ID A0A287AQF5_PIG Unreviewed; 1079 AA.
AC A0A287AQF5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 34.
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=DGKI {ECO:0000313|Ensembl:ENSSSCP00000046130.2,
GN ECO:0000313|VGNC:VGNC:87274};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000046130.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000046130.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000046130.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000046130.2}
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-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; A0A287AQF5; -.
DR Ensembl; ENSSSCT00000046679.3; ENSSSCP00000046130.2; ENSSSCG00000016521.5.
DR VGNC; VGNC:87274; DGKI.
DR GeneTree; ENSGT00940000158094; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000008227; Chromosome 18.
DR Bgee; ENSSSCG00000016521; Expressed in hippocampal formation and 20 other cell types or tissues.
DR ExpressionAtlas; A0A287AQF5; baseline and differential.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
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:0005095; F:GTPase inhibitor activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046959; P:habituation; IEA:Ensembl.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR CDD; cd20850; C1_DGKiota_rpt1; 1.
DR CDD; cd20896; C1_DGKiota_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR047486; C1_DGKiota_rpt1.
DR InterPro; IPR047487; C1_DGKiota_rpt2.
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 PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF92; DIACYLGLYCEROL KINASE IOTA; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
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:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 373..508
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REPEAT 972..996
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1008..1040
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..350
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 119087 MW; 6EED223E218BD189 CRC64;
MDAAGRGCHL PPLPEARGPA RSPEVAAAVS AVRRPCFCSG AASAPSAAAG AVAMNPSSSA
GEEKGATGGS SSSGSGAGSC CLGAEGGADP RGAGAAAAAG AAALEEPGAA GPKEKDEALE
EKLRNLTFRK QVSYRKAISR AGLQHLAPAR PLSLPVANGP AKEPRATLDW SENAVNGEHL
WLETNVSGDL CYLGEESCQV RFAKSALRRK CAVCKIVVHT ACIEQLEKIN FRCKPTFREG
GSRSPRENFV RHHWVHRRRQ EGKCKQCGKG FQQKFSFHSK EIVAISCSWC KQAFHNKVTC
FMLHHIEEPC SLGAHAAVIV PPTWIIKVKK PQNSLKASNR KKKRTSFKRK ASKRGTEQEN
KGRPFVIKPI SSPLMKPLLV FVNPKSGGNQ GTKVLQMFMW YLNPRQVFDL SQEGPKDALE
LYRKVPNLRI LACGGDGTVG WILSILDELQ LSPQPPVGVL PLGTGNDLAR TLNWGGGYTD
EPVSKILCQV EDGTIVQLDR WNLHVERNPD LPPEELEDGV CKLPLNVFNN YFSLGFDAHV
TLEFHESREA NPEKFNSRFR NKMFYAGAAF SDFLQRSSRD LSKHVKVVCD GTDLTPKIQE
LKFQCIVFLN IPRYCAGTMP WGNPGDHHDF EPQRHDDGYI EVIGFTMASL AALQVGGHGE
RLHQCREVML LTYKSIPMQV DGEPCRLAPA MIRISLRNQA NMVQKSKRRT SMPLLNDIHQ
VQAADLRRVS APPGSFTIPQ SVPDRLRIRV NKISLQDYEG FHYDKEKLRE ASIPLGILVV
RGDCDLETCR MYIDRLQEDL QSVSSGSQRV HYQDHETSFP RALSAQRLSP RWCFLDATSA
DRFYRIDRSQ EHLHFVMEIS QDEIFILDPD MVLSQQAGTP PGMPDLVVEQ ASGMTDWWNP
ALRKRMLSDS GLGMITPHYE DSDLRDFSHS RVLQSPVSSE DHAILQAVIA GDLMKLIESY
KNGGSLLIQG PDHCSLLHFA AKTGNGEIVK YILDHGPSEL LDMADSETGE TALHKAACQR
NRAVCQLLVD AGASLRKTDS KGKTPQERAQ QAGDPDLAAY LESRQNYKII GHEDLETAV
//
