ID A0A061F0U9_THECC Unreviewed; 434 AA.
AC A0A061F0U9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN ORFNames=TCM_026246 {ECO:0000313|EMBL:EOY10975.1};
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:EOY10975.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY10975.1, 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; CM001883; EOY10975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061F0U9; -.
DR EnsemblPlants; EOY10975; EOY10975; TCM_026246.
DR Gramene; EOY10975; EOY10975; TCM_026246.
DR HOGENOM; CLU_000288_144_0_1; -.
DR Proteomes; UP000026915; Chromosome 5.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
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:SF114; 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 12..263
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 434 AA; 48309 MW; C1003647C34E76F9 CRC64;
MATEGKKLTT ILSIDGGGVR GIIPATILAF LESELQKLDG KEARIADYFD FIAGTSTGGL
VTAMLSSPDP DDPSNRPFSA GKILQFYFAE SANIFPQKPK QPRHIDEMSR LEHAVNQFVQ
SMGSIPEDEY GRERLRFMFP DCRSLIDLVV RLWKFVFDPK FNGEKLKEVV EEKVGDRRLS
ETLTNVIIPS FDIKLLQTVV FSTLKAARDD LEDAPLQDVC LSTSAAPYYL PLHKFEINSV
NRSRNFNMVD GGVAANNPTL LALSEVAKEM SLDGKAQCLD NMDCSKFLVL SLGTGSSKRN
NKLEIVNENW GPLRWLWGDN GIPFLDVLMN AIDAMVDIYL SAFFRGASFE DNYLRIQTDS
LNDSEIGMDN SNLENLQNLE NIGNELLEKP VSAMNLETGL LKPIRGAGTN RAAIIKLAKR
LSEERKRRLA QSSA
//
