ID   CYP1_SOYBN              Reviewed;         172 AA.
AC   Q8W171; C6SYU0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase 1 {ECO:0000250|UniProtKB:O49886};
DE            Short=PPIase 1 {ECO:0000250|UniProtKB:O49886};
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin 1 {ECO:0000303|Ref.1};
DE   AltName: Full=Cyclosporin A-binding protein 1 {ECO:0000250|UniProtKB:O49886};
DE   AltName: Full=Rotamase 1 {ECO:0000250|UniProtKB:O49886};
GN   Name=Cyp1 {ECO:0000303|Ref.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAL51087.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=cv. Williams 82 {ECO:0000269|Ref.1};
RA   Kan Y.-C., Liu S.-W., Guo Z.-J., Li D.-B.;
RT   "Characterization of a cyclophilin cDNA from soybean cells.";
RL   J. Integr. Plant Biol. 44:173-176(2002).
RN   [2] {ECO:0000312|EMBL:ACU14413.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250|UniProtKB:O49886}.
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:0000305};
CC   -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC       its effects via an inhibitory action on PPIase (By similarity).
CC       {ECO:0000250|UniProtKB:O49886}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O49886}.
CC   -!- INDUCTION: Not induced by infection with virulent or avirulent
CC       P.syringae. Not induced by phenylmethylsulfonyl fluoride (PMSF) and
CC       yeast elicitator (YE). {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF456323; AAL51087.1; -; mRNA.
DR   EMBL; BT090338; ACU14413.1; -; mRNA.
DR   AlphaFoldDB; Q8W171; -.
DR   SMR; Q8W171; -.
DR   STRING; 3847.GLYMA11G10480.2; -.
DR   PRIDE; Q8W171; -.
DR   ProMEX; Q8W171; -.
DR   eggNOG; KOG0865; Eukaryota.
DR   InParanoid; Q8W171; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Chaperone; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..172
FT                   /note="Peptidyl-prolyl cis-trans isomerase 1"
FT                   /id="PRO_0000395399"
FT   DOMAIN          7..170
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   CONFLICT        154..155
FT                   /note="SG -> FS (in Ref. 2; ACU14413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="P -> L (in Ref. 2; ACU14413)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   172 AA;  18179 MW;  F4189F46BA83DF44 CRC64;
     MPNPKVFFDM TIGGQSAGRI VMELYADVTP RTAENFRALC TGEKGVGRSG KPLHYKGSSF
     HRVIPSFMCQ GGDFTAGNGT GGESIYGAKF ADENFVKKHT GPGILSMANA GPGTNGSQFF
     ICTEKTEWLD GKHVVFGQVI EGLNVVKDIE KVGSGSGRTS KPVVIANCGQ PS