ID A0A1S3VFJ2_VIGRR Unreviewed; 438 AA.
AC A0A1S3VFJ2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN Name=LOC106774533 {ECO:0000313|RefSeq:XP_014517045.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014517045.1};
RN [1] {ECO:0000313|RefSeq:XP_014517045.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014517045.1};
RG RefSeq;
RL Submitted (NOV-2023) 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|RuleBase:RU361262}.
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DR RefSeq; XP_014517045.1; XM_014661559.2.
DR AlphaFoldDB; A0A1S3VFJ2; -.
DR GeneID; 106774533; -.
DR KEGG; vra:106774533; -.
DR OrthoDB; 518048at2759; -.
DR Proteomes; UP000087766; Chromosome 10.
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:UP000087766}.
FT DOMAIN 69..262
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 417..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 438 AA; 47009 MW; A7E9886623A08E5C CRC64;
MAAMSTSPMN LNMIDSNFQV DKLTNEIFSI LENNFLFGYG DAENRTNSVQ NARDAKPAKH
SAGKVRILCI DGAGATDGIL AAKSLAHLEA CLRRKSGDAN SRVADFFDAA AGSGVGGVLA
ALLFTRGKDG QPLFTAEEAL RFLSDNRRRI SRRPGILRRV LRPESKAEKL FRKTFGECTL
RDTVKPVLIP CYDLVTRAPF VFSRADALEM DGYDFKMSDV CAATSADPSF AGPTEMRSVD
GRTRIVAVDG GVAMNNPTAA AITHVLNNKH EFPFCNGVAD LLVLSLGNGE SDFNAVKSPS
GFVKIAGEGA SDMVDQAVSM AFGDCRMSNY VRIQSSGVMS KANKGAQVKS CKSETDLVAV
SEEMLSQKNV ESVLFKGKKV ANNSNLEKLE LFGGEIIKEG ERRKTCILPT VVLKNNNASP
SPSRTSSATT LSTLSSNC
//
