位置:首页 > 蛋白库 > DGK5_ARATH
DGK5_ARATH
ID   DGK5_ARATH              Reviewed;         509 AA.
AC   Q9C5E5; Q8LE70; Q9SKS9;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Diacylglycerol kinase 5;
DE            Short=AtDGK5;
DE            Short=DAG kinase 5;
DE            EC=2.7.1.107;
DE   AltName: Full=Diglyceride kinase 5;
DE            Short=DGK 5;
GN   Name=DGK5; OrderedLocusNames=At2g20900; ORFNames=F5H14.13;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9C5E5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9C5E5-2; Sequence=VSP_046410, VSP_046411;
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {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; AC006234; AAD20931.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07093.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07094.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07095.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07096.1; -; Genomic_DNA.
DR   EMBL; AF360300; AAK26010.1; -; mRNA.
DR   EMBL; BT000983; AAN41383.1; -; mRNA.
DR   EMBL; AK316877; BAH19585.1; -; mRNA.
DR   EMBL; AK317470; BAH20135.1; -; mRNA.
DR   EMBL; AY085589; AAM62810.1; -; mRNA.
DR   PIR; G84594; G84594.
DR   RefSeq; NP_001031381.1; NM_001036304.1. [Q9C5E5-1]
DR   RefSeq; NP_565492.1; NM_127660.4. [Q9C5E5-2]
DR   RefSeq; NP_850007.1; NM_179676.3. [Q9C5E5-1]
DR   RefSeq; NP_973498.1; NM_201769.3. [Q9C5E5-2]
DR   AlphaFoldDB; Q9C5E5; -.
DR   BioGRID; 1977; 1.
DR   IntAct; Q9C5E5; 1.
DR   STRING; 3702.AT2G20900.1; -.
DR   iPTMnet; Q9C5E5; -.
DR   PaxDb; Q9C5E5; -.
DR   PRIDE; Q9C5E5; -.
DR   ProteomicsDB; 224215; -. [Q9C5E5-1]
DR   DNASU; 816624; -.
DR   EnsemblPlants; AT2G20900.1; AT2G20900.1; AT2G20900. [Q9C5E5-1]
DR   EnsemblPlants; AT2G20900.2; AT2G20900.2; AT2G20900. [Q9C5E5-2]
DR   EnsemblPlants; AT2G20900.3; AT2G20900.3; AT2G20900. [Q9C5E5-2]
DR   EnsemblPlants; AT2G20900.4; AT2G20900.4; AT2G20900. [Q9C5E5-1]
DR   GeneID; 816624; -.
DR   Gramene; AT2G20900.1; AT2G20900.1; AT2G20900. [Q9C5E5-1]
DR   Gramene; AT2G20900.2; AT2G20900.2; AT2G20900. [Q9C5E5-2]
DR   Gramene; AT2G20900.3; AT2G20900.3; AT2G20900. [Q9C5E5-2]
DR   Gramene; AT2G20900.4; AT2G20900.4; AT2G20900. [Q9C5E5-1]
DR   KEGG; ath:AT2G20900; -.
DR   Araport; AT2G20900; -.
DR   TAIR; locus:2051343; AT2G20900.
DR   eggNOG; KOG1169; Eukaryota.
DR   InParanoid; Q9C5E5; -.
DR   OMA; DSWHIML; -.
DR   OrthoDB; 633642at2759; -.
DR   PhylomeDB; Q9C5E5; -.
DR   BioCyc; ARA:AT2G20900-MON; -.
DR   PRO; PR:Q9C5E5; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9C5E5; baseline and differential.
DR   Genevisible; Q9C5E5; AT.
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; IPR016961; Diacylglycerol_kinase_pln.
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   PIRSF; PIRSF030829; Diacylglycerol_kinase_pln; 1.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Plant defense; Reference proteome; Stress response; Transferase.
FT   CHAIN           1..509
FT                   /note="Diacylglycerol kinase 5"
FT                   /id="PRO_0000422113"
FT   DOMAIN          36..187
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   REGION          439..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         485..491
FT                   /note="GEHSNKK -> VDISQLS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640, ECO:0000303|Ref.5"
FT                   /id="VSP_046410"
FT   VAR_SEQ         492..509
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640, ECO:0000303|Ref.5"
FT                   /id="VSP_046411"
FT   CONFLICT        31
FT                   /note="E -> Q (in Ref. 5; AAM62810)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="F -> S (in Ref. 5; AAM62810)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102
FT                   /note="R -> G (in Ref. 5; AAM62810)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   509 AA;  57377 MW;  F6F9A08630D327DA CRC64;
     MEKYNSLSDF LKEFYIPTYV LSAETEEEEE EESRPTPASP VLVFINSKSG GQLGGELILT
     YRSLLNHNQV FDLDQETPDK VLRRIYLNLE RLKDDDFARQ IREKLKIIVA GGDGTAGWLL
     GVVCDLKLSH PPPIATVPLG TGNNLPFAFG WGKKNPGTDR TAVESFLEQV LKAKVMKIDN
     WHILMRMKTP KEGGSCDPVA PLELPHSLHA FHRVSPTDEL NKEGCHTFRG GFWNYFSLGM
     DAQISYAFHS ERKLHPEKFK NQLVNQSTYV KLGCTQGWFC ASLFHPASRN IAQLAKVKIA
     TRNGQWQDLH IPHSIRSIVC LNLPSFSGGL NPWGTPNPRK QRDRGLTPPF VDDGLIEVVG
     FRNAWHGLVL LAPNGHGTRL AQANRIRFEF HKGATDHTFM RMDGEPWKQP LPLDDETVMV
     EISHLGQVNM LATHDCRSRS VFDPSTPRHQ DGAEDYDDNE DDSVAEGEEF RKFGAADTFK
     IPDEGEHSNK KGRASRRRNS NVHGWSHVL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024