ID   CYPH_MAIZE              Reviewed;         172 AA.
AC   P21569;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin;
DE   AltName: Full=Cyclosporin A-binding protein;
DE   AltName: Full=Rotamase;
GN   Name=CYP; Synonyms=ROT1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7753032; DOI=10.1007/bf00705653;
RA   Marivet J., Frendo P., Burkard G.;
RT   "DNA sequence analysis of a cyclophilin gene from maize: developmental
RT   expression and regulation by salicylic acid.";
RL   Mol. Gen. Genet. 247:222-228(1995).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
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   -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC       its effects via an inhibitory action on PPIase.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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; M55021; AAA63403.1; -; mRNA.
DR   EMBL; X68678; CAA48638.1; -; Genomic_DNA.
DR   PIR; C39252; CSZM.
DR   AlphaFoldDB; P21569; -.
DR   SMR; P21569; -.
DR   STRING; 4577.GRMZM2G326111_P01; -.
DR   PaxDb; P21569; -.
DR   PRIDE; P21569; -.
DR   ProMEX; P21569; -.
DR   MaizeGDB; 65166; -.
DR   eggNOG; KOG0865; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P21569; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IMP:AgBase.
DR   GO; GO:0016018; F:cyclosporin A binding; IMP: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   2: Evidence at transcript level;
KW   Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..172
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000064146"
FT   DOMAIN          7..170
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   172 AA;  18349 MW;  16863EB1AAA33C67 CRC64;
     MANPRVFFDM TVGGAPAGRI VMELYANEVP KTAENFRALC TGEKGVGKSG KPLHYKGSTF
     HRVIPEFMCQ GGDFTRGNGT GGESIYGEKF PDEKFVRKQP APGVLSMANA GPNTNGSQFF
     ICTVATPWLD GKHVVFGQVV EGMDVVKAIE KVGTRNGSTS KVVKVADCGQ LS