ID A0A0D3B7L2_BRAOL Unreviewed; 407 AA.
AC A0A0D3B7L2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Patatin {ECO:0000256|RuleBase:RU361262};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU361262};
GN Name=106332679 {ECO:0000313|EnsemblPlants:Bo3g042350.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo3g042350.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo3g042350.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo3g042350.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) 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|ARBA:ARBA00010240, ECO:0000256|RuleBase:RU361262}.
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DR RefSeq; XP_013626608.1; XM_013771154.1.
DR AlphaFoldDB; A0A0D3B7L2; -.
DR STRING; 109376.A0A0D3B7L2; -.
DR EnsemblPlants; Bo3g042350.1; Bo3g042350.1; Bo3g042350.
DR GeneID; 106332679; -.
DR Gramene; Bo3g042350.1; Bo3g042350.1; Bo3g042350.
DR KEGG; boe:106332679; -.
DR eggNOG; KOG0513; Eukaryota.
DR HOGENOM; CLU_000288_144_0_1; -.
DR OMA; PIEFNLI; -.
DR OrthoDB; 1201767at2759; -.
DR Proteomes; UP000032141; Chromosome C3.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblPlants.
DR GO; GO:0016020; C:membrane; IEA:EnsemblPlants.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblPlants.
DR GO; GO:0016298; F:lipase activity; IEA:EnsemblPlants.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:EnsemblPlants.
DR GO; GO:0051607; P:defense response to virus; IEA:EnsemblPlants.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:EnsemblPlants.
DR GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblPlants.
DR CDD; cd07214; Pat17_isozyme_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; PTHR32176:SF109; PATATIN-LIKE PROTEIN 2; 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|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW ProRule:PRU01161}; Reference proteome {ECO:0000313|Proteomes:UP000032141}.
FT DOMAIN 22..228
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT MOTIF 26..31
FT /note="GXGXXG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT MOTIF 64..68
FT /note="GXSXG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT MOTIF 215..217
FT /note="DGA/G"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT ACT_SITE 66
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 407 AA; 44478 MW; A4B7A83AC2601A7F CRC64;
MQMESPKSPL QPPTYGNLVT ILSIDGGGIR GIIPATILAF LESELQKLDG NEARLADYFD
VVAGTSTGGL VTAMLTAPNK EGRPLFAASE IKEFYLEHCP KIFPQNHFPF SATKNLVKSL
TGPKYDGEYL HQLIHAKLGD TRLHQTLTNV VIPTFDIKHL QPTIFSSYEV KKNPLKNATL
ADITISTSAA PTYLPAHFFK THDSAGNVKE YNLIDGGVAA NNPALVAIGE VTKEITRGSS
DFFPIRPNDY GRFLVLSLGT GTSKSEEKFN ANEVAGWGML SWLTHDNSTP LIDTFMQASS
DMVDFHLSAV FRALHSEANY IRIQDDTLNG DAASVDISTV ENLDILAKTG DELLKKPVSR
VNLESGCNEN AYEVTNEKAL IKLAGILSKE KMIRDSRSPH GKKPNSK
//