ID A0A3B3V293_9TELE Unreviewed; 887 AA.
AC A0A3B3V293;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=DGKQ {ECO:0000313|Ensembl:ENSPLAP00000019021.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000019021.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000019021.1}
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 RefSeq; XP_014906016.1; XM_015050530.1.
DR AlphaFoldDB; A0A3B3V293; -.
DR STRING; 48699.ENSPLAP00000019021; -.
DR Ensembl; ENSPLAT00000017094.1; ENSPLAP00000019021.1; ENSPLAG00000023980.1.
DR GeneID; 106958576; -.
DR KEGG; plai:106958576; -.
DR CTD; 1609; -.
DR GeneTree; ENSGT00940000159492; -.
DR OrthoDB; 4642163at2759; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000261500; Unplaced.
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:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
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 CDD; cd20803; C1_DGKtheta_typeV_rpt1; 1.
DR CDD; cd20804; C1_DGKtheta_typeV_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
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; IPR000159; RA_dom.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 3.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 35..83
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 96..143
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 158..208
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 530..667
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 859..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 97844 MW; 6D1A7DEB3C70B4D0 CRC64;
MAESTRPSPA DPDAANCRAA SPAAVKRRAQ QSTMGHCFKK VTLTKPTFCH SCSDFVWGLI
GFLCEVCNFM CHEKCLKTLR AVCTCMAPSK VQVPVAHCFG PAGQKKRFCC VCRKQTEGST
ALRCEVCELH VHADCAAFSC ADCRCCHLDQ NLQQESLQHQ WREGDPASAR CEFCRRSCGS
SEVLSGLRCE WCGVTSHASC CHRLPAECAL GRLRSMLLPP PCVRLQSRNF SKMQCYRIGE
SGSQDRNNWD EAEPAAAAPR ELQSAAPETS KQVFKVFDGD DALRRGFFRL APSCRGVKNE
EVEAALRAFY LPGEPHDFDL ENVGAVQHHH SSDARVLRAK LRRDDVIKVH AAWSRSSAVS
VEVSETSTAA SVLSDVLLQL DRQGEDASSF SLQEVYMSSK QVQRQTLSPQ EKMVDKLQEI
RKLSLRQMNQ TRFYIVQNQN PAVQVGLLIS GLPPLLTKEE YCGLLEEHLD FKGHLVALTH
FYEAQGAVAL QISCFAEAER IYMLSKDTTI SNKTLTSLII PEIQCQKLGD AVCPLLVFVN
PKSGGLKGRE LLHSFRKLLN PHQVFDITNG GPLAGLHAFR EVPRFRVLVC GGDGTVGWVL
GVLETVRHKL VCREPPIGIV PLGTGNDLAR ILRWGPGYGG DDPYHILASV DEADEVQMDR
WTILLDAQDV SEDGKDSGVL EPPKIVQMNN YFGLGIDAEL SLDFHLAREG EPDKFTSRFH
NKGVYVKVGL QKISRSRSLH KELQLQVDKQ PVPLPNIEGL IFLNIPSWGS GADLWGSEAD
GRFSRPRIDD GLLEVVGVTG VVHMGQVQSG LRSGIRIAQG SYIRLIVSKE LPVQVDGEPW
LQAPGHIIIS AAGPKVRMLR KSKLKQRKSP SSSDGRSDSP SSRDGGH
//
