ID M1BAE3_SOLTU Unreviewed; 280 AA.
AC M1BAE3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN Name=102598099 {ECO:0000313|EnsemblPlants:PGSC0003DMT400040780};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400040780, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400040780}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400040780};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Lipolytic acyl hydrolase (LAH).
CC {ECO:0000256|RuleBase:RU361262}.
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; M1BAE3; -.
DR EnsemblPlants; PGSC0003DMT400040780; PGSC0003DMT400040780; PGSC0003DMG400015769.
DR Gramene; PGSC0003DMT400040780; PGSC0003DMT400040780; PGSC0003DMG400015769.
DR Gramene; RHC02H1G2704.2.1; RHC02H1G2704.2.1; RHC02H1G2704.2.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1BAE3; baseline and differential.
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; PTHR32176:SF120; 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:UP000011115}.
FT DOMAIN 1..110
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 280 AA; 31051 MW; 9B42B73E852F44DE CRC64;
MMNGPKYDGK YLHALTKRLL GGTRLHDTLT AVVIPTFDIK TLQPVIFSSY EANSKPDLDA
ELADICISTS AAPTFLPAYC FKTQDAQNKD REFNLIDGGV AANNPTLIAI GEVTKQVLMK
HEDLFPIKPM EYGRFLVISL GTGNAKNEGK YNAKMAAKWG LLSWLTHDNS TPIIEAFNQA
SADMVDYHNF VVFKALQSDD QYLRIQDDTL TGNLASVDIA TKENLEGLVK VGERLLDKPA
SKINLDKGVY EAVENGGTNK EALRRFAKTL SDERKFRQSK
//
