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Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin A) (Cyclosporin A-binding protein) (Rotamase A) [Cleaved into: Peptidyl-prolyl cis-trans isomerase A, N-terminally processed]

 PPIA_CRIGR              Reviewed;         164 AA.
P14851;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 114.
RecName: Full=Peptidyl-prolyl cis-trans isomerase A;
Short=PPIase A;
EC=5.2.1.8 {ECO:0000250|UniProtKB:P62937};
AltName: Full=Cyclophilin A;
AltName: Full=Cyclosporin A-binding protein;
AltName: Full=Rotamase A;
Contains:
RecName: Full=Peptidyl-prolyl cis-trans isomerase A, N-terminally processed;
Name=PPIA;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=2408007; DOI=10.1093/nar/18.1.200;
Bergsma D.J., Sylvester D.;
"A Chinese hamster ovary cyclophilin cDNA sequence.";
Nucleic Acids Res. 18:200-200(1990).
-!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of
proline imidic peptide bonds in oligopeptides and may therefore
assist protein folding. {ECO:0000250|UniProtKB:P62937}.
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-peptidylproline (omega=180) = [protein]-
peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
ChEBI:CHEBI:83834; EC=5.2.1.8;
Evidence={ECO:0000250|UniProtKB:P62937};
-!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some
of its effects via an inhibitory action on PPIase.
{ECO:0000250|UniProtKB:P62937}.
-!- SUBUNIT: Interacts with protein phosphatase PPP3CA/calcineurin A.
{ECO:0000250|UniProtKB:P62937}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Secreted {ECO:0000250}.
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}.
-!- PTM: 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). {ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
A subfamily. {ECO:0000305}.
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EMBL; X17105; CAA34961.1; -; mRNA.
RefSeq; XP_007643466.1; XM_007645276.1.
ProteinModelPortal; P14851; -.
SMR; P14851; -.
PRIDE; P14851; -.
Ensembl; ENSCGRT00001016740; ENSCGRP00001012506; ENSCGRG00001013904.
GeneID; 100769490; -.
KEGG; cge:100769490; -.
CTD; 5478; -.
HOVERGEN; HBG001065; -.
KO; K03767; -.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
GO; GO:0045069; P:regulation of viral genome replication; ISS:UniProtKB.
Gene3D; 2.40.100.10; -; 1.
InterPro; IPR029000; Cyclophilin-like_dom_sf.
InterPro; IPR024936; Cyclophilin-type_PPIase.
InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
PANTHER; PTHR11071; PTHR11071; 1.
Pfam; PF00160; Pro_isomerase; 1.
PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
PRINTS; PR00153; CSAPPISMRASE.
SUPFAM; SSF50891; SSF50891; 1.
PROSITE; PS00170; CSA_PPIASE_1; 1.
PROSITE; PS50072; CSA_PPIASE_2; 1.
2: Evidence at transcript level;
Acetylation; Cytoplasm; Glycoprotein; Isomerase; Isopeptide bond;
Phosphoprotein; Rotamase; Secreted; Ubl conjugation.
CHAIN 1 164 Peptidyl-prolyl cis-trans isomerase A.
/FTId=PRO_0000423237.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:P62937}.
CHAIN 2 164 Peptidyl-prolyl cis-trans isomerase A, N-
terminally processed.
/FTId=PRO_0000064113.
DOMAIN 7 163 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P62937}.
MOD_RES 2 2 N-acetylvaline; in Peptidyl-prolyl cis-
trans isomerase A, N-terminally
processed.
{ECO:0000250|UniProtKB:P62937}.
MOD_RES 28 28 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P62937}.
MOD_RES 44 44 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62937}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000250|UniProtKB:P62937}.
MOD_RES 82 82 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P62937}.
MOD_RES 93 93 Phosphothreonine.
{ECO:0000250|UniProtKB:P62937}.
MOD_RES 125 125 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62937}.
MOD_RES 131 131 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62937}.
MOD_RES 133 133 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17742}.
CARBOHYD 108 108 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 28 28 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P62937}.
CROSSLNK 28 28 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P62937}.
CROSSLNK 82 82 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P62937}.
SEQUENCE 164 AA; 17899 MW; 9B8E807747ADBA13 CRC64;
MVNPTVFFDI SADGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SSFHRIIPGF
MCQGGDFTRH NGTGGRSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE
WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITISD CGQL


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