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
//