ID W9RIQ0_9ROSA Unreviewed; 467 AA.
AC W9RIQ0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN ORFNames=L484_013411 {ECO:0000313|EMBL:EXB80085.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB80085.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE344800; EXB80085.1; -; Genomic_DNA.
DR RefSeq; XP_010099619.1; XM_010101317.1.
DR AlphaFoldDB; W9RIQ0; -.
DR STRING; 981085.W9RIQ0; -.
DR GeneID; 21396583; -.
DR KEGG; mnt:21396583; -.
DR eggNOG; KOG0513; Eukaryota.
DR OrthoDB; 518048at2759; -.
DR Proteomes; UP000030645; 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; PATATIN-LIKE PROTEIN 6; 1.
DR PANTHER; PTHR32241:SF3; 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:UP000030645}.
FT DOMAIN 86..295
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 467 AA; 50897 MW; A13B49EB43E1CB55 CRC64;
MMNENININN QPEMHEPSID TDKLSYEIFS ILESKFLFGY DDQKLWVPKQ IAPAPTAGEA
PPQSLVSGET NGVSAIKNQR GKICILSIDG GGMRGILSGK ALAYLEQSLK AKSGNPDARI
ADYFDVAAGA GVGGIFTAML FATRDQSRPI SKADDTWRFL TDNGRRFYRS TPNSGGFLRR
IFRASGGSSG SATAGLEKSM KEVFVEKGRS LTLKDTLKPV LIPCYDLSST APFLFSRADA
LETDSFDFEL WEVCRATSAE PGSFEPVQMR SVDGQTRCLA VDGGLAMSNP TAAAITHVLH
NKQEFPFVRG VEDLLVLSIG TGQLLEVSYE GEQVRKWKAK EWARPTARIT TDASADFVDQ
AVSMAFGHSR STNYVRVQAN GSSLGRCGPN VDTDSSPGNV NMLLGLAEEM LKQKNVESVL
FGGKKIGEQS NFEKLDWFAG ELVLEHQRRS CRIAPTVAFK QATSKTI
//
