ID   Q93W25_WHEAT            Unreviewed;       171 AA.
AC   Q93W25;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 136.
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=CyP3 {ECO:0000313|EMBL:AAK49428.1};
GN   Synonyms=CyP1 {ECO:0000313|EMBL:AAK49426.1}, TaBWCyp A-1
GN   {ECO:0000313|EMBL:BAN09078.1};
GN   ORFNames=CFC21_082064 {ECO:0000313|EMBL:KAF7077524.1}, CFC21_091348
GN   {ECO:0000313|EMBL:KAF7088217.1}, CFC21_091349
GN   {ECO:0000313|EMBL:KAF7088218.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EMBL:AAK49428.1};
RN   [1] {ECO:0000313|EMBL:AAK49428.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Endosperm {ECO:0000313|EMBL:AAK49428.1};
RX   AGRICOLA=IND23239870; DOI=10.1006/jcrs.2001.0382;
RA   Johnson J.C., Clarke B.C., Bhave M.;
RT   "Isolation and characterisation of cDNAs encoding protein disulphide
RT   isomerases and cyclophilins in wheat.";
RL   J. Cereal Sci. 34:159-171(2001).
RN   [2] {ECO:0000313|EMBL:BAN09078.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Haque M.E., Abe F., Mori M., Oyanagi A., Komatsu S., Kawaguchi K.;
RT   "cDNA sequences derived from Triticum aestivum cv. Bobwhite.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AFS50133.1, ECO:0007829|PDB:4E1Q}
RP   X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS).
RX   PubMed=23519664; DOI=10.1107/s0907444912051529;
RA   Sekhon S.S., Kaur H., Dutta T., Singh K., Kumari S., Kang S., Park S.G.,
RA   Park B.C., Jeong D.G., Pareek A., Woo E.J., Singh P., Yoon T.S.;
RT   "Structural and biochemical characterization of the cytosolic wheat
RT   cyclophilin TaCypA-1.";
RL   Acta Crystallogr. D 69:555-563(2013).
RN   [4] {ECO:0000313|EMBL:KAF7077524.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7077524.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [5] {ECO:0000313|EnsemblPlants:TraesCS6A02G068900.1.cds1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS6A02G068900.1.cds1};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [6] {ECO:0000313|EnsemblPlants:TraesCS6A02G068900.1.cds1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [7] {ECO:0000313|EMBL:KAF7077524.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7077524.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) 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. {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|RuleBase:RU363019};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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DR   EMBL; AF262982; AAK49426.1; -; mRNA.
DR   EMBL; AF262984; AAK49428.1; -; mRNA.
DR   EMBL; JQ678695; AFS50133.1; -; mRNA.
DR   EMBL; AB711117; BAN09078.1; -; mRNA.
DR   EMBL; CM022226; KAF7077524.1; -; Genomic_DNA.
DR   EMBL; CM022228; KAF7088217.1; -; Genomic_DNA.
DR   EMBL; CM022228; KAF7088218.1; -; Genomic_DNA.
DR   PDB; 4E1Q; X-ray; 1.25 A; A=1-171.
DR   PDB; 4HY7; X-ray; 1.20 A; A=1-171.
DR   PDBsum; 4E1Q; -.
DR   PDBsum; 4HY7; -.
DR   SMR; Q93W25; -.
DR   STRING; 4565.Q93W25; -.
DR   PaxDb; 4565-Traes_6AS_82E93D872-1; -.
DR   EnsemblPlants; TraesCS6A02G068900.1; TraesCS6A02G068900.1.cds1; TraesCS6A02G068900.
DR   EnsemblPlants; TraesCS6D02G066700.1; TraesCS6D02G066700.1.cds1; TraesCS6D02G066700.
DR   Gramene; TraesCAD_scaffold_069074_01G000300.1; TraesCAD_scaffold_069074_01G000300.1; TraesCAD_scaffold_069074_01G000300.
