ID M4AX42_XIPMA Unreviewed; 727 AA.
AC M4AX42;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 59.
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=DGKB {ECO:0000313|Ensembl:ENSXMAP00000019037.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000019037.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000019037.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000019037.2};
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=1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43428, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18155, ChEBI:CHEBI:30616, ChEBI:CHEBI:78227,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023395};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000256|ARBA:ARBA00023395};
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; M4AX42; -.
DR Ensembl; ENSXMAT00000019065.2; ENSXMAP00000019037.2; ENSXMAG00000018947.2.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000159770; -.
DR HOGENOM; CLU_003770_1_0_1; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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:0005509; F:calcium ion binding; IEA:InterPro.
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; cd20845; C1_DGKbeta_rpt1; 1.
DR CDD; cd20891; C1_DGKbeta_rpt2; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 2.60.200.40; -; 2.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 1.10.238.110; Diacylglycerol kinase alpha; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR047471; C1_DGKbeta-like_rpt1.
DR InterPro; IPR047470; C1_DGKbeta_rpt2.
DR InterPro; IPR029477; DAG_kinase_typeI_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR038199; DGK_typeI_N_sf.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF32; DIACYLGLYCEROL KINASE BETA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF14513; DAG_kinase_N; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000002852};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 111..146
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 156..191
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 206..256
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 270..320
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 357..491
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 20..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 81741 MW; 3ADAD5F682F895CD CRC64;
MQTFLESELP EEFCQHLFMS FSNKGPRPSP SSADKPRVSG KCRKKPLSTS QGKQSVVNTA
DVENMKKKSK VAALPIKNNS TPLKTSAPPG PLDMVQLKDI VFYLSLLEGG RPEDKLEFMF
RLYDTDGNGS LDSSELEHII SQMMHVAEYL EWDVTELKPI LQEMMHEIDY DQDGTVSLGE
WIQGGLTTIP LLVLLGLETN VKDDGQHVWR LKHFNKPAYC NLCLNMLIGL GKQGLCCSFC
KYTVHERCVA RAPLSCIKTY VKSKKNTEVM HHFWVEGNCP TKCDKCHKTI KCYQGLTGLH
CVWCQITLHN KCASHVKPEC DCGPLKDHIL PPNSICPVVL VRLCLFWSAG LEITTIEGTH
PLLVFVNPKS GGKQGERIYR KFQYLLNPRQ VYNLAKNGPL SGLNFFRDVP DFRVLTCGGD
GTVGWILDFI DKANLDRNPP VCILPLGTGN DLARCLRWGG GYEGENLLKI LRDIENSTEV
MLDRWKIDVT SADKEERGDP VPYSIMNNYF SIGVDASIAH RFHVMREKHP EKFNSRTKNK
LWYFEFGTSE TFSATCKKLH DFLEVECDGV TLDLSSISLE GIAILNIPSM HGGSNLWGES
KKRRGQRKAG KKSQEKRTPV VDPKELMFAV QDLSDQLLEV VGLEGAMEMG QIYTGLKSAG
RRLAQCSSVT IRTTKSLPMQ IDGEPWMQTP CTIQIVHKNQ AHMLMGAPQG RSFFSSILRR
TRSESKD
//
