ID A0A2Y9SA68_PHYMC Unreviewed; 1234 AA.
AC A0A2Y9SA68;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-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=DGKK {ECO:0000313|RefSeq:XP_023972689.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023972689.1};
RN [1] {ECO:0000313|RefSeq:XP_023972689.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023972689.1};
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=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_023972689.1; XM_024116921.1.
DR AlphaFoldDB; A0A2Y9SA68; -.
DR STRING; 9755.ENSPCTP00005031238; -.
DR KEGG; pcad:102994216; -.
DR InParanoid; A0A2Y9SA68; -.
DR OrthoDB; 4642163at2759; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000248484; Chromosome 21.
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; cd20800; C1_DGK_typeII_rpt1; 1.
DR CDD; cd20852; C1_DGK_typeII_rpt2; 1.
DR CDD; cd13274; PH_DGK_type2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF33; DIACYLGLYCEROL KINASE KAPPA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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 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:UP000248484};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 182..275
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 293..343
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 364..415
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 453..588
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1234 AA; 137746 MW; 7B50E26EB78F860B CRC64;
MDRGAAAAQG TAPPQVGEQP VESPEPPPPW PPPKPPPPPP SPPARAPQLL HAPSPEPTPQ
FCPEPAPEPG PEATPEPAPE LDTEAISEPA TEPAPEPAPE PAPDPAPEPI PVPAVEPAPQ
PGPEPAPEPA TESCPEPAQV SRPEPSPAPH LLQCPVVAPE KGLRTSPSPR TLVPVPLSNI
KKILKEGPLL KNCNSFKRWK LRYFLVRGQR LCFAHHPAFA RFETIDLSQV ALAESSCRNL
CHSFCVITPQ RKVTLAAPNR KDMEEWINVI KTVQQGEIRK IPAAENNPFL VGMHYWYSSH
SPRTQHCNVC RGTIPALSRN VIICEVCKVK SHRLCALRAS KDCKWNTLSI TDDLLMPADE
KTMPHQWVEG NISVSSQCAV CHENCGSYQR LQDFRCLWCN STVHDDCRRR FSKECWFGSH
RSSVIPPTAL SDPKGDGQLV VSPDFWNLDW SSACSCPLLI FINSKSGDHQ GIVFLRKFKQ
YLNPSQVFDL SKGGPEAGLC MFKNFARFRI VVCGGDGSVS WVLSMIDAFG LQKRCQLAVI
PLGTGNDLAR VLGWGAFWNK NKSPLNILNR VEQADVRILD RWSVMIRETP RQTPLLRGQV
EMDVPRFEAA AIQHLESATT ELNKILKAKY PTEMIIATRF LCSAVEDFVV DIVKAWSRIK
QNNTAIESVI LKSDLMYDKL SVLIDVLAED ATVEKSTTAH ADSAKADGKP VIPQIDHIAK
CKLELATKAQ NLQKSLKLII FQVEQVLDEQ SRQTISVKNF SSTFFLEDDS EDINQMSPRH
RSRLGTLSSI SSLKSEDLDN LSLEHLYFTP ETIRFKERCV MNNYFGIGLD AKISLEFNTR
RDEHPGQYNS RLKNKMWYGL LGSKELFQRS YRKLEERVHL ECDGEAISLP NLQGIVVLNI
TSYAGGVNFW GSSTATTEYE APAIDDGKLE VVAIFGSVQM AMSRIINLHH HRIAQCCEVM
ITIDGEEGIP VQVDGEAWVQ RPGLIKIRYK NTAQMLTRDR DFENSMKTWE CKHSEIQAAS
QPQLDSQESQ DSLSDEEYAQ MQHLAQLAEN LISRLTDLSK VHQHVSVLMD SVNASANILN
DIFYNQDSSN EAGAASCTPI ETLTRNDAVD VTFSLKGLYD DTKAFLDENL LRNAEYEATL
QTSLDAMNKE FEKLSEIDWM NSILFPEEKS SDTDSRSLRL KVKFPKLGKK KPEEEDKPKS
GQGIQGFIGH LWHRRHREDE GKDDDPPTPS GSQL
//
