ID   PT2K3_SOLTU             Reviewed;         386 AA.
AC   Q42502; Q2MYG6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Patatin-2-Kuras 3;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=pat2-k3; Synonyms=PGM01;
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. Superior; TISSUE=Tuber;
RX   PubMed=6150463; DOI=10.1093/nar/12.21.7987;
RA   Mignery G.A., Pikaard C.S., Hannapel D.J., Park W.D.;
RT   "Isolation and sequence analysis of cDNAs for the major potato tuber
RT   protein, patatin.";
RL   Nucleic Acids Res. 12:7987-8000(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-100; 129-137; 143-167;
RP   252-348 AND 352-371, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 255-386, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Kennebec; TISSUE=Tuber;
RX   PubMed=16322504; DOI=10.1534/genetics.105.051219;
RA   Stupar R.M., Beaubien K.A., Jin W., Song J., Lee M.-K., Wu C., Zhang H.-B.,
RA   Han B., Jiang J.;
RT   "Structural diversity and differential transcription of the patatin
RT   multicopy gene family during potato tuber development.";
RL   Genetics 172:1263-1275(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   -!- TISSUE SPECIFICITY: Tuber. {ECO:0000269|PubMed:16322504,
CC       ECO:0000269|PubMed:16884497}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates progressively during tuber formation
CC       from stolon. {ECO:0000269|PubMed:16322504}.
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; X01125; CAA25592.1; -; mRNA.
DR   EMBL; DQ114419; AAZ75960.1; -; mRNA.
DR   EMBL; DQ274354; ABC58937.1; -; mRNA.
DR   PIR; S51596; S51596.
DR   AlphaFoldDB; Q42502; -.
DR   SMR; Q42502; -.
DR   PRIDE; Q42502; -.
DR   InParanoid; Q42502; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q42502; differential.
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   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Plant defense; Reference proteome;
KW   Signal; Storage protein; Vacuole.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:16884497"
FT   CHAIN           24..386
FT                   /note="Patatin-2-Kuras 3"
FT                   /id="PRO_5000145462"
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;  42465 MW;  178107C161B7DEBD CRC64;
     MATTKSVLVL FFMILATTSS TCATLGEMVT VLSIDGGGIK GIIPATILEF LEGQLQEVDN
     NKDARLADYF DVIGGTSTGG LLTAMITTPN ENNRPFAAAK DIVPFYFEHG PHIFNSSGSI
     FGPMYDGKYF LQVLQEKLGE TRVHQALTEV AISSFDIKTN KPVIFTKSNL AKSPELDAKM
     YDICYSTAAA PTYFPPHYFV THTSNGDKYE FNLVDGAVAT VGDPALLSLS VATKLAQVDP
     KFASIKSLNY KQMLLLSLGT GTNSEFDKTY TAEEAAKWGP LRWILAIQQM TNAASSYMTD
     YYLSTVFQAR HSQNNYLRVQ ENALTGTTTE MDDASEANME LLVQVGEKLL KKPVSKDSPE
     TYEEALKRFA KLLSDRKKLR ANKASY