DGKZ_RAT
ID DGKZ_RAT Reviewed; 929 AA.
AC O08560;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Diacylglycerol kinase zeta {ECO:0000303|PubMed:15157668};
DE Short=DAG kinase zeta;
DE EC=2.7.1.107 {ECO:0000250|UniProtKB:Q13574};
DE AltName: Full=104 kDa diacylglycerol kinase;
DE AltName: Full=DGK-IV;
DE AltName: Full=Diglyceride kinase zeta;
DE Short=DGK-zeta;
GN Name=Dgkz {ECO:0000312|RGD:70929}; Synonyms=Dagk6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=Wistar;
RX PubMed=8855332; DOI=10.1073/pnas.93.20.11196;
RA Goto K., Kondo H.;
RT "A 104-kDa diacylglycerol kinase containing ankyrin-like repeats localizes
RT in the cell nucleus.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:11196-11201(1996).
RN [2]
RP INTERACTION WITH PIP5K1A.
RX PubMed=15157668; DOI=10.1016/j.cellsig.2004.01.010;
RA Luo B., Prescott S.M., Topham M.K.;
RT "Diacylglycerol kinase zeta regulates phosphatidylinositol 4-phosphate 5-
RT kinase Ialpha by a novel mechanism.";
RL Cell. Signal. 16:891-897(2004).
CC -!- FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into
CC phosphatidic acid/phosphatidate/PA and regulates the respective levels
CC of these two bioactive lipids. Thereby, acts as a central switch
CC between the signaling pathways activated by these second messengers
CC with different cellular targets and opposite effects in numerous
CC biological processes. Also plays an important role in the biosynthesis
CC of complex lipids. Does not exhibit an acyl chain-dependent substrate
CC specificity among diacylglycerol species. Can also phosphorylate 1-
CC alkyl-2-acylglycerol in vitro but less efficiently and with a
CC preference for alkylacylglycerols containing an arachidonoyl group (By
CC similarity). The biological processes it is involved in include T cell
CC activation since it negatively regulates T-cell receptor signaling
CC which is in part mediated by diacylglycerol (By similarity). By
CC generating phosphatidic acid, stimulates PIP5KIA activity which
CC regulates actin polymerization (By similarity). Through the same
CC mechanism could also positively regulate insulin-induced translocation
CC of SLC2A4 to the cell membrane (By similarity). Regulates RASGRP1
CC activity (By similarity). {ECO:0000250|UniProtKB:Q13574,
CC ECO:0000250|UniProtKB:Q80UP3}.
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:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43428, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18155, ChEBI:CHEBI:30616, ChEBI:CHEBI:78227,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-ditetradecanoyl-sn-glycerol + ATP = 1,2-ditetradecanoyl-
CC sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43444,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:80651,
CC ChEBI:CHEBI:83550, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43445;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:43416, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:64839, ChEBI:CHEBI:75466, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43417;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + ATP = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40335, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:72864, ChEBI:CHEBI:77096,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40336;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-
CC octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:43424, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:75468, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43425;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycerol + ATP = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40359, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77129, ChEBI:CHEBI:77130, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40360;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
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:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycerol + ATP = 1-(9Z)-
CC octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:43420, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:74551, ChEBI:CHEBI:75447, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43421;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-eicosanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycerol +
CC ATP = 1-eicosanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:40331, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77093, ChEBI:CHEBI:77094,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40332;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycerol + ATP =
CC 1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + ADP
CC + H(+); Xref=Rhea:RHEA:40351, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77125, ChEBI:CHEBI:77126, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40352;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-2-acyl-sn-glycerol + ATP = 1-O-alkyl-2-acyl-sn-
CC glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:44072,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52595,
CC ChEBI:CHEBI:73332, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + ATP = 1-O-hexadecyl-2-
CC acetyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41676,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75936,
CC ChEBI:CHEBI:78385, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol +
CC