ID A0A368QNS0_SETIT Unreviewed; 429 AA.
AC A0A368QNS0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN ORFNames=SETIT_3G386800v2 {ECO:0000313|EMBL:RCV19464.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV19464.1};
RN [1] {ECO:0000313|EMBL:RCV19464.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV19464.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV19464.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV19464.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipolytic acyl hydrolase (LAH).
CC {ECO:0000256|RuleBase:RU361262}.
CC -!- FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH)
CC activity. Hydrolyzes phospholipids as well as galactolipids. May play a
CC role in disease resistance. {ECO:0000256|ARBA:ARBA00025642}.
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|RuleBase:RU361262}.
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DR EMBL; CM003530; RCV19464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368QNS0; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; PTHR32241:SF4; OS12G0611300 PROTEIN; 1.
DR PANTHER; PTHR32241; PATATIN-LIKE PROTEIN 6; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
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}.
FT DOMAIN 54..258
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 429 AA; 43950 MW; A03BBD8E31DC87AE CRC64;
MASPPADVDL GKLSYEIFSL LESKFLFGGA GSVPGTPARA AAAAGEDRGR VRVLAIDGCG
PGPGDALLAA VALARLEAAL RERAGDPDAR VADFFDAAAG AGAGGVLAAM LFLKGEDGRA
RYTAADALAF VAASLGRKQG GWGGDGGGGR RSRWAALLFR RGERSSPLRR VFGDATLRDT
VAPLLVPCYD LATAAPFLFS RADAVESDSF DFHLRDVCAA TCAGGAAAAA VRSVDGRTSI
AAASGGVAAM GNPAAAAITH VLHNKQEFPL AAGVDDLLVV SIGSGSSAGA GAAASATPSA
GWRTPMPPRS PSPAEMVRLT AEGVADMVDQ AVAMAFGHTC GRNYVRIQAA SPACSGKKSV
DPKKAVAVAD GMLTQRNVEA ELFRGRRLSE KSNREKLDAF AAELVKEHER RARSHGLPNV
VIKQGSYSH
//
