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Database: UniProt
Entry: A0A0D3B7L2_BRAOL
LinkDB: A0A0D3B7L2_BRAOL
Original site: A0A0D3B7L2_BRAOL 
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
//
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