ID   PATA3_SOLTU             Reviewed;         387 AA.
AC   Q2MY58;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Patatin group A-3;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
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], 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 and stolon. {ECO:0000269|PubMed:16322504}.
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}.
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; DQ274480; ABC55680.1; -; mRNA.
DR   AlphaFoldDB; Q2MY58; -.
DR   SMR; Q2MY58; -.
DR   PRIDE; Q2MY58; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q2MY58; 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   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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..387
FT                   /note="Patatin group A-3"
FT                   /id="PRO_0000296703"
FT   DOMAIN          32..230
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COILED          361..385
FT                   /evidence="ECO:0000255"
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"
SQ   SEQUENCE   387 AA;  42620 MW;  0212D2A92D6E5DEF CRC64;
     MATTKSFLIL IVMILATTSS TFASLEEMVT VLSIDGGGVK GIIPGTILEF LEGQLQKMDN
     NADARLADYF DVIGGTSTGG LLTAMITTPN ENNRPFAAAN EIVPFYFEHG PHIFNSSTGQ
     FFGPKYDGKY LMQVLQEKLG ETRVHQALTE VAISSFDIKT NKPVIFTKSN LAKSPELDAK
     MYDICYSTAA APTYFPPHYF ATNTINGDKY EFNLVDGAVA TVADPALLSV SVATRRAQED
     PAFASIRSLN YKKMLLLSLG TGTTSEFDKT HTAEETAKWG ALQWMLVIQQ MTEAASSYMT
     DYYLSTVFQD LHSQNNYLRV QENALTGTTT KADDASEANM ELLAQVGENL LKKPVSKDNP
     ETYEEALKRF AKLLSDRKKL RANKASY