ID A0A2P5DLM1_TREOI Unreviewed; 446 AA.
AC A0A2P5DLM1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-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=TorRG33x02_247530 {ECO:0000313|EMBL:PON74174.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON74174.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
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|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:PON74174.1}.
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DR EMBL; JXTC01000262; PON74174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5DLM1; -.
DR STRING; 63057.A0A2P5DLM1; -.
DR InParanoid; A0A2P5DLM1; -.
DR OrthoDB; 518048at2759; -.
DR Proteomes; UP000237000; 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 CDD; cd07199; Pat17_PNPLA8_PNPLA9_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; PTHR32241:SF12; OS03G0784100 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000237000}.
FT DOMAIN 72..268
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 426..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 47396 MW; AA4CAF86BA209FB0 CRC64;
MAALSSLPML NMDSSYGVDK LTYEIFSILE NKFLFGYGDP NSKISNPEKP HNLISSTNGG
GGSSNGKVRI LSIDGGGATD GLLAADSLSR LEASLREKSG NPNAAIADYF DVVAGSGAGG
VLAAMLFTRG RDGGPLFTAE AALKFMAKNR RKIFRSSPAG FFRRVLMPAA GRAEKLFGKV
FGELSLRDTL KSVLIPCYDL ATGAPFLFSR ADAFEMDGYD FKMRDVCAAT SADPTTAGAF
EMKSVDQRTK ILAVDGGIAM NNPTAAAITH VLNNKQEFPL CNGVEDLLVV SLGNGESEFG
AGDVTSSPAT ARLLRIAGEG ASDLVDQAVS MAFGECRASN YIRIQGNGII AKNYGGSEKA
KMSNKKMDML KETENMLSQK NVESVLFSGK RIVGSSNIEK IDLFASELVK EQERRKTSIL
PMVALKQMSP SPRTSSATTL SSLSSN
//
