ID   PPIM_MAIZE              Reviewed;          30 AA.
AC   Q10724;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase, microsomal;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin;
DE   AltName: Full=Rotamase;
DE   Flags: Fragment;
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] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Seedling {ECO:0000269|PubMed:8645184};
RX   PubMed=8645184; DOI=10.1042/bj3150965;
RA   Sheldon P.S., Venis M.A.;
RT   "Purification and characterization of cytosolic and microsomal cyclophilins
RT   from maize (Zea mays).";
RL   Biochem. J. 315:965-969(1996).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000250|UniProtKB:Q9SP02,
CC       ECO:0000269|PubMed:8645184}.
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:8645184};
CC   -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC       {ECO:0000269|PubMed:8645184}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8645184}.
CC   -!- SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:8645184}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:8645184}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000255}.
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DR   PIR; S69600; S69600.
DR   AlphaFoldDB; Q10724; -.
DR   SMR; Q10724; -.
DR   STRING; 4577.GRMZM2G084521_P03; -.
DR   PaxDb; Q10724; -.
DR   eggNOG; KOG0865; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:AgBase.
DR   GO; GO:0016018; F:cyclosporin A binding; IDA:AgBase.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:AgBase.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
PE   1: Evidence at protein level;
KW   Chaperone; Direct protein sequencing; Endoplasmic reticulum; Isomerase;
KW   Microsome; Reference proteome; Rotamase.
FT   CHAIN           1..>30
FT                   /note="Peptidyl-prolyl cis-trans isomerase, microsomal"
FT                   /id="PRO_0000302880"
FT   DOMAIN          12..>30
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   UNSURE          15
FT                   /note="V or I"
FT                   /evidence="ECO:0000269|PubMed:8645184"
FT   NON_TER         30
FT                   /evidence="ECO:0000303|PubMed:8645184"
SQ   SEQUENCE   30 AA;  3407 MW;  8357DB32F0030849 CRC64;
     KKDLTEVTHK VYFDVEIDGK PAGRIVMGLF