ID   PT2K1_SOLTU             Reviewed;         374 AA.
AC   Q3YJT3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Patatin-2-Kuras 1;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=pat2-k1;
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], PROTEIN SEQUENCE OF 12-88; 131-155; 223-234;
RP   240-270; 299-306 AND 340-359, TISSUE SPECIFICITY, AND IDENTIFICATION BY
RP   MASS 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).
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:16884497}.
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; DQ114417; AAZ75958.1; -; mRNA.
DR   AlphaFoldDB; Q3YJT3; -.
DR   SMR; Q3YJT3; -.
DR   PRIDE; Q3YJT3; -.
DR   InParanoid; Q3YJT3; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q3YJT3; 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..11
FT                   /evidence="ECO:0000269|PubMed:16884497"
FT   CHAIN           12..374
FT                   /note="Patatin-2-Kuras 1"
FT                   /id="PRO_0000296710"
FT   DOMAIN          20..217
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COILED          309..372
FT                   /evidence="ECO:0000255"
FT   MOTIF           24..29
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           63..67
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           203..205
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        65
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        203
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   374 AA;  41108 MW;  26D1913638EF4311 CRC64;
     MILATTGSTC ATLGEMVTVL SIDGGGIKGI IPATILEFLE GQLQEVDNNK DARLADYFDV
     IGGTSTGGLL TAMITTPNEN NRPFAAAKDI VPFYFEHGPH IFNSSGTIFG PMYDGKYLLQ
     VLQEKLGETR VHQALTEVAI SSFDIKTNKP VIFTKSNLAK SPELDAKMYD ICYSTAAAPI
     YFPPHYFVTH TSNGDRYEFN LVDGAVATVG DPALLSLSVA TRLAQEDPAF SSIKSLDYKQ
     MLLLSLGTGT NSEFDKTYTA EEAAKWGPLR WLLAIQQMTN AASSYMTDYY LSTVFQARHS
     QNNYLRVQEN ALTGTTTEMD DASEANMELL VQVGETLLKK PVSKDSPETY EEALKRFAKL
     LSDRKKLRAN KASY