ID F1RW19_PIG Unreviewed; 1265 AA.
AC F1RW19;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 4.
DT 27-MAR-2024, entry version 82.
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:ENSSSCP00000013098.4,
GN ECO:0000313|VGNC:VGNC:87275};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000013098.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000013098.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000013098.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000013098.4}
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 AlphaFoldDB; F1RW19; -.
DR STRING; 9823.ENSSSCP00000013098; -.
DR PaxDb; 9823-ENSSSCP00000013098; -.
DR Ensembl; ENSSSCT00000013458.5; ENSSSCP00000013098.4; ENSSSCG00000012308.5.
DR VGNC; VGNC:87275; DGKK.
DR eggNOG; KOG1170; Eukaryota.
DR GeneTree; ENSGT00940000162262; -.
DR HOGENOM; CLU_001799_3_0_1; -.
DR InParanoid; F1RW19; -.
DR OrthoDB; 4642163at2759; -.
DR TreeFam; TF313104; -.
DR Reactome; R-SSC-114508; Effects of PIP2 hydrolysis.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000008227; Chromosome X.
DR Bgee; ENSSSCG00000012308; Expressed in oocyte and 8 other cell types or tissues.
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: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 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:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 213..306
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 324..374
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 395..446
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 484..619
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..71
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1265 AA; 141197 MW; D44E97834BB149A2 CRC64;
MDRGAAAAQG TAPPQDGEQP AESPEPPPPW PPPQPPPPPP ARVPPLLHAP SPEPAPQFCP
EPAPEPGPEA TPEPATELDT EPIPEPETEP ALEPTPEPAP ELDVESISEP ATEPAPEPAP
EPAPEPVPEP APEPAPDPAP EPIPVPAVEP APGPAPEPAT EPATKFCPEP AQVSRPEPSP
APRLLQCPVV APERGLKTSP SPRTPVLLSS IKKILKEGPL LKNCNSFKRW KLRYFLVRGQ
RLCFAHHPAF ARFETIDLSQ VALAESSCRN LCHSFCVITP QRKVTLAAPN RKDMEEWINV
IKTVQQGEIR KIPAAENNPF LVGMHYWYSS HSSRTQHCNV CRGSIPAFSR NVIICEVCKV
KSHRLCALRA SKDCKWNTLS ITDDLLMPAD EVTMPHQWVE GNISASSQCA VCHENCGSYQ
RLQDFRCLWC NSTVHDDCRR RFSKECWFGS HRSSVIPPTA LSDPKGDGQL VVSSDFWNLD
WSSACSCPLL IFINSKSGDH QGIVFLRKFK QYLNPSQVFD LSKGGPEAGL CMFKNFARFR
IVVCGGDGSV SWVLSLIDAF ELNERCQLAV IPLGTGNDLA RVLGWGAFWN RNKSPLNILN
RVEQASVRIL DRWSVMIRET PRQTPLLRGQ VEMDVPRFEA AAIQHLESAT TELNKILKAK
YPTEMIIATR FLCSAVEDFV VDIVKAWSRI KQNNTAIESV ILKSDLMYDK LSVLIDILAE
DAAVEKSSTA YADSATADGK PFVPQIDHIA KCKMELATKA QNLQKSLKLI IFQVEQVLDE
QSRQTISVKN FSSTFFLEDD SEDINQMSPR HRSRLGTLSS ISSLKSEDLE NLNLEHLYFT
PEMIRFKERC VMNNYFGIGL DAKISLEFNT RRDEHPGQYN SRLKNKMWYG LLGSKELFQR
SYRKLEERVH LECDGEAISL PNLQGIVVLN ITSYAGGVNF WGSSTATTEY EAPAIDDGKL
EVVAIFGSVQ MAMSRIINLH HHRIAQCREV MITIDGEEGI PVQVDGEAWV QRPGLIKIRY
KNAAQMLTRD RDLENSMKMW ECKHSEIQAA SQPQLDSQES QDSLSDEEYA QMQRLVQLAE
NLISRLTDLS KVHQHVPVLM DSVNASANIL NNIFYSQDST NEAGAASCTP IETLTRNDAV
DVTLSLKGLY DDTKAFLDEN LLRNAEYEAT LQTSLDAMSK EFEKLSKIDW MNSILIPEEK
SSDTDSRSLR LKVKFPKLGK KKPEEEDRPK SGQGIQGFIG NLWHRRHRRD EAKDDDLPTS
SESQL
//
