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   31-MAY-2011, entry version 43.
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 (Foxglove).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Lamiales; Plantaginaceae; Digitalideae; Digitalis.
OX   NCBI_TaxID=49450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RC   STRAIN=cv. VIII;
RX   MEDLINE=21216637; PubMed=11118437; DOI=10.1074/jbc.M007005200;
RA   Metzner M., Stoller G., Ruecknagel P., Lu K.P., Fischer G.,
RA   Luckner M., 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-
CC       Ser-Pro bonds.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME REGULATION: Inhibited in vitro by juglone.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC       seedlings.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: Like all plant Pin1-type PPIases, do not contain
CC       the N-terminal WW domain found in other eukaryotic parvulins, but
CC       contains a four-amino acid insertion next to the phospho-specific
CC       recognition site of the active site. These extra amino acids may
CC       be important for mediating the substrate interaction of plant
CC       enzymes.
CC   -!- MISCELLANEOUS: Three amino acid residues (P79S, E91D and A95G)
CC       differ when compared with the partial sequence of purified
CC       protein. The existence of two or more genes coding for this
CC       protein is not exluded.
CC   -!- SIMILARITY: Belongs to the ppiC/parvulin rotamase family.
CC   -!- SIMILARITY: Contains 1 PpiC domain.
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DR   EMBL; AJ133755; CAB94994.1; -; mRNA.
DR   ProteinModelPortal; Q9LEK8; -.
DR   SMR; Q9LEK8; 2-118.
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   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
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       Peptidyl-prolyl cis-trans isomerase Pin1.
FT                                /FTId=PRO_0000193441.
FT   DOMAIN        3    118       PpiC.
SQ   SEQUENCE   118 AA;  12834 MW;  131B74FB4AC3F229 CRC64;
     MSSEKVRASH ILIKHQGSRR KSSWKDPDGS LISATTRDDA VSQLQSLRQE LLSDPASFSD
     LASRHSHCSS AKRGGDLGPF GRGQMQKPFE EATFALKVGE ISDIVDTDSG VHIIKRTG
//