PATM2_SOLTU
ID PATM2_SOLTU Reviewed; 386 AA.
AC Q2MY52;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Patatin group M-2;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ274486; ABC55686.1; -; mRNA.
DR AlphaFoldDB; Q2MY52; -.
DR SMR; Q2MY52; -.
DR PRIDE; Q2MY52; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q2MY52; baseline and 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 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 group M-2"
FT /id="PRO_0000296707"
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; 42651 MW; DAF168B5BDCDE993 CRC64;
MATTKSFLIL FFMILATTSS TCAKLEKMVT VLSIDGGGIK GIIPAIILEF LEGQLQEVDN
NKDARLADYF DVIGGTSTGG LLTAMITTPN ENNRPFAAAK DIVPFYFEHG PHIFNYSGSI
IGPMYDGKYL LQVLQEKLGE TRVHQALTEV AISSFDIKTN KPVIFTKSNL AKSPELDAKM
YDICYSTAAA PIYFPPHYFI THTSNGDIYE FNLVDGGVAT VGDPALLSLS VATRLAQEDP
AFSSIKSLDY KQMLLLSLGT GTNSEFDKTY TAQEAAKWGP LRWMLAIQQM TNAASSYMTD
YYISTVFQAR HSQNNYLRVQ ENALTGTTTE MDDASEANME LLVQVGETLL KKPVSKDSPE
TYEEALKRFA KLLSDRKKLR ANKASY