ID A0A3B6HMC7_WHEAT Unreviewed; 433 AA.
AC A0A3B6HMC7;
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};
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:TraesCS4A02G017400.1};
RN [1] {ECO:0000313|EnsemblPlants:TraesCS4A02G017400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS4A02G017400.1};
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 [2] {ECO:0000313|EnsemblPlants:TraesCS4A02G017400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
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 AlphaFoldDB; A0A3B6HMC7; -.
DR SMR; A0A3B6HMC7; -.
DR STRING; 4565.A0A3B6HMC7; -.
DR PaxDb; 4565-Traes_4AS_D2A85E4CA-1; -.
DR EnsemblPlants; TraesCS4A02G017400.1; TraesCS4A02G017400.1; TraesCS4A02G017400.
DR Gramene; TraesCS4A02G017400.1; TraesCS4A02G017400.1; TraesCS4A02G017400.
DR Gramene; TraesCS4A03G0029600.1; TraesCS4A03G0029600.1.CDS; TraesCS4A03G0029600.
DR OMA; MVGLFQS; -.
DR OrthoDB; 1090545at2759; -.
DR Proteomes; UP000019116; Chromosome 4A.
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:SF60; 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 53..256
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 433 AA; 46694 MW; 22772D8139E79839 CRC64;
MSPVHVPELS SGGSGSGSLT LNPVQRALSR LSSSSALTPR SPPPSYGSIV TVLSIDGGGV
RGIIPGTILA FLEEKLQELD GPDVRIADYF DVIAGTSTGG LVTAMLTAPD AKGRPLFAAK
DINNFYLEHC PKIFPAGYGG PLGLLRSMRG PKYDGQYLHS VVKELLGETR VGEALQNIVI
PTFDIKLLQP TIFSRYDARN DVSKNALLSD VCISTSAAPT YLPGHHFETK DKDGRPRAFN
LIDGGVAANN PTMLAMTDVS KQILLGNQDF FPIKPADYGK FMVLSLGTGS AKVEEKFDAA
ACSKWGILGW LYNHGATPLI DSFSQASADL VDIQASVLFQ ALRCEKRYLR IQDDELKGDT
SSVDVSTPEN LNRLVEVGKA LLKRSVCRVN VETGKTVPDD NRGTNEEELI GFAHMLSQER
KARLQKKGVT ITQ
//
