ID A0A061FCS4_THECC Unreviewed; 381 AA.
AC A0A061FCS4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN ORFNames=TCM_033882 {ECO:0000313|EMBL:EOY14527.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY14527.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY14527.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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 EMBL; CM001886; EOY14527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FCS4; -.
DR EnsemblPlants; EOY14527; EOY14527; TCM_033882.
DR Gramene; EOY14527; EOY14527; TCM_033882.
DR eggNOG; KOG0513; Eukaryota.
DR HOGENOM; CLU_000288_144_0_1; -.
DR InParanoid; A0A061FCS4; -.
DR OMA; LQSENCY; -.
DR Proteomes; UP000026915; Chromosome 8.
DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR32176:SF38; 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:UP000026915}.
FT DOMAIN 15..206
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 381 AA; 41696 MW; 173A795D59CF71CB CRC64;
MEHQLPTYGE KIIILSIDGG GIRGIIPGTV LAFLEAQLQK LDGEEARLAD YFDIIAGTST
GGLVTAMLTA QNQKNCPLYA AKGIKDFYLE HCPKIFPQDR SPLAPAANFL KTITGPKYDG
KYLHKLFERK VGRNTTEPGT GQRCDPNGKV DPWRNALLSD ICIGTSPATT FLPAHHFKTQ
DSKGVVKEFN LIDGGVAAND PALVAVSEMT KEIVRRSPEF FPIKPTDYSR FVVISLGTGS
AKSVEKFDAD EAAKWGVLGW LTSENSTPLV DIFTQASSDM TEYHLAAVFQ ALQSENCYLR
IQDDTLTGPL ASVDIATKQN LENLVNVGVD FLKKPALRVN LETGKMEPSD LGTNEKALIS
YLLEKRLRDM RAPRGSTATK K
//
