ID A0A1U7RDM3_MESAU Unreviewed; 166 AA.
AC A0A1U7RDM3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN Name=Ppil1 {ECO:0000313|RefSeq:XP_005084969.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005084969.1};
RN [1] {ECO:0000313|RefSeq:XP_005084969.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|RuleBase:RU363019}.
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:0000256|ARBA:ARBA00000971,
CC ECO:0000256|RuleBase:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|RuleBase:RU363019}.
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DR RefSeq; XP_005084969.1; XM_005084912.3.
DR AlphaFoldDB; A0A1U7RDM3; -.
DR STRING; 10036.ENSMAUP00000006491; -.
DR GeneID; 101826928; -.
DR KEGG; maua:101826928; -.
DR CTD; 51645; -.
DR eggNOG; KOG0881; Eukaryota.
DR OrthoDB; 554597at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IEA:Ensembl.
DR GO; GO:0016018; F:cyclosporin A binding; IEA:Ensembl.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:1990403; P:embryonic brain development; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01922; cyclophilin_SpCYP2_like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 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 InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019,
KW ECO:0000313|RefSeq:XP_005084969.1};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022728};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Rotamase {ECO:0000256|RuleBase:RU363019};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT DOMAIN 17..164
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT BINDING 54..65
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 70..71
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 99..104
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 109..113
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 119
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 125
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
SQ SEQUENCE 166 AA; 18293 MW; 4A8238DD19F0B63B CRC64;
MAAIPPDTWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TRFHRIIKDF
MIQGGDPTGT GRGGASIYGK QFEDELHPEL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ
WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKIL KAYPSG
//
