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PPIA_RAT
ID   PPIA_RAT                Reviewed;         164 AA.
AC   P10111; P18303; Q5BK98;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 189.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase A;
DE            Short=PPIase A;
DE            EC=5.2.1.8 {ECO:0000250|UniProtKB:P62937};
DE   AltName: Full=Cyclophilin A;
DE   AltName: Full=Cyclosporin A-binding protein;
DE   AltName: Full=Rotamase A;
DE   AltName: Full=p1B15;
DE   AltName: Full=p31;
DE   Contains:
DE     RecName: Full=Peptidyl-prolyl cis-trans isomerase A, N-terminally processed;
GN   Name=Ppia;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=3293952; DOI=10.1089/dna.1988.7.261;
RA   Danielson P.E., Forss-Petter S., Brow M.A., Calavetta L., Douglass J.,
RA   Milner R.J., Sutcliffe J.G.;
RT   "p1B15: a cDNA clone of the rat mRNA encoding cyclophilin.";
RL   DNA 7:261-267(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=1851525; DOI=10.1016/0169-328x(91)90007-k;
RA   Lad R.P., Smith M.A., Hilt D.C.;
RT   "Molecular cloning and regional distribution of rat brain cyclophilin.";
RL   Brain Res. Mol. Brain Res. 9:239-244(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sabra;
RX   PubMed=2996604; DOI=10.1016/0167-4781(85)90119-8;
RA   Theodor L., Peleg D., Meyuhas O.;
RT   "P31, a mammalian housekeeping protein encoded by a multigene family
RT   containing a high proportion of pseudogenes.";
RL   Biochim. Biophys. Acta 826:137-146(1985).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary, and Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-31; 56-69; 77-125; 132-144 AND 155-164, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   PROTEIN SEQUENCE OF 2-29.
RC   TISSUE=Liver;
RX   PubMed=1599421; DOI=10.1042/bj2840381;
RA   Connern C.P., Halestrap A.P.;
RT   "Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-
RT   isomerase from rat liver mitochondrial matrix reveals the existence of a
RT   distinct mitochondrial cyclophilin.";
RL   Biochem. J. 284:381-385(1992).
RN   [7]
RP   ACETYLATION AT VAL-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA   Lubec G., Chen W.-Q.;
RL   Submitted (FEB-2007) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the cis-trans isomerization of proline imidic
CC       peptide bonds in oligopeptides (By similarity). Exerts a strong
CC       chemotactic effect on leukocytes partly through activation of one of
CC       its membrane receptors BSG/CD147, initiating a signaling cascade that
CC       culminates in MAPK/ERK activation (By similarity). Activates
CC       endothelial cells (ECs) in a proinflammatory manner by stimulating
CC       activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by
CC       inducing expression of adhesion molecules including SELE and VCAM1 (By
CC       similarity). Induces apoptosis in ECs by promoting the FOXO1-dependent
CC       expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and
CC       apoptosis (By similarity). In response to oxidative stress, initiates
CC       proapoptotic and antiapoptotic signaling in ECs via activation of NF-
CC       kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (By
CC       similarity). Negatively regulates MAP3K5/ASK1 kinase activity,
CC       autophosphorylation and oxidative stress-induced apoptosis mediated by
CC       MAP3K5/ASK1 (By similarity). Necessary for the assembly of TARDBP in
CC       heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates
CC       TARDBP binding to RNA UG repeats and TARDBP-dependent expression of
CC       HDAC6, ATG7 and VCP which are involved in clearance of protein
CC       aggregates (By similarity). Plays an important role in platelet
CC       activation and aggregation (By similarity). Regulates calcium
CC       mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via
CC       increased ROS production as well as by facilitating the interaction
CC       between integrin and the cell cytoskeleton (By similarity). Binds
CC       heparan sulfate glycosaminoglycans (By similarity).
CC       {ECO:0000250|UniProtKB:P17742, ECO:0000250|UniProtKB:P62937}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC         Evidence={ECO:0000250|UniProtKB:P62937};
CC   -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC       its effects via an inhibitory action on PPIase.
CC       {ECO:0000250|UniProtKB:P62937}.
CC   -!- SUBUNIT: Interacts with protein phosphatase PPP3CA/calcineurin A (By
CC       similarity). Interacts with isoform 2 of BSG/CD147 (By similarity).
CC       Interacts with FOXO1; the interaction promotes FOXO1 dephosphorylation,
CC       nuclear accumulation and transcriptional activity (By similarity).
CC       Interacts with integrin ITGA2B:ITGB3; the interaction is ROS and
CC       peptidyl-prolyl cis-trans isomerase (PPIase) activity-dependent and is
CC       increased in the presence of thrombin (By similarity). Interacts with
CC       MAP3K5 (By similarity). Interacts with TARDBP; the interaction is
CC       dependent on the RNA-binding activity of TARDBP and the PPIase activity
CC       of PPIA/CYPA and the acetylation of PPIA/CYPA at Lys-125 favors the
CC       interaction (By similarity). Interacts with HNRNPA1, HNRNPA2B1, HNRNPC,
CC       RBMX, HNRNPK and HNRNPM (By similarity). {ECO:0000250|UniProtKB:P17742,
CC       ECO:0000250|UniProtKB:P62937}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62937}.
CC       Secreted {ECO:0000250|UniProtKB:P62937}. Nucleus
CC       {ECO:0000250|UniProtKB:P62937}. Note=Secretion occurs in response to
CC       oxidative stress in vascular smooth muscle through a vesicular
CC       secretory pathway that involves actin remodeling and myosin II
CC       activation, and mediates ERK1/2 activation.
