ID G1MD26_AILME Unreviewed; 803 AA.
AC G1MD26;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Diacylglycerol kinase {ECO:0000256|RuleBase:RU361128};
DE Short=DAG kinase {ECO:0000256|RuleBase:RU361128};
DE EC=2.7.1.107 {ECO:0000256|RuleBase:RU361128};
GN Name=DGKB {ECO:0000313|Ensembl:ENSAMEP00000017254.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000017254.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000017254.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000017254.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00023371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000256|ARBA:ARBA00023371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43428, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18155, ChEBI:CHEBI:30616, ChEBI:CHEBI:78227,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023395};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000256|ARBA:ARBA00023395};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000256|ARBA:ARBA00023400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:456216; EC=2.7.1.107;
CC Evidence={ECO:0000256|RuleBase:RU361128};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00005175}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR AlphaFoldDB; G1MD26; -.
DR STRING; 9646.ENSAMEP00000017254; -.
DR Ensembl; ENSAMET00000017961.2; ENSAMEP00000017254.2; ENSAMEG00000016332.2.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000159770; -.
DR HOGENOM; CLU_003770_1_0_1; -.
DR InParanoid; G1MD26; -.
DR TreeFam; TF313104; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR CDD; cd20845; C1_DGKbeta_rpt1; 1.
DR CDD; cd20891; C1_DGKbeta_rpt2; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 2.60.200.40; -; 2.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 1.10.238.110; Diacylglycerol kinase alpha; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR047471; C1_DGKbeta-like_rpt1.
DR InterPro; IPR047470; C1_DGKbeta_rpt2.
DR InterPro; IPR029477; DAG_kinase_typeI_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR038199; DGK_typeI_N_sf.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF32; DIACYLGLYCEROL KINASE BETA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF14513; DAG_kinase_N; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 148..183
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 193..228
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 243..293
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 308..357
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 433..567
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 386..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 90466 MW; 66EA5F5A30EE6F97 CRC64;
MTNQEKWAHL SPSEFSQLQK YAEYSTKKLK DVLEEFHGNG VLAKYNPEGK QDILNQTIDF
EGFKLFMKTF LEAELPDDFT AHLFMSFSNK FPHSSPMVKS KPALLSGGLR MNKGAITPPR
TSPANTCSPE VIHLKDIVCY LSLLERGRPE DKLEFMFRLY DTDGNGFLDS SELENIISQM
MHVAEYLEWD VTELNPILHE MMEEIDYDHD GTVSLEEWIQ GGMTTIPLLV LLGLENNVKD
DGQHVWRLKH FNKPAYCNLC LNMLIGVGKQ GLCCSFCKYT VHERCVARAP PSCIKTYVKS
KKNTDVMHHY WVEGNCPTKC DKCHKTVKCY QGLTGLHCVW CQITLHNKCA SHLKPECDCG
PLKDHILPPT TICPVVLQTL PTSGVSVPEE RQATVKKEKG GSQQSNKVTD KNKMQRANSV
TVDGQGLQIT PVPGTHPLLV FVNPKSGGKQ GERIYRKFQY LLNPRQVYSL SGNGPMPGLN
FFRDVPDFRV LACGGDGTVG WILDCIEKAN VVKHPPVAIL PLGTGNDLAR CLRWGGGYEG
ENLMKILKDI ENSTEIMLDR WKFEVIPNDK DEKGDPVPYS IINNYFSIGV DASIAHRFHI
MREKHPEKFN SRMKNKFWYF EFGTSETFSA TCKKLHESVE IECDGVQIDL INISLEGIAI
LNIPSMHGGS NLWGESKKRR SHRRIEKKGS DKRTTLTDAK ELKFASQDLS DQLLEVVGLE
GAMEMGQIYT GLKSAGRRLA QCSSVVIRTS KSLPMQIDGE PWMQTPCTIK ITHKNQAPML
MGPPPKTGLF CSLVKRTRNR SKE
//
