ID   PAT04_SOLTU             Reviewed;         386 AA.
AC   Q2MY42;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Patatin-04/09;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
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], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Kennebec;
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   -!- 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; DQ274491; ABC55691.1; -; mRNA.
DR   EMBL; DQ274496; ABC55696.1; -; mRNA.
DR   AlphaFoldDB; Q2MY42; -.
DR   SMR; Q2MY42; -.
DR   Allergome; 639; Sola t 1.
DR   PRIDE; Q2MY42; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q2MY42; 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-04/09"
FT                   /id="PRO_0000296690"
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"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   386 AA;  42628 MW;  5F690E27736A6CF7 CRC64;
     MATTKSFLIL FFMILATTSS TCAKLEEMVT VLSIDGGGIK GIIPAIILEF LEGQLQEVDN
     NKDARLADYF DVIGGTSTGG LLTAMITTPN ENNRPFAAAK DIVPFYFEHG PHIFNYSGSI
     FGPRYDGKYL LQVLQEKLGE TRVHQALTEV AISSFDIKTN KPVIFTKSNL AKSPELDAKM
     YDICYSTAAA PIYFPPHHFV THTSNGATYE FNLVDGGVAT VGDPALLSLS VATRLAQEDP
     AFSSIKSLDY KQMLLLSLGT GTNSEFDKTY TAEEAAKWGP LRWMLAIQQM TNAASSYMTD
     YYISTVFQAR HSQNNYLRVQ ENALNGTTTE MDDASEANME LLVQVGETLL KKPVSKDSPE
     TYEEALKRFA KLLSDRKKLR ANKASY