ID   PAT16_SOLTU             Reviewed;         386 AA.
AC   Q41487; Q41473;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Patatin-16;
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].
RC   STRAIN=cv. Sumi; TISSUE=Tuber;
RX   PubMed=2420638; DOI=10.1016/0014-5793(86)81175-9;
RA   Nakamura K., Hattori T., Asahi T.;
RT   "Direct immunological identification of full-length cDNA clones for plant
RT   protein without gene fusion to E. coli protein.";
RL   FEBS Lett. 198:16-20(1986).
CC   -!- FUNCTION: Probable lipolytic acyl hydrolase (LAH), an activity which is
CC       thought to be involved in the response of tubers to pathogens.
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. This tuber protein
CC       represents approximately 40% of the total protein in mature tubers.
CC   -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR   EMBL; Z27221; CAA81735.1; -; mRNA.
DR   PIR; A23634; A23634.
DR   PIR; T07592; T07592.
DR   AlphaFoldDB; Q41487; -.
DR   SMR; Q41487; -.
DR   PRIDE; Q41487; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q41487; 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..386
FT                   /note="Patatin-16"
FT                   /id="PRO_0000296701"
FT   DOMAIN          32..229
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COILED          360..384
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           215..217
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        215
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   386 AA;  42628 MW;  A58E1DC9529BF0EF CRC64;
     MATTKSFLIL IVMILATTSS TFASLEEMVT VLSIDGGGIK GIIPGTILEF LEGQLQKMDN
     NADARLADYF DVIGGTSTGG LLTAMITTPN ENNRPFAAAN EIVPFYFEHG PHIFNSSTGQ
     FFRKYDGKYL MQVLQEKLGE TRVHQALTEV AISSFDIKTN KPVIFTKSNL AKSPELDAKM
     YDICYSTAAA PTYFPPHYFA TNTINGDKYE LNLVDGAVAT VADPALLSVS VATRRAQEDP
     AFASIRSLNY KKMLLLSLGT GTTSEFDKTH TAEETAKWGA LQWMLVIQQM TEAASSYMTD
     YYLSTVFQDL HSQNNYLRVQ ENPLTGTTTK ADDASEANME LLAQVGENLL KKPVSKDNPE
     TYEEALKRFA KLLSDRKKLR ANKASY