CYPH_SOLLC
ID CYPH_SOLLC Reviewed; 171 AA.
AC P21568;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000303|PubMed:1702215};
DE Short=PPIase {ECO:0000303|PubMed:1702215};
DE EC=5.2.1.8 {ECO:0000269|PubMed:1702215};
DE AltName: Full=Cyclophilin {ECO:0000303|PubMed:1702215};
DE AltName: Full=Cyclosporin A-binding protein {ECO:0000303|PubMed:1702215};
DE AltName: Full=Rotamase {ECO:0000303|PubMed:1702215};
GN Name=CYP {ECO:0000303|PubMed:1702215};
GN Synonyms=ROT1 {ECO:0000303|PubMed:1702215};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, CATALYTIC
RP ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=cv. Mo17;
RX PubMed=1702215; DOI=10.1073/pnas.87.24.9519;
RA Gasser C.S., Gunning D.A., Budelier K.A., Brown S.M.;
RT "Structure and expression of cytosolic cyclophilin/peptidyl-prolyl cis-
RT trans isomerase of higher plants and production of active tomato
RT cyclophilin in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9519-9523(1990).
CC -!- FUNCTION: PPIases accelerate the folding of proteins (PubMed:1702215).
CC It catalyzes the cis-trans isomerization of proline imidic peptide
CC bonds in oligopeptides (PubMed:1702215). {ECO:0000269|PubMed:1702215}.
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; Evidence={ECO:0000269|PubMed:1702215};
CC -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA) (PubMed:1702215). CsA
CC mediates some of its effects via an inhibitory action on PPIase
CC (PubMed:1702215). {ECO:0000269|PubMed:1702215}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14832}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, floral buds, growing shoots
CC and stamens at anthesis. {ECO:0000269|PubMed:1702215}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; M55019; AAA63543.1; -; mRNA.
DR PIR; A39252; CSTO.
DR RefSeq; NP_001234488.1; NM_001247559.1.
DR AlphaFoldDB; P21568; -.
DR SMR; P21568; -.
DR STRING; 4081.Solyc01g111170.2.1; -.
DR Allergome; 11323; Sola l 5.
DR Allergome; 11404; Sola l 5.0101.
DR PaxDb; P21568; -.
DR PRIDE; P21568; -.
DR EnsemblPlants; Solyc01g111170.3.1; Solyc01g111170.3.1.1; Solyc01g111170.3.
DR GeneID; 100736432; -.
DR Gramene; Solyc01g111170.3.1; Solyc01g111170.3.1.1; Solyc01g111170.3.
DR KEGG; sly:100736432; -.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P21568; -.
DR OMA; GEGYPGS; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P21568; -.
DR Proteomes; UP000004994; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; IDA:AgBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:AgBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
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 Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..171
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000064145"
FT DOMAIN 7..170
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 171 AA; 17911 MW; 25013625D21E3D21 CRC64;
MANPKVFFDL TIGGAPAGRV VMELFADTTP KTAENFRALC TGEKGVGKMG KPLHYKGSTF
HRVIPGFMCQ GGDFTAGNGT GGESIYGAKF NDENFVKKHT GPGILSMANA GPGTNGSQFF
ICTAKTEWLN GKHVVFGQVV EGMDVIKKAE AVGSSSGRCS KPVVIADCGQ L
