位置:首页 > 蛋白库 > DGK6_ARATH
DGK6_ARATH
ID   DGK6_ARATH              Reviewed;         466 AA.
AC   F4JKI3; Q9M0J4; Q9SUC8;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Diacylglycerol kinase 6;
DE            Short=AtDGK6;
DE            Short=DAG kinase 6;
DE            EC=2.7.1.107;
DE   AltName: Full=Diglyceride kinase 6;
DE            Short=DGK 6;
GN   Name=DGK6; OrderedLocusNames=At4g28130; ORFNames=F26K10.10, T13J8.230;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   FUNCTION.
RX   PubMed=23346092; DOI=10.3389/fpls.2013.00001;
RA   Arisz S.A., van Wijk R., Roels W., Zhu J.K., Haring M.A., Munnik T.;
RT   "Rapid phosphatidic acid accumulation in response to low temperature stress
RT   in Arabidopsis is generated through diacylglycerol kinase.";
RL   Front. Plant Sci. 4:1-1(2013).
CC   -!- FUNCTION: Phosphorylates the second messenger diacylglycerol (DAG) to
CC       generate phosphatidic acid (PA), another important signaling molecule.
CC       PA is required for plant development and responses to abiotic stress
CC       and pathogen attack. May be involved in the accumulation of PA during
CC       cold stress. {ECO:0000269|PubMed:23346092}.
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB36781.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79614.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79615.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL035524; CAB36781.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161572; CAB79614.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161572; CAB79615.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85443.1; -; Genomic_DNA.
DR   PIR; C85327; C85327.
DR   PIR; D85327; D85327.
DR   PIR; T02913; T02913.
DR   PIR; T09029; T09029.
DR   RefSeq; NP_194542.2; NM_118953.2.
DR   AlphaFoldDB; F4JKI3; -.
DR   STRING; 3702.AT4G28130.1; -.
DR   PaxDb; F4JKI3; -.
DR   PRIDE; F4JKI3; -.
DR   ProteomicsDB; 224216; -.
DR   EnsemblPlants; AT4G28130.1; AT4G28130.1; AT4G28130.
DR   GeneID; 828928; -.
DR   Gramene; AT4G28130.1; AT4G28130.1; AT4G28130.
DR   KEGG; ath:AT4G28130; -.
DR   Araport; AT4G28130; -.
DR   TAIR; locus:2123703; AT4G28130.
DR   eggNOG; KOG1169; Eukaryota.
DR   HOGENOM; CLU_002706_46_2_1; -.
DR   InParanoid; F4JKI3; -.
DR   OMA; INIDNWH; -.
DR   OrthoDB; 633642at2759; -.
DR   PRO; PR:F4JKI3; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JKI3; baseline and differential.
DR   Genevisible; F4JKI3; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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   Gene3D; 3.40.50.10330; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
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   PANTHER; PTHR11255; PTHR11255; 1.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Plant defense; Reference proteome;
KW   Stress response; Transferase.
FT   CHAIN           1..466
FT                   /note="Diacylglycerol kinase 6"
FT                   /id="PRO_0000422114"
FT   DOMAIN          43..194
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
SQ   SEQUENCE   466 AA;  52490 MW;  C94BA5687CFFF252 CRC64;
     MVQSETSMEK YKNLSDFLKK FFIPSYVLSP EDEPEAQISC TTAPENPILV FINSKSGGQL
     GAELILTYRT LLNDKQVFDL EVETPDKVLQ RIYLNLERLK DDSLASKIRD KLKIIVAGGD
     GTAGWLLGVV SDLNLSNPPP IATVPLGTGN NLPFAFGWGK KNPGTDRSSV ESFLGKVINA
     KEMKIDNWKI LMRMKHPKEG SCDITLKLPH SLPRIFPSDQ ENMEGYHTYR GGFWNYFSLG
     MDAQVSYAFH SQRKLHPERF KNQLVNQSTY LKLSCTQGWF FASLFHPSSQ NIAKLAKIQI
     CDRNGQWNDL HIPQSIRSIV CLNLPSFSGG LNPWGTPNPK KQRDRSLTAP FVDDGLIEIV
     GFRNAWHGLI LLSPNGHGTR LAQANRVRLE FKKGAAKHAY MRIDGEPWKQ PLPSNDETVM
     VEISHHGQVN MLATQNCRSK SMYESSSIIR FSNDEDDSSV VENEEF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024