ID   PAT05_SOLTU             Reviewed;         387 AA.
AC   Q3YJT5;
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-05;
DE            EC=3.1.1.-;
DE   AltName: Full=Patatin-1-Kuras 1;
DE   Flags: Precursor;
GN   Name=pat1-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 24-40; 66-100; 126-180;
RP   236-247; 253-278 AND 320-372, 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).
RN   [2]
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       ECO:0000269|PubMed:16884497}.
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}.
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DR   EMBL; DQ114415; AAZ75956.1; -; mRNA.
DR   EMBL; DQ274492; ABC55692.1; -; mRNA.
DR   AlphaFoldDB; Q3YJT5; -.
DR   SMR; Q3YJT5; -.
DR   STRING; 4113.PGSC0003DMT400022567; -.
DR   PRIDE; Q3YJT5; -.
DR   eggNOG; KOG0513; Eukaryota.
DR   InParanoid; Q3YJT5; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q3YJT5; 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   Direct protein sequencing; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Plant defense; Reference proteome; Signal;
KW   Storage protein; Vacuole.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:16884497"
FT   CHAIN           24..387
FT                   /note="Patatin-05"
FT                   /id="PRO_0000296691"
FT   DOMAIN          32..230
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
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           216..218
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        216
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   387 AA;  42528 MW;  AA0B646FC1874BFB CRC64;
     MATTKSVLVL IFMILATTSS TFATLGEMVT VLSIDGGGIK GIIPGIILEF LEGQLQKMDN
     NADARLADYF DVIGGTSTGG LLTAMITTPN ENNRPFAAAK DIVPFYFQHG PHIFNSSTGQ
     FFGPKYDGKY LMQVLQEKLG ETRVHQALTE VAISSFDIKT NKPVIFTKSN LAKSPELDAK
     MSDICYSTAA APTYFPPHYF ATNTSNGDKY EFNLVDGAVA TVADPALLSV SVATRRAEED
     PAFASIRSLN YKQLLLLSLG TGTNSEFDKT HTAQETAKWG ALQWMLVIQQ MTEAASSYMT
     DYYLSTVFQD LHSQNNYLRV QENALTGTTT KADDASEANM ELLVQVGENL LKKPVSKDNP
     ETYEEALKRF AKLLSDRKKF RANKASY