ID   PT2K4_SOLTU             Reviewed;         374 AA.
AC   Q3YJT0;
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-2-Kuras 4;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=pat2-k4;
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. 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   -!- 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; DQ114420; AAZ75961.1; -; mRNA.
DR   AlphaFoldDB; Q3YJT0; -.
DR   SMR; Q3YJT0; -.
DR   STRING; 4113.PGSC0003DMT400036586; -.
DR   PRIDE; Q3YJT0; -.
DR   InParanoid; Q3YJT0; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q3YJT0; 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..11
FT                   /evidence="ECO:0000255"
FT   CHAIN           12..374
FT                   /note="Patatin-2-Kuras 4"
FT                   /id="PRO_0000296712"
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;  41137 MW;  3D33DDAC8B00EB4B CRC64;
     MILATTSSTC ATLGEMVTVL SIDGGGIKGI IPAIILEFLE GQLQEVDNNA DARLADYFDV
     IGGTSTGGLL TAMITTPNEN NRPFAAAKDI VPFYFEHGPH IFNYSGSILG PMYDGKYLLQ
     VLQEKLGETR VHQALTEVAI SSFDIKTNKP VIFTKSNLAE SPQLDAKMYD ICYSTAAAPI
     YFPPHYFVTH TSNGDRYEFN LVDGGVATVG DPALLSLSVA TKLAQVDPKF ASIKSLDYKQ
     MLLLSLGTGT NSEFDKTYTA QETAKWGPLR WMLAIQQMTN AASSYMTDYY ISTVFQARHS
     QNNYLRVQEN ALTGTTTEMD DASEANMELL VQVGETLLKK PVSKDSPETY EEALKRFAKL
     LSDRKKLRAN KASY