5
resolver
uniprot_sec
Q9R137
resolver
activity_regulation
ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase. {ECO:0000250|UniProtKB:P62937}.
uniprot
proteins
amino_acid_sequence
MVNPTVFFDITADDEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCGQL
uniprot
proteins
ec_number
5.2.1.8
uniprot
proteins
function
FUNCTION: Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:24429998). 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 pro-inflammatory 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 (PubMed:25678563). Plays an important role in platelet activation and aggregation (PubMed:24429998). 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 (PubMed:24429998). Binds heparan sulfate glycosaminoglycans (By similarity). {ECO:0000250|UniProtKB:P62937, ECO:0000269|PubMed:24429998, ECO:0000269|PubMed:25678563}.
uniprot
proteins
mass_dalton
17971
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000250|UniProtKB:P62937}.
uniprot
proteins
protein_family
Cyclophilin-type PPIase family
uniprot
proteins
protein_family
PPIase A subfamily
uniprot
proteins
pubmed
10964515
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1565646
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16352598
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2197604
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24429998
uniprot
proteins
pubmed
25678563
uniprot
proteins
pubmed
25967121
uniprot
proteins
pubmed
7664883
uniprot
proteins
sequence_length
164
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62937}. Secreted {ECO:0000250|UniProtKB:P62937}. Nucleus {ECO:0000250|UniProtKB:P62937}. 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. {ECO:0000250|UniProtKB:P62937}.
uniprot
proteins