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Database: UniProt
Entry: A0A1S3STL0_SALSA
LinkDB: A0A1S3STL0_SALSA
Original site: A0A1S3STL0_SALSA 
ID   A0A1S3STL0_SALSA        Unreviewed;       921 AA.
AC   A0A1S3STL0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=LOC106611706 {ECO:0000313|RefSeq:XP_014067671.1};
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_014067671.1};
RN   [1] {ECO:0000313|RefSeq:XP_014067671.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014067671.1};
RG   RefSeq;
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_014067671.1; XM_014212196.1.
DR   AlphaFoldDB; A0A1S3STL0; -.
DR   OrthoDB; 4642163at2759; -.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000087266; Chromosome ssa09.
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   CDD; cd20854; C1_DGKtheta_typeV_rpt3; 1.
DR   CDD; cd17111; RA1_DAGK-theta; 1.
DR   CDD; cd01783; RA2_DAGK-theta; 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; IPR020454; DAG/PE-bd.
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   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR   PANTHER; PTHR11255:SF34; 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   PRINTS; PR00008; DAGPEDOMAIN.
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   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU361128};
KW   Kinase {ECO:0000256|RuleBase:RU361128, ECO:0000313|RefSeq:XP_014067671.1};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU361128};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          44..92
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          105..152
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          167..218
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          373..433
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          563..700
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..921
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   921 AA;  102412 MW;  AD566F6D4077DA22 CRC64;
     MANSTRTKNE NSIMESPSAS PLSGRKKAQQ SPGSRSRYHV SAPGHCFRKV TLTKPTFCHN
     CSDFIWGLIG FICEVCNFMC HEKCLKTVRT ACSCMAPTLV RVPVAHCFGP AGQKKRFCCV
     CRKHLEGNTA IRCEVCELHA HSECAAFSCG DCRLCHQDGS QDFDTLHHHW REGNIPSGAR
     CEVCRRTCGS SDVLAGMRCE WCGMTTHAAC YVIVPPECGL GRLRSMLLHP ACVRICSRNF
     SKMHCYRISE SCQNELDNLD EVDTQIPATT KESQPATTAD SGKQVLKVFD GDDAVKRSHF
     RLVSIPRITK NEEESALRTF YIPDDSLDYE LQDNGQQALH SNDILNRNGT PDEKAIFKEN
     VPEVWLLRAK PQDTEVLKVY AGWLKVGVAY ISISISKNST VDSVIKEVLT QLGRQDEDPS
     SFSLVEVYMG SKQVQRQGLT GQELLLYKLQ EIRKISLRQM NQTRFYIVES RKQVVQVNLL
     LEGLPVQLSK EEYTDLLQEH LAIKSHLVTI THVYGSQVGA VVVQISCFSE AERIYMLAKD
     TSVSNQQLTS LVIPEIMHNK LPKGGSPLLV FVNPKSGVLK GQELLYGFRK LLNPHQVFDM
     TNGGPLPGLH TFREVPRFRV LVCGGDGTVG WVLGVLEAVR HKLVCPEPPI GIVPLGTGND
     LARILRWGAG YSGEDPHHIL VSVDEAEEVQ MDRWTILLDA QEVTEDGKEN GFLEPPKIVQ
     MNNYFGLGID AELSLDFHHA REEEPGKFNS RFHNKGVYLK AGLQKLSHTR NLHKDLKLQV
     DKQDVELPSI EGLIFLNIPS WGSGADLWGS EGDSRYGKPR IDDGMLEVVG VTGVVHMGQV
     QGGMRSGIRL AQGNYVRITV TKPIPVQVDG EPWIQAPGNI IISAAGPKVR MLRKSKHKQK
     KQPASLKERR SESPSSSDGG H
//
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