ID A0A3B6TR88_WHEAT Unreviewed; 422 AA.
AC A0A3B6TR88;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN ORFNames=CFC21_111398 {ECO:0000313|EMBL:KAF7111375.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS7D02G491200.1};
RN [1] {ECO:0000313|EMBL:KAF7111375.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7111375.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS7D02G491200.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS7D02G491200.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS7D02G491200.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7111375.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7111375.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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|ARBA:ARBA00010240, ECO:0000256|RuleBase:RU361262}.
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DR EMBL; CM022231; KAF7111375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6TR88; -.
DR SMR; A0A3B6TR88; -.
DR STRING; 4565.A0A3B6TR88; -.
DR PaxDb; 4565-Traes_7DL_F71DA020E-1; -.
DR EnsemblPlants; TraesCS7D02G491200.1; TraesCS7D02G491200.1; TraesCS7D02G491200.
DR Gramene; TraesCAD_scaffold_032559_01G000200.1; TraesCAD_scaffold_032559_01G000200.1; TraesCAD_scaffold_032559_01G000200.
DR Gramene; TraesCLE_scaffold_078275_01G000100.1; TraesCLE_scaffold_078275_01G000100.1; TraesCLE_scaffold_078275_01G000100.
DR Gramene; TraesCS7D02G491200.1; TraesCS7D02G491200.1; TraesCS7D02G491200.
DR Gramene; TraesCS7D03G1162900.1; TraesCS7D03G1162900.1.CDS; TraesCS7D03G1162900.
DR Gramene; TraesKAR7D01G0435290.1; cds.TraesKAR7D01G0435290.1; TraesKAR7D01G0435290.
DR Gramene; TraesPAR_scaffold_015330_01G000200.1; TraesPAR_scaffold_015330_01G000200.1; TraesPAR_scaffold_015330_01G000200.
DR Gramene; TraesRN7D0101195400.1; TraesRN7D0101195400.1; TraesRN7D0101195400.
DR Gramene; TraesROB_scaffold_050890_01G000100.1; TraesROB_scaffold_050890_01G000100.1; TraesROB_scaffold_050890_01G000100.
DR Gramene; TraesWEE_scaffold_028946_01G000100.1; TraesWEE_scaffold_028946_01G000100.1; TraesWEE_scaffold_028946_01G000100.
DR OMA; GLLEPCQ; -.
DR OrthoDB; 1090545at2759; -.
DR Proteomes; UP000019116; Chromosome 7D.
DR Proteomes; UP000815260; Chromosome 7D.
DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07214; Pat17_isozyme_like; 1.
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:SF79; PATATIN; 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 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:UP000019116}.
FT DOMAIN 45..248
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 422 AA; 45844 MW; 0FAE8CE93F5AFB4F CRC64;
MPVTQAPGRS TGPVSVARRE LSSHAWSLSS PASPQPRYGS IVTVLSIDGG GVRGIIPGTI
LAFLEEKLQE LDGPDVRIAD YFDVVAGTST GGLVAAMLTA PNAEGRPLFA AKDVNKFYLE
HCPNIFPAVC KGPLGWLKSM MGPKYSGHHL HKVVKELLGD TRVNETLKNI VIPTFDIKLL
QPTIFSTYDA MRDVSKNALL SDVCISTSAA PTYLPGHHFE SKDKDGKTRA FNLIDGGVVA
NNPTLLAMTH VSKQILMGNQ DFLPIKHAGY GKFMILSLGT GTAKIEEKFD AAECGKWGLL
GWLYKRGATP IIDSFSEAST DLVDIQASVL FQVLGCNKSY LRIQHDELTG EMASVDVSTS
KNLNGLISVG KALLKRQVCK VNVETGKNEP DLERGTNEQE LARFARMLSE ERKARKEAYK
LV
//
