ID A0A2K6TX41_SAIBB Unreviewed; 1266 AA.
AC A0A2K6TX41;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=DGKK {ECO:0000313|Ensembl:ENSSBOP00000024236.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000024236.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000024236.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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=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; A0A2K6TX41; -.
DR STRING; 39432.ENSSBOP00000024236; -.
DR Ensembl; ENSSBOT00000041096.1; ENSSBOP00000024236.1; ENSSBOG00000028597.1.
DR GeneTree; ENSGT00940000162262; -.
DR OMA; ECKHTEI; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005886; C:plasma membrane; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030168; P:platelet activation; IEA:UniProt.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR CDD; cd20800; C1_DGK_typeII_rpt1; 1.
DR CDD; cd20852; C1_DGK_typeII_rpt2; 1.
DR CDD; cd13274; PH_DGK_type2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF33; DIACYLGLYCEROL KINASE KAPPA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50003; PH_DOMAIN; 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 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:UP000233220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 211..304
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 322..372
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 393..444
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 482..617
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..111
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1266 AA; 141855 MW; E5C133800ACE6D41 CRC64;
MDRGAAASQD TAPPQDGEQP AESPEPPPPW PPPPPPPAPP PAPPPPLSEP SPEPVPEPCP
ELAPGPCPEA TSEPATELYT ELAPEPATEP APEPAPELVP EPTPEPAPDW VQELPPESAT
DRVPEPTPEL APEPAPELTP ELALEPAPEP TPEPVTELAP EFCPEVAPES RPSPAPGLLP
CPVDTRERGL KTSPTPLPSP RTPMSWSRIK KILKEGPLLK NCNSLKRWKP RYFLIQGQKL
YFAHHPAFAH FDTIDLSEAV VAESSCRNLC HSFCVITPQR KITVAASNRK DMEEWINVIK
TVQQGEIHKI PAAENNPFLV GMHYWYSSYS HRTQHCNVCR ESIPALSRDV IICEVCKVKS
HRLCALRASK DCKWNTLSLT DDLLLPADEV NMPHQWAEGN MPVGSQCAVC HESCGSYQRL
QDFRCLWCNS TVHDDCRRRF SKECCFGNHR SSVIPPTALS DPNGDGQLVV SSDFWNLDWS
STCSCPLLIF INSKSGDHQG IVFLRKFKQY LNPSQVFDLL KGGPEAGLCM FKNFARFRIL
VCGGDGSVSW VLSLIDAFGL HERCQLAVIP LGTGNDLARV LGWGAFWNKS KSPLDILNRV
EQASVRFLDR WSVMIRETPR QIPLLKGQVE MDVPRFEAAA IQRVESAATE LNKILKAKYP
TEIIIATRFL CSAVEDFVLN IVKAWGQIKQ SNTAIQSVIL KSDLMYDKLS VVMDVLAEEA
ADTSVEKSAT VPADSSKADR KSFIPQMDHI AKYRLELTTK AQNLQKSLKL IIFQVEQVLD
EESRQTISVK NFGSTFFLED DPEDISQTSP RRRSRRGTLS SISSLKSEDL DNLNLDHLHF
TPETIRFKEK CVMNNYFGIG LDAKISLDFN TRRDEHPERY NSRLKNKMWY GLLGSKELLQ
RTYRKLEERV HLECDGEPIS LPNLQGIVVL NITSYAGGIN FWGSNAATME YEAPAIDDGK
LEVVAIFGSV QMAMSRIINL HHHRIAQCRE VMITIDGEEG IPVQVDGEAW IQRPGLIKIR
YKNAAQMLTR DRDFENSMKT WECKHTEIQA APQPQLHSQD SQECLSDEEY AQMQHLARLA
ENLISRLNDL SKVHQHVSVL MDSVNASANV LNNTFYGQDS GSELGAASCI PIETLSRNDA
VDITFSLKGL YDDTTAFLDE KLLRSSEDEA TLQSTLDAMN KEFKKLSEID WMNSIFVSEE
KSSDTDSRSL RLKIKFPKLR RKKLEEERKP ESGQSVQGFI GRLWHRRHRE DEAKGDDPPT
PSRSQL
//
