ID   PT3K1_SOLTU             Reviewed;         374 AA.
AC   Q3YJS9;
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=Probable inactive patatin-3-Kuras 1;
DE   Flags: Precursor;
GN   Name=pat3-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 12-126; 132-156; 169-234;
RP   240-256 AND 266-356, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE
RP   SPECIFICITY, AND GLYCOSYLATION AT ASN-48 AND ASN-191.
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   -!- 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   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16884497}.
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   -!- CAUTION: Lacks the conserved Ser residue involved in nucleophilic
CC       attack and essential for hydrolase activity. Its enzyme activity is
CC       therefore unsure. {ECO:0000305}.
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DR   EMBL; DQ114421; AAZ75962.1; -; mRNA.
DR   AlphaFoldDB; Q3YJS9; -.
DR   SMR; Q3YJS9; -.
DR   iPTMnet; Q3YJS9; -.
DR   PRIDE; Q3YJS9; -.
DR   ProMEX; Q3YJS9; -.
DR   InParanoid; Q3YJS9; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q3YJS9; 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:0006629; P:lipid metabolic 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   Direct protein sequencing; Glycoprotein; Lipid metabolism; Plant defense;
KW   Reference proteome; Signal; Storage protein; Vacuole.
FT   SIGNAL          1..11
FT                   /evidence="ECO:0000269|PubMed:16884497"
FT   CHAIN           12..374
FT                   /note="Probable inactive patatin-3-Kuras 1"
FT                   /id="PRO_0000296713"
FT   DOMAIN          20..217
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           24..29
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16884497"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16884497"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   374 AA;  41193 MW;  95169A24CCB71B2F CRC64;
     MMLATTSSTF ATLGEMVTVL SIDGGGIKGI IPATILEFLE GQLQEVDNNT DARLADYFDV
     IGGTGTGGLL TAMITTPNEN NRPFAAAKDI IPFYFDHGPK IFEPSGFHLV EPKYDGKYLM
     QVLQEKLGET RVHQALTEVA ISSFDIKTNK PVIFTKSNLA KTPELDAKMY DICYSTAAAP
     TYFPPHYFAT NTSNGDQYDF NLVDGDVAAV DPSLLSISVA TRLAQEDPAF ASIKSLNYKQ
     MLLLSLGTGT NSEFAKNYTA EEAAKWGILQ WMSPLWEMRS AASSYMNDYY LSTVFQALDS
     QNNYLRVQEN ALTGTATTFD DASVANMILL VQVGENLLKK SVSEDNHETY EVALKRFAKL
     LSDRKKLRAN KASF