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Database: UniProt
Entry: A0A2P5BLR6_PARAD
LinkDB: A0A2P5BLR6_PARAD
Original site: A0A2P5BLR6_PARAD 
ID   A0A2P5BLR6_PARAD        Unreviewed;       107 AA.
AC   A0A2P5BLR6;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN   ORFNames=PanWU01x14_227770 {ECO:0000313|EMBL:PON49741.1};
OS   Parasponia andersonii (Sponia andersonii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX   NCBI_TaxID=3476 {ECO:0000313|EMBL:PON49741.1, ECO:0000313|Proteomes:UP000237105};
RN   [1] {ECO:0000313|Proteomes:UP000237105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PON49741.1}.
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DR   EMBL; JXTB01000255; PON49741.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5BLR6; -.
DR   OrthoDB; 1079044at2759; -.
DR   Proteomes; UP000237105; Unassembled WGS sequence.
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:SF108; 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|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU361262};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU361262};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237105}.
FT   DOMAIN          22..107
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
SQ   SEQUENCE   107 AA;  11601 MW;  02E9DAC793903887 CRC64;
     MEGTNATVRL QPPTYGNLIT VLSIDGGGIR GIIPGTILSF LEEELQKLDG EDARLADYFD
     VIAGTSTGGL VTAMLTAPNE KNRPVFAAKD IKDFYLTQCP KIFPQNR
//
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