DR   Gramene; TraesCAD_scaffold_132108_01G000100.1; TraesCAD_scaffold_132108_01G000100.1; TraesCAD_scaffold_132108_01G000100.
DR   Gramene; TraesCLE_scaffold_092035_01G000100.1; TraesCLE_scaffold_092035_01G000100.1; TraesCLE_scaffold_092035_01G000100.
DR   Gramene; TraesCLE_scaffold_173486_01G000100.1; TraesCLE_scaffold_173486_01G000100.1; TraesCLE_scaffold_173486_01G000100.
DR   Gramene; TraesCS6A02G068900.1; TraesCS6A02G068900.1.cds1; TraesCS6A02G068900.
DR   Gramene; TraesCS6A03G0154200.1; TraesCS6A03G0154200.1.CDS1; TraesCS6A03G0154200.
DR   Gramene; TraesCS6D02G066700.1; TraesCS6D02G066700.1.cds1; TraesCS6D02G066700.
DR   Gramene; TraesCS6D03G0139300.1; TraesCS6D03G0139300.1.CDS1; TraesCS6D03G0139300.
DR   Gramene; TraesKAR6A01G0027250.1; cds.TraesKAR6A01G0027250.1; TraesKAR6A01G0027250.
DR   Gramene; TraesKAR6D01G0032330.1; cds.TraesKAR6D01G0032330.1; TraesKAR6D01G0032330.
DR   Gramene; TraesPAR_scaffold_073207_01G000300.1; TraesPAR_scaffold_073207_01G000300.1; TraesPAR_scaffold_073207_01G000300.
DR   Gramene; TraesPAR_scaffold_114312_01G000100.1; TraesPAR_scaffold_114312_01G000100.1; TraesPAR_scaffold_114312_01G000100.
DR   Gramene; TraesRN6D0100156600.1; TraesRN6D0100156600.1; TraesRN6D0100156600.
DR   Gramene; TraesROB_scaffold_028515_01G000400.1; TraesROB_scaffold_028515_01G000400.1; TraesROB_scaffold_028515_01G000400.
DR   Gramene; TraesROB_scaffold_065375_01G000300.1; TraesROB_scaffold_065375_01G000300.1; TraesROB_scaffold_065375_01G000300.
DR   Gramene; TraesWEE_scaffold_060470_01G000100.1; TraesWEE_scaffold_060470_01G000100.1; TraesWEE_scaffold_060470_01G000100.
DR   Gramene; TraesWEE_scaffold_079725_01G000300.1; TraesWEE_scaffold_079725_01G000300.1; TraesWEE_scaffold_079725_01G000300.
DR   eggNOG; KOG0865; Eukaryota.
DR   HOGENOM; CLU_012062_4_2_1; -.
DR   OMA; TWLTGKH; -.
DR   OrthoDB; 339082at2759; -.
DR   BRENDA; 5.2.1.8; 6500.
DR   Proteomes; UP000019116; Chromosome 6A.
DR   Proteomes; UP000019116; Chromosome 6D.
DR   Proteomes; UP000815260; Chromosome 6A.
DR   Proteomes; UP000815260; Chromosome 6D.
DR   ExpressionAtlas; Q93W25; baseline and differential.
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   CDD; cd01926; cyclophilin_ABH_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   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF578; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE 3-RELATED; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4E1Q, ECO:0007829|PDB:4HY7};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          7..170
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   171 AA;  18391 MW;  62D45AF2BC55FC6F CRC64;
     MANPRVFFDM TVGGAPAGRI VMELYKDAVP RTVENFRALC TGEKGVGKSG KPLHYKGSAF
     HRVIPDFMCQ GGDFTRGNGT GGESIYGEKF ADEKFVHKHT KPGILSMANA GPNTNGSQFF
     ICTVPCNWLD GKHVVFGEVV EGMDVVKNIE KVGSRSGTCS KQVVIADCGQ L
//