CC       {ECO:0000250|UniProtKB:P62937}.
CC   -!- PTM: Acetylation at Lys-125 markedly inhibits catalysis of cis to trans
CC       isomerization (By similarity). PPIA acetylation also antagonizes the
CC       immunosuppressive effects of cyclosporine by inhibiting the sequential
CC       steps of cyclosporine binding and calcineurin inhibition (By
CC       similarity). Acetylation at Lys-125 favors the interaction with TARDBP
CC       (By similarity). {ECO:0000250|UniProtKB:P62937}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M19533; AAA41009.1; -; mRNA.
DR   EMBL; M25637; AAB59719.1; -; mRNA.
DR   EMBL; BC059141; AAH59141.1; -; mRNA.
DR   EMBL; BC091153; AAH91153.1; -; mRNA.
DR   PIR; A29819; CSRTA.
DR   RefSeq; NP_058797.1; NM_017101.1.
DR   RefSeq; XP_006250863.1; XM_006250801.3.
DR   AlphaFoldDB; P10111; -.
DR   SMR; P10111; -.
DR   BioGRID; 247550; 4.
DR   IntAct; P10111; 4.
DR   MINT; P10111; -.
DR   STRING; 10116.ENSRNOP00000009179; -.
DR   BindingDB; P10111; -.
DR   ChEMBL; CHEMBL2780; -.
DR   GlyGen; P10111; 1 site.
DR   iPTMnet; P10111; -.
DR   PhosphoSitePlus; P10111; -.
DR   World-2DPAGE; 0004:P10111; -.
DR   jPOST; P10111; -.
DR   PaxDb; P10111; -.
DR   PRIDE; P10111; -.
DR   Ensembl; ENSRNOT00000106407; ENSRNOP00000089529; ENSRNOG00000068764.
DR   GeneID; 100360977; -.
DR   GeneID; 25518; -.
DR   KEGG; rno:100360977; -.
DR   KEGG; rno:25518; -.
DR   UCSC; RGD:3372; rat.
DR   CTD; 5478; -.
DR   CTD; 645142; -.
DR   RGD; 3372; Ppia.
DR   VEuPathDB; HostDB:ENSRNOG00000027864; -.
DR   eggNOG; KOG0865; Eukaryota.
DR   GeneTree; ENSGT00950000183087; -.
DR   HOGENOM; CLU_012062_4_3_1; -.
DR   InParanoid; P10111; -.
DR   OMA; MRAPIVN; -.
DR   OrthoDB; 1403619at2759; -.
DR   PhylomeDB; P10111; -.
DR   TreeFam; TF316719; -.
DR   Reactome; R-RNO-210991; Basigin interactions.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:P10111; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000027864; Expressed in thymus and 20 other tissues.
DR   ExpressionAtlas; P10111; baseline and differential.
DR   Genevisible; P10111; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0016018; F:cyclosporin A binding; IDA:RGD.
DR   GO; GO:1904399; F:heparan sulfate binding; ISS:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR   GO; GO:0032148; P:activation of protein kinase B activity; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR   GO; GO:0060352; P:cell adhesion molecule production; ISS:UniProtKB.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0042118; P:endothelial cell activation; ISS:UniProtKB.
DR   GO; GO:0030595; P:leukocyte chemotaxis; ISS:UniProtKB.
DR   GO; GO:0034389; P:lipid droplet organization; ISO:RGD.
DR   GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:RGD.
DR   GO; GO:0061944; P:negative regulation of protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR   GO; GO:1903901; P:negative regulation of viral life cycle; ISO:RGD.
DR   GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR   GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR   GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
DR   GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; ISO:RGD.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR   GO; GO:2001233; P:regulation of apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045069; P:regulation of viral genome replication; ISS:UniProtKB.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW   Isomerase; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Rotamase; Secreted; Ubl conjugation.
FT   CHAIN           1..164
FT                   /note="Peptidyl-prolyl cis-trans isomerase A"
FT                   /id="PRO_0000423252"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000269|PubMed:1599421, ECO:0000269|Ref.5,
FT                   ECO:0000269|Ref.7"
FT   CHAIN           2..164
FT                   /note="Peptidyl-prolyl cis-trans isomerase A, N-terminally
FT                   processed"
FT                   /id="PRO_0000064121"
FT   DOMAIN          7..163
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
FT   MOD_RES         2
FT                   /note="N-acetylvaline; in Peptidyl-prolyl cis-trans
FT                   isomerase A, N-terminally processed"
FT                   /evidence="ECO:0000269|Ref.7"
FT   MOD_RES         28
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
FT   MOD_RES         44
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
FT   MOD_RES         76
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
FT   MOD_RES         82
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
FT   MOD_RES         93
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
FT   MOD_RES         125
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
FT   MOD_RES         131
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
FT   MOD_RES         133
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P17742"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        28
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
FT   CROSSLNK        28
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
FT   CROSSLNK        82
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62937"
SQ   SEQUENCE   164 AA;  17874 MW;  444C1ECF7F12841D CRC64;
     MVNPTVFFDI TADGEPLGRV CFELFADKVP KTAENFRALS TGEKGFGYKG SSFHRIIPGF
     MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE
     WLDGKHVVFG KVKEGMSIVE AMERFGSRNG KTSKKITISD CGQL
 
 
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