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Database: UniProt
Entry: A0A1S3YWX7_TOBAC
LinkDB: A0A1S3YWX7_TOBAC
Original site: A0A1S3YWX7_TOBAC 
ID   A0A1S3YWX7_TOBAC        Unreviewed;       392 AA.
AC   A0A1S3YWX7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN   Name=LOC107780525 {ECO:0000313|RefSeq:XP_016456565.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016456565.1};
RN   [1] {ECO:0000313|Proteomes:UP000084051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [2] {ECO:0000313|RefSeq:XP_016456565.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Lipolytic acyl hydrolase (LAH).
CC       {ECO:0000256|RuleBase:RU361262}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000256|ARBA:ARBA00004116}.
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. {ECO:0000256|RuleBase:RU361262}.
CC   -!- SIMILARITY: Belongs to the patatin family.
CC       {ECO:0000256|ARBA:ARBA00010240, ECO:0000256|RuleBase:RU361262}.
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DR   RefSeq; XP_016456565.1; XM_016601079.1.
DR   AlphaFoldDB; A0A1S3YWX7; -.
DR   SMR; A0A1S3YWX7; -.
DR   PaxDb; 4097-A0A1S3YWX7; -.
DR   GeneID; 107780525; -.
DR   KEGG; nta:107780525; -.
DR   OMA; GNKYEFN; -.
DR   OrthoDB; 772842at2759; -.
DR   Proteomes; UP000084051; Unplaced.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   PANTHER; PTHR32176:SF85; PATATIN GROUP D-2; 1.
DR   PANTHER; PTHR32176; XYLOSE ISOMERASE; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|RuleBase:RU361262};
KW   Lipid degradation {ECO:0000256|RuleBase:RU361262};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU361262};
KW   Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Storage protein {ECO:0000256|ARBA:ARBA00022761};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..392
FT                   /note="Patatin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010262928"
FT   DOMAIN          32..230
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
SQ   SEQUENCE   392 AA;  42489 MW;  060CB9F72B03A3E7 CRC64;
     MAITGSFFIL FLLVLTTTGS TSSVVGEMVT VLSIDGGGIK GIIPAIVLSF LESELQELDC
     DEDARLADYF DVIAGTSTGG ILTTMISAPN EKGRPFSAAK DIVSFYFDHG PCIFPPGASP
     PFFAPKYDGK YLHNVLQEKL GETRLNQTLT NVVIPTFDMK KLQPIIFTKS EIANSPQLDA
     KLSDICIGTS AAPTYFPPYY FENDDGKGNK YEFNLIDGGV VAGNPALIAL STVINSTETD
     PSFASIKPMD DKNILLLSLG TGTIADFAGK YTAEEAAHWG LVSWLFHNNS NPLNEMTSAA
     SAIMNDYYIT TIYRALGAKI NYLRIEENAL TGTTTQMDNA TEANMNLLVQ VGENLLKKPA
     SNGNPETNEE ALKRFAKLLS ERKKLRANKA SQ
//
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