PIN1_DIGLA
ID PIN1_DIGLA Reviewed; 118 AA.
AC Q9LEK8;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase Pin1;
DE Short=PPIase Pin1;
DE EC=5.2.1.8;
DE AltName: Full=DlPar13;
DE AltName: Full=Rotamase Pin1;
GN Name=PARV12.8;
OS Digitalis lanata (Grecian foxglove).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plantaginaceae; Digitalideae; Digitalis.
OX NCBI_TaxID=49450;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=cv. VIII;
RX PubMed=11118437; DOI=10.1074/jbc.m007005200;
RA Metzner M., Stoller G., Ruecknagel P., Lu K.P., Fischer G., Luckner M.,
RA Kuellertz G.;
RT "Functional replacement of the essential ess1 in yeast by the plant
RT parvulin DlPar13.";
RL J. Biol. Chem. 276:13524-13529(2001).
CC -!- FUNCTION: Prolyl cis/trans isomerase with specificity for phospho-Ser-
CC Pro bonds. {ECO:0000269|PubMed:11118437}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11118437}. Nucleus
CC {ECO:0000269|PubMed:11118437}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC seedlings. {ECO:0000269|PubMed:11118437}.
CC -!- PTM: The N-terminus is blocked.
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 -!- MISCELLANEOUS: Three amino acid residues (P79S, E91D and A95G) differ
CC when compared with the partial sequence of purified protein. The
CC existence of two or more genes coding for this protein is not exluded.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000305}.
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DR EMBL; AJ133755; CAB94994.1; -; mRNA.
DR AlphaFoldDB; Q9LEK8; -.
DR SMR; Q9LEK8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Isomerase; Nucleus; Rotamase.
FT CHAIN 1..118
FT /note="Peptidyl-prolyl cis-trans isomerase Pin1"
FT /id="PRO_0000193441"
FT DOMAIN 3..118
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 118 AA; 12834 MW; 131B74FB4AC3F229 CRC64;
MSSEKVRASH ILIKHQGSRR KSSWKDPDGS LISATTRDDA VSQLQSLRQE LLSDPASFSD
LASRHSHCSS AKRGGDLGPF GRGQMQKPFE EATFALKVGE ISDIVDTDSG VHIIKRTG
