ID   PT2K2_SOLTU             Reviewed;         386 AA.
AC   Q3YJT2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Patatin-2-Kuras 2;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=pat2-k2;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kuras; TISSUE=Tuber;
RX   PubMed=16884497; DOI=10.1111/j.1742-4658.2006.05364.x;
RA   Bauw G., Nielsen H.V., Emmersen J., Nielsen K.L., Joergensen M.,
RA   Welinder K.G.;
RT   "Patatins, Kunitz protease inhibitors and other major proteins in tuber of
RT   potato cv. Kuras.";
RL   FEBS J. 273:3569-3584(2006).
CC   -!- FUNCTION: Probable lipolytic acyl hydrolase (LAH), an activity which is
CC       thought to be involved in the response of tubers to pathogens.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- DOMAIN: The nitrogen atoms of the two glycine residues in the GGXR
CC       motif define the oxyanion hole, and stabilize the oxyanion that forms
CC       during the nucleophilic attack by the catalytic serine during substrate
CC       cleavage.
CC   -!- MISCELLANEOUS: Patatin have a dual role as a somatic storage protein
CC       and as an enzyme involved in host resistance.
CC   -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR   EMBL; DQ114418; AAZ75959.1; -; mRNA.
DR   AlphaFoldDB; Q3YJT2; -.
DR   SMR; Q3YJT2; -.
DR   PRIDE; Q3YJT2; -.
DR   InParanoid; Q3YJT2; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q3YJT2; baseline.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Plant defense; Reference proteome; Signal; Storage protein; Vacuole.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..386
FT                   /note="Patatin-2-Kuras 2"
FT                   /id="PRO_0000296711"
FT   DOMAIN          32..229
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COILED          321..384
FT                   /evidence="ECO:0000255"
FT   MOTIF           36..41
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           75..79
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           215..217
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        77
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        215
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   386 AA;  42583 MW;  5A96AE0C48C90CFC CRC64;
     MATTKSFLIL FFMILATTSS TCATLGEMVT VLSIDGGGIK GIIPAVILEF LEGQLQEVDN
     NKDARLADYF DVIGGTSTGG LLTAMITTPN ENNRPFAAAK DIIPFYFEHG PHIFNYSGSI
     FGPMYDGKYL LQVLQEKLGE TRVHQALTEV AISSFDIKTN KPVIFTKSNL AKSPELDAKM
     YDICYSTAAA PMYFPPHYFI THTSDGDIYE FNLVDGAVAT VGDPALLSLS VATRLAQEDP
     AFSSIKSLDY KQMLLLSLGT GTNSEFDKTY TAEEAAKWGP LRWLLAIQQM TNAASSYMTD
     YYISTVFQAH HSQNNYLRVQ ENALTGTTTE MDDASEANME LLVQVGETLL KKPVSKDSPE
     TYEEALKRFA KLLSDRKKLR ANKASY