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Database: UniProt
Entry: A0A286XC43_CAVPO
LinkDB: A0A286XC43_CAVPO
Original site: A0A286XC43_CAVPO 
ID   A0A286XC43_CAVPO        Unreviewed;       935 AA.
AC   A0A286XC43;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 9.
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=DGKQ {ECO:0000313|Ensembl:ENSCPOP00000022969};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Caviidae; Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000022969, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Ensembl:ENSCPOP00000022969, ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000022969,
RC   ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
RA   Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
RA   Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
RA   Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
RA   Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
RA   Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
RA   Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
RA   Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
RA   Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
RA   Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
RA   Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
RA   Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
RA   Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
RA   Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
RA   Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
RA   Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29
RT   mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000022969}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000022969};
RG   Ensembl;
RL   Submitted (OCT-2017) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-
CC         3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107;
CC         Evidence={ECO:0000256|RuleBase:RU361128};
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC       family. {ECO:0000256|RuleBase:RU361128}.
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DR   EMBL; AAKN02046979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_013002804.1; XM_013147350.1.
DR   Ensembl; ENSCPOT00000045246; ENSCPOP00000022969; ENSCPOG00000002313.
DR   GeneID; 100731359; -.
DR   CTD; 1609; -.
DR   GeneTree; ENSGT00940000159492; -.
DR   OrthoDB; 1275907at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   CDD; cd00029; C1; 2.
DR   Gene3D; 3.40.50.10330; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
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; PTHR11255; 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; SSF111331; SSF111331; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 3.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU361128};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005447};
KW   Kinase {ECO:0000256|RuleBase:RU361128};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00733152};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Transferase {ECO:0000256|RuleBase:RU361128};
KW   Zinc {ECO:0000256|SAAS:SAAS00732909};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS00732991}.
FT   DOMAIN       67    115       Phorbol-ester/DAG-type.
FT                                {ECO:0000259|PROSITE:PS50081}.
FT   DOMAIN      128    175       Phorbol-ester/DAG-type.
FT                                {ECO:0000259|PROSITE:PS50081}.
FT   DOMAIN      190    241       Phorbol-ester/DAG-type.
FT                                {ECO:0000259|PROSITE:PS50081}.
FT   DOMAIN      404    503       Ras-associating. {ECO:0000259|PROSITE:
FT                                PS50200}.
FT   DOMAIN      580    717       DAGKc. {ECO:0000259|PROSITE:PS50146}.
FT   REGION        1     67       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A286XC43}.
FT   REGION      279    305       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A286XC43}.
FT   REGION      358    393       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A286XC43}.
FT   REGION      913    935       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A286XC43}.
SQ   SEQUENCE   935 AA;  101063 MW;  3C1041C861422087 CRC64;
     MAAAAEPGTR AWLGDGSSRP GSPACSPVLG AGGRARLGAG RGSGSGSGPE QAPGRAGDTA
     SGPAVPSHSF RKVTLTKPTF CHLCSDFIWG LAGFLCDVCN FMSHEKCLRH VKTPCAGVAP
     SLVRVPVAHC FGPPGLYKRK FCAVCRKVLE TPAFRCEVCE LHIHADCVPF ACSDCRQCHQ
     DGHHDHDTYH HHWREGNLPL GGRCEICRKT CGSSDVLAGV RCEWCGVQAH SLCSAMLAPE
     CTFGRLRTMV LPPGCVRLLS RNFSKMHCFR IAETTAPELG DRDDGMDGSA ALGPGRDMPA
     APESSKQTLK IFDGNDTMKR NHFRLVTVPR LARSEEVLEA ALRAYYVSED AGNFELQEFP
     LPSPAADAQA PGKAGSGGSA EEDSSRGSGA REPEAWVIRA RPRTQEVLKI YPGWLKVGVA
     YVSIRVTSQS TAHSVVLEVL PLLGRQAEGP ESFHLVEVLM GSRQVQRMVL ADEESLLQRL
     RDIRQTSLRQ ASQTRFYVVE SRAVAPHISL FVSGLPPGLS PQEYGSLLHE AMATKGAVVL
     DVTCFAEAER LYMLARDTAV HGRPLTTLVL PDVLHTKLPP DCCPLLVFVN PRSGGLKGRD
     LLCSFRKLLN PHQVFDLTNG GPLPGFHLFS QVPCFRVLVC GGDGTVGWVL TALEETRHHL
     ACQEPSVAIL PLGTGNDLGR VLRWGAGYSG EDPFSMLVSV DEADAVLVDR WTILLDAHGA
     AGAENSVLDA EPPKIVQMSN YCGIGIDAEL SLDFHQAREE EPGKFTSRFH NKGVYVRVGL
     QKISHSRGLH KEIRLQVEQR EVELPSIEGL IFINIPSWGS GADLWGSDSD SRFEKPRMDD
     GLLEVVGVTG VMHMGQVQGG LRSGIRIAQG SYFRVTLLKA TPVQVDGEPW VQAPGHMIIS
     AAGPKVHMLR KAKQKPRKPA AIRGDAVPAP EGSAK
//
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