ID A0A1S3KUA0_SALSA Unreviewed; 1423 AA.
AC A0A1S3KUA0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=LOC106561949 {ECO:0000313|RefSeq:XP_013981894.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013981894.1};
RN [1] {ECO:0000313|RefSeq:XP_013981894.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013981894.1};
RG RefSeq;
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 RefSeq; XP_013981894.1; XM_014126419.1.
DR GeneID; 106561949; -.
DR CTD; 553380; -.
DR OrthoDB; 4642163at2759; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000087266; Chromosome ssa11.
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: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; cd20849; C1_DGKzeta_rpt1; 1.
DR CDD; cd20895; C1_DGKzeta_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 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; IPR047485; C1_DGKzeta_rpt1.
DR InterPro; IPR047484; C1_DGKzeta_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:SF43; DIACYLGLYCEROL KINASE ZETA; 1.
DR Pfam; PF12796; Ank_2; 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; PS50088; ANK_REPEAT; 1.
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:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 673..807
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REPEAT 1352..1384
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 77..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..651
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1423 AA; 159173 MW; 657EF04293C272DE CRC64;
MNRSVARSLS LSLSRATHGL KVRQAGKRRG WSFICFHQPL QRDIEKGTHK RWVVMDTFFR
RHFRLKGAEQ CQYRRPGVAV PTSKARRRSS VGLPSAGLVQ RRRSSVGLPF TGPVGRRRSS
AGLSPTSQSQ RRRSSVGLPS GYVGRRRSSV GLACAAHQQR RRSSEVQGLP HCYYGGGQLV
KTRYYTRRRS STTMVCVNPR FSVRRRQAAK LRTIDTQLLG PSMLLASLVQ MSAEQQRAPG
AQGGEGASGE GTESCPSSSC CSESEGDSCS QRECSTRSEG SGSEQEGTEA SSSSSSYPEG
ERTSPWQDWN QAHSMAALTM ESIQSRPLIR APRCLRRNSS HLLPAEAVHR SRAAYGVHGR
YRRSSQLRRP STVSNSARLV PAPSRRSSIV ARHSSRSLYR NCSACWKPRG RRESLSPLQG
IYYDPRLETW SGFVSKAIAK SGLQHLSAQP SASALAKFDP DREIRSSCDW TENALYGEHI
WFETNVSGDF CYVGEQHCFA KTLQKSVARK KCAACKIVVH TICIEQLEKI NFRCKPSFRE
SGSRNIREPT VVRHHWVHRR RQDGKCRQCG KGFQQKFAFH SKEIVAISCS WCKQAYHNKV
SCFMLQQIEE SCSLGAHASV IVPPTWILRV RRPQTSLKSS KKKKRTSFKR KSSKKGAEEA
RWKPFIVRPI PSQLMRPLLV FVNPKSGGNQ GAKIIQSFMW YLNPRQVFDL SLGGPKDGLE
MYRKVHNLRI LACGGDGTVG WILSALDQLQ LNPQPAVAIL PLGTGNDLAR TLNWGGGYTD
EPVSKLLSHV EDGNVVQLDR WNLTVEPNQD AGADEKDEHQ TDKLPLDIFN NYFSLGFDAH
VTLEFHESRE ANPEKFNSRF RNKMFYAGTA FSDFLMGSSK DLAKHIKVVC DGTDLTSKVQ
DLKLQCLVFL NIPRYCAGTM PWGNPSEHHD FEPQRHDDGC IEVIGFTMTS LATLQVGGHG
ERLNQCREVT LTTYKSIPMQ VDGEPCKLAP STIRISLRNQ ANMVQKTKRR TSIPLLNDQQ
PFPERLRIRV NRISMHDYEA LHYDKEKLKE ASIPLGLIVV PGDSDLETCR SHIERLQEED
EGAKPKTLSS QKLSPKWCFL DSTTADRFYR IDRAQEHLNY VTEISQDELF ILDPELVITE
TVSTSPGMPD LVDSSGELPE ASSKFAFPSS SSSPPPSPGP SPTSPQSDSE AMAVRHKKSH
FFSPSGFPFP VRKRITELQK TTQRKRTSSD SSVVEALAHS GSLRSSKPAL TRAGCIHRSN
TTAADFNPTL RSEKNTLCNT DKVSPEVLIE CVKRKDHLKL KELHKLGADL SVQDPPGCTL
LHYAVDTGSK ETVKYILDNA PTDILDVTEK ENGETVLHKA ASLCQRTICH YLVEAGASLM
KTDLQGDTPK HRAEKAKDAE LAAYLENRQH YQMIQREDQE TAV
//
