ID   PT1K2_SOLTU             Reviewed;         375 AA.
AC   Q3YJT4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Patatin-1-Kuras 2;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=pat1-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], PROTEIN SEQUENCE OF 118-126; 132-156; 224-235;
RP   320-340 AND 346-357, 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).
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}.
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DR   EMBL; DQ114416; AAZ75957.1; -; mRNA.
DR   AlphaFoldDB; Q3YJT4; -.
DR   SMR; Q3YJT4; -.
DR   PRIDE; Q3YJT4; -.
DR   InParanoid; Q3YJT4; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q3YJT4; 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   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:0000255"
FT   CHAIN           12..375
FT                   /note="Patatin-1-Kuras 2"
FT                   /id="PRO_0000296709"
FT   DOMAIN          20..218
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COILED          349..373
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           204..206
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        204
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   375 AA;  41315 MW;  A367948DA5339FD7 CRC64;
     MILATTSSTF ASLEEMVTVL SIDGGGIKGI IPGTILEFLE GQLQKMDNNA DARLADYFDV
     IGGTSTGGLL TAMITTPNEN NRPFAAANEI VPFYFEHGPH IFNSSTGQFF GPKYDGKYLM
     QVLQEKLGET RVHQALTEVA ISSFDIKTNK PVIFTKSNLA KSPELDAKMY DICYSTAAAP
     TYFPPHYFAT NTINGDKYKF NLVDGAVATV ADPALLSVSV ATRRAQEDPA FASIRSLNYK
     KMLLLSLGTG TTSEFDKTHT AEETAKWGAL QWMLVIQQMT EAASSYMTDY YLSTVFQDLH
     SQNNYLRVQE NALTGTTTKA DDASEANMEL LAQVGENLLK KPVSKDNPET YEEALKRFAK
     LLSDRKKLRA NKASY