PPIA
entrez
5478
canonical
uniprot
P62937
canonical
ensembl
ENSG00000196262
resolver
ensp
ENSP00000419425
resolver
ensp
ENSP00000427976
resolver
ensp
ENSP00000503804
resolver
ensp
ENSP00000504216
resolver
genesymbol
HEL-S-69p
resolver
genesymbol
PPIA
resolver
genesymbol_syn
CYPA
resolver
hgnc
HGNC:9253
resolver
uniprot
A8K220
resolver
uniprot
P05092
resolver
uniprot
Q3KQW3
resolver
uniprot
Q567Q0
resolver
uniprot
Q6IBU5
resolver
uniprot
Q96IX3
resolver
uniprot
Q9BRU4
resolver
uniprot
Q9BTY9
resolver
uniprot
Q9UC61
resolver
uniprot
V9HWF5
resolver
uniprot_entry
PPIA_HUMAN
resolver
uniprot_entry
V9HWF5_HUMAN
resolver
uniprot_sec
A8K220
resolver
uniprot_sec
P05092
resolver
uniprot_sec
Q3KQW3
resolver
uniprot_sec
Q567Q0
resolver
uniprot_sec
Q6IBU5
resolver
uniprot_sec
Q96IX3
resolver
uniprot_sec
Q9BRU4
resolver
uniprot_sec
Q9BTY9
resolver
uniprot_sec
Q9UC61
resolver
activity_regulation
ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase. {ECO:0000269|PubMed:2001362}.
uniprot
proteins
amino_acid_sequence
MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE
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:2001362, PubMed:20676357, PubMed:21245143, PubMed:21593166, PubMed:25678563). 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 (PubMed:11943775, PubMed:21245143). 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 (PubMed:15130913). Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). 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 (PubMed:23180369). Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (PubMed:26095851). 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 (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 (PubMed:11943775). Inhibits replication of influenza A virus (IAV) (PubMed:19207730). Inhibits ITCH/AIP4-mediated ubiquitination of matrix protein 1 (M1) of IAV by impairing the interaction of ITCH/AIP4 with M1, followed by the suppression of the nuclear export of M1, and finally reduction of the replication of IAV (PubMed:22347431, PubMed:30328013). {ECO:0000250|UniProtKB:P17742, ECO:0000269|PubMed:11943775, ECO:0000269|PubMed:15130913, ECO:0000269|PubMed:19207730, ECO:0000269|PubMed:2001362, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:21245143, ECO:0000269|PubMed:21593166, ECO:0000269|PubMed:22347431, ECO:0000269|PubMed:23180369, ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:26095851, ECO:0000269|PubMed:30328013, ECO:0000269|PubMed:31063815}.; FUNCTION: (Microbial infection) May act as a mediator between human SARS coronavirus nucleoprotein and BSG/CD147 in the process of invasion of host cells by the virus (PubMed:15688292). {ECO:0000269|PubMed:15688292}.; FUNCTION: (Microbial infection) Stimulates RNA-binding ability of HCV NS5A in a peptidyl-prolyl cis-trans isomerase activity-dependent manner. {ECO:0000269|PubMed:21593166}.; FUNCTION: (Microbial infection) May act as a receptor for M.genitalium adhesin protein P140 (also called MgPa) (PubMed:29551599, PubMed:33013867). {ECO:0000305|PubMed:29551599, ECO:0000305|PubMed:33013867}.
uniprot
proteins
mass_dalton
18012
uniprot
proteins
mutagenesis
MUTAGEN 55; /note="R->A: Loss of peptidyl-prolyl cis-trans isomerase activity. No loss of its interaction with BSG/CD147 or its ability to induce leukocyte chemotaxis. No effect on its interaction with MAP3K5/ASK1. Loss of its ability to negatively regulate oxidative stress-induced apoptosis mediated by MAP3K5/ASK1. Reduced interaction with TARDBP. No loss of interaction with influenza A virus matrix protein 1 or its ability to inhibit viral replication."; /evidence="ECO:0000269|PubMed:19207730, ECO:0000269|PubMed:21245143, ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:26095851"; MUTAGEN 60; /note="F->A: Loss of ability to stimulate MAPK/ERK phosphorylation."; /evidence="ECO:0000269|PubMed:11943775"; MUTAGEN 69; /note="R->A: No effect on peptidyl-prolyl cis-trans isomerase activity. Reduced interaction with BSG/CD147 and ability to induce leukocyte chemotaxis."; /evidence="ECO:0000269|PubMed:21245143"; MUTAGEN 70; /note="H->A: No effect on peptidyl-prolyl cis-trans isomerase activity. Reduced interaction with BSG/CD147 and ability to induce leukocyte chemotaxis."; /evidence="ECO:0000269|PubMed:21245143"; MUTAGEN 107; /note="T->A: No effect on peptidyl-prolyl cis-trans isomerase activity. Reduced interaction with BSG/CD147 and ability to induce leukocyte chemotaxis."; /evidence="ECO:0000269|PubMed:21245143"; MUTAGEN 113; /note="F->A: Reduced ability to stimulate MAPK/ERK phosphorylation."; /evidence="ECO:0000269|PubMed:11943775"; MUTAGEN 121; /note="W->A: 200-fold decrease of sensitivity to CsA. Reduced ability to stimulate MAPK/ERK phosphorylation."; /evidence="ECO:0000269|PubMed:11943775, ECO:0000269|PubMed:2001362"; MUTAGEN 121; /note="W->E: Loss of peptidyl-prolyl cis-trans isomerase activity."; /evidence="ECO:0000269|PubMed:20676357"; MUTAGEN 121; /note="W->F: 75-fold decrease of sensitivity to CsA."; /evidence="ECO:0000269|PubMed:2001362"; MUTAGEN 121; /note="W->H: No effect on peptidyl-prolyl cis-trans isomerase activity."; /evidence="ECO:0000269|PubMed:20676357"; MUTAGEN 125; /note="K->Q: Acetylation-mimetic mutant; no effect on its interaction with TARDBP."; /evidence="ECO:0000269|PubMed:25678563"; MUTAGEN 125; /note="K->R: Loss of acetylation and interaction with TARDBP."; /evidence="ECO:0000269|PubMed:25678563"; MUTAGEN 126; /note="H->A: Loss of peptidyl-prolyl cis-trans isomerase activity and interaction with HCVNS5A. Loss of ability to stimulate MAPK/ERK phosphorylation."; /evidence="ECO:0000269|PubMed:11943775, ECO:0000269|PubMed:21593166
uniprot
proteins
post_translational_modification
PTM: Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization and stabilizes cis rather than trans forms of the HIV-1 capsid. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (PubMed:20364129, Ref.12). Acetylation at Lys-125 favors its interaction with TARDBP (PubMed:25678563). {ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0000269|Ref.12}.
uniprot
proteins
protein_family
Cyclophilin-type PPIase family
uniprot
proteins
protein_family
PPIase A subfamily
uniprot
proteins
pubmed
11353871
uniprot
proteins
pubmed
11943775
uniprot
proteins
pubmed
12218175
uniprot
proteins
pubmed
12357034
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15130913
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15688292
uniprot
proteins
pubmed
16527992
uniprot
proteins
pubmed
1896075
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19207730
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
1946361
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
2001362
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20147391
uniprot
proteins
pubmed
20364129
uniprot
proteins
pubmed
20676357
uniprot
proteins
pubmed
21245143
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21593166
uniprot
proteins
pubmed
2197089
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22347431
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23180369
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25489052
uniprot
proteins
pubmed
25678563
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26095851
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29551599
uniprot
proteins
pubmed
30328013
uniprot
proteins
pubmed
31063815
uniprot
proteins
pubmed
3297675
uniprot
proteins
pubmed
33013867
uniprot
proteins
pubmed
7657784
uniprot
proteins
pubmed
8263916
uniprot
proteins
pubmed
8421500
uniprot
proteins
pubmed
8421501
uniprot
proteins
pubmed
8513493
uniprot
proteins
pubmed
8652511
uniprot
proteins
pubmed
9299338
uniprot
proteins
pubmed
9385632
uniprot
proteins
pubmed
9769216
uniprot
proteins
sequence_length
165
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26095851, ECO:0000269|PubMed:29551599}. Secreted {ECO:0000269|PubMed:16527992}. Nucleus {ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:29551599}. Cell membrane {ECO:0000269|PubMed:29551599}. Note=Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that includes Rho GTPase signaling, actin remodeling, and myosin II activation. {ECO:0000269|PubMed:16527992}.; SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33013867}. Note=(Microbial infection) Increased amounts of protein are secreted after treatment with M.genitalium P140 adhesin (MgPa). {ECO:0000269|PubMed:33013867}.
uniprot
proteins