ID A0A2K6JTG5_RHIBE Unreviewed; 1235 AA.
AC A0A2K6JTG5;
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:ENSRBIP00000002306.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000002306.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000002306.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000002306.1}
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; A0A2K6JTG5; -.
DR STRING; 61621.ENSRBIP00000002306; -.
DR Ensembl; ENSRBIT00000012446.1; ENSRBIP00000002306.1; ENSRBIG00000011306.1.
DR GeneTree; ENSGT00940000162262; -.
DR OMA; ECKHTEI; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000233180; 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:UP000233180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 180..273
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 291..341
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 362..413
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 451..586
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1235 AA; 138074 MW; 726A66B5FED1DFB5 CRC64;
PPPAPPLLSE PSPEPVPEPC PEPAPGPCLE ATSEPATELY TEPTPEPATE PAPEPATEPA
PEPATEPAPE PATEPAPEPA PEPATEPAPE PTPEPAPESV PEQAPELTPE VTPEPAPEPT
PEPVTELAPE FCPEAPPESR PSPAPCLLQC PVDTRERGLK TSPSPLPSPR TPMSWSRIKK
ILKEGPMLKN CNSFKRWKLR YFLVQGQKLY FAHHPAFAHF ETIDLSQAAV AESSCRNLCH
SFCVITPQRK ITLAAPNRKD MEEWINVIKT VQQGEIYKIP AAENNPFLVG MHYWYSSYSH
RTQHCNVCRE SIPALSRDAI ICEVCKVKSH RLCALRASKD CKWNTLSITD DLLLPADEVN
MPHQWVEGNM PVSSQCAVCH ENCGSYQRLQ DFRCLWCNST VHDDCRRRFS KECCFGSHRS
SVIPPTALSD PKGDGQLVVS SDFWNLDWSS ACSCPLLIFI NSKSGDHQGI VFLRKFKQYL
NPSQVFDLLK GGPEAGLSMF KNFARFRILV CGGDGSVSWV LSLIDAFGLH EKCQLAVIPL
GTGNDLARVL GWGAFWNKSK SPLDILNRVE QASVRILDRW SVMIRETPRQ TPLLKGQVEM
DVPRFEAAAI QHLESAATEL NKILKAKYPT EMIIATRFLC SAVEDFVIDI VKAWGQIKQN
NTAIVSVILK SDLMYDKLSV LIDVLAEEAA TTSAEKSATV YADSSKADRK PFVLQIDHIA
KCKLELATKA QNLQKSLKLI IFQVEQALDE ESRQTISVKN FSSTFFLEDD PEDTNQTSPR
RRSRRGTLSA ISSLKSEDLD NLNLDHLYFT PESIRFKEKC VMNNYFGIGL DAKISLDFNT
RRDEHPGQYN SRLKNKMWYG LLGTKELLQR SYRKLEERVH LECDGETISL PNLQGIVVLN
ITSYAGGINF WGSNTATTEY EAPAIDDGKL EVVAIFGSVQ MAMSRIVNLH HHRIAQCHEV
MITIDGEEGI PVQVDGEAWI QRPGLIKIRY KNAAQMLTRD RDFENSMKMW EYKHTEIQAA
PQPQLDSQDS QESLSDEEYA QMQHLARLAE NLISKLNDLS KVHQHVSVLM DSVNASANIL
NDIFYGQDSG NEMGAASCIP IETLSRNDAV DVTFSLKGLY DDTTAFLDEK LLRSAEDETA
LQSTLDAMNK EFKKLSAIDW MNPIFAPEEK SSDTDSRSLR LKIKFPKLGK KKLEEEHKPK
SGQSVQSFVG SLWHRRHCED EAKGDDPLTP SRSQL
//
