ID A0A2I3SL15_PANTR Unreviewed; 1283 AA.
AC A0A2I3SL15; A0A2J8JH28;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
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=DGKK {ECO:0000313|Ensembl:ENSPTRP00000077739.1};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000077739.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000077739.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000077739.1}
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=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 EMBL; AACZ04051935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC205432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016799683.1; XM_016944194.1.
DR STRING; 9598.ENSPTRP00000077739; -.
DR Ensembl; ENSPTRT00000079526.1; ENSPTRP00000077739.1; ENSPTRG00000048026.1.
DR GeneID; 473607; -.
DR KEGG; ptr:473607; -.
DR CTD; 139189; -.
DR GeneTree; ENSGT00940000162262; -.
DR InParanoid; A0A2I3SL15; -.
DR OrthoDB; 4642163at2759; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000002277; Chromosome X.
DR Bgee; ENSPTRG00000048026; Expressed in pituitary gland.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IBA:GO_Central.
DR GO; GO:0030168; P:platelet activation; IEA:UniProt.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
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 PRINTS; PR01217; PRICHEXTENSN.
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; 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:UP000002277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 228..321
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 339..389
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 410..461
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 499..634
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1283 AA; 142917 MW; 8FD319E0CF36656F CRC64;
MDRGAAAAQG TAPPQDGEQP AESPEPPPPW PPPPPPPAPP PAPPPAPPPA PPLLSEASPE
PIPEPCPELA PGPCPEATSE SATELYTEPT PEPAPEPATE PAPEPATEPA PEPATEPAPE
PAPEPATESA PEPTPEPALE SVPEPVPEPA PELTPEVAPE LAPEPTPEPV TELAPEFCPE
AAPEFRPSPA PCLLQCPVDT RERGLKTSPS PSPSPSPRTP MSWSRIKKIL KEGPMLKNCN
SFKRWKLRYF LVQGQKLYFA HHPAFAHFET IDLSQATVAE SSCRNLCHSF CVITPQRKIT
LAAPNRKDME EWINIIKTIQ QGEIYKIPAA ENNPFLVGMH CWYSSYSHRT QHCNVCRESI
PALSRDAIIC EVCKVKSHRL CALRASKDCK WNTLSITDDL LLPADEVNMP HQWVEGNMPV
SSQCAVCHES CGSYQRLQDF RCLWCNSTVH DDCRRRFSKE CCFGSHRSSV IPPTALSDPK
GDGQLVVSSD FWNLDWSSAC SCPLLIFINS KSGDHQGIVF LRKFKQYLNP SQVFDLLKGG
PEAGLSMFKN FARFRILVCG GDGSVSWVLS LIDAFGLHEK CQLAVIPLGT GNDLARVLGW
GAFWNKSKSP LDILNRVEQA SVRILDRWSV MIRETPRQTP LLKGQVEMDV PRFEAAAIQH
LESAATELNK ILKAKYPTEM IIATRFLCSA VEDFVVDIVK AWGQIKQNNT AIVSVILKSD
LMYDRLSVLI DVLAEEAAAT SAEKSATEYA DSSKADRKPF VPQIDHIAKC KLELATKAQS
LQKSLKLIIF QVEQALDEES RQTISVKNFS STFFLEDDPE DINQTSPRRR SRRGTLSSIS
SLKSEDLDNL NLDHLHFTPE SIRFKEKCVM NNYFGIGLDA KISLDFNTRR DEHPGQYNSR
LKNKMWYGLL GTKELLQRSY RKLEERVHLE CDGETISLPN LQGIVVLNIT SYAGGINFWG
SNTATTEYEA PAIDDGKLEV VAIFGSVQMA MSRIINLHHH RIAQCHEVMI TIDGEEGIPV
QVDGEAWIQR PGLIKIRYKN AAQMLTRDRD FENSMKMWEY KHTEIQAAPQ PQLDFQDSQE
SLSDEEYAQM QHLARLAENL ISKLNDLSKI HQHVSVLMGS VNASANILND IFYSQDSGNE
MGAASCIPIE TLSRNDAVDV TFSLKGLYDD TTAFLDEKLL RSAEDETALQ SALDAMNKEF
KKLSEIDWMN PIFVPEEKSS DTDSRSLRLK IKFPKLGKKK LEEERKPKSG QSVQSFIGNL
WHRRHREDEA EGDDPLTPSR SQL
//
