ID   PIN1_MALDO              Reviewed;         121 AA.
AC   Q94G00;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase Pin1;
DE            Short=PPIase Pin1;
DE            EC=5.2.1.8;
DE   AltName: Full=MdPin1;
DE   AltName: Full=Rotamase Pin1;
GN   Name=PIN1;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Granny Smith;
RX   PubMed=11118438; DOI=10.1074/jbc.m007006200;
RA   Yao J.-L., Kops O., Lu P.-J., Lu K.P.;
RT   "Functional conservation of phosphorylation-specific prolyl isomerases in
RT   plants.";
RL   J. Biol. Chem. 276:13517-13523(2001).
CC   -!- FUNCTION: Prolyl cis/trans isomerase with specificity for phospho-Ser-
CC       Pro bonds.
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: Inhibited in vitro by juglone.
CC   -!- DEVELOPMENTAL STAGE: Expressed in 1 to 3 week-old fruit but not in
CC       mature fruit. Expression is tightly associated with cell division.
CC   -!- MISCELLANEOUS: Like all plant Pin1-type PPIases, do not contain the N-
CC       terminal WW domain found in other eukaryotic parvulins, but contains a
CC       four-amino acid insertion next to the phospho-specific recognition site
CC       of the active site. These extra amino acids may be important for
CC       mediating the substrate interaction of plant enzymes.
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {ECO:0000305}.
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DR   EMBL; AF290200; AAK83088.1; -; mRNA.
DR   AlphaFoldDB; Q94G00; -.
DR   SMR; Q94G00; -.
DR   STRING; 3750.XP_008355527.1; -.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR023058; PPIase_PpiC_CS.
DR   Pfam; PF00639; Rotamase; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   2: Evidence at transcript level;
KW   Isomerase; Rotamase.
FT   CHAIN           1..121
FT                   /note="Peptidyl-prolyl cis-trans isomerase Pin1"
FT                   /id="PRO_0000193442"
FT   DOMAIN          6..121
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   121 AA;  13220 MW;  24B179CEBD86A60B CRC64;
     MSSSAGNQVR ASHILIKHQG SRRKASWKDP EGQIIRNTTR DSAVSQLKAL RDDILSGKAK
     FDDLAARYSD CSSAKRGGDL GPFGRNQMQK PFEEATFALK VGEMSDIVDT DSGVHIIKRT
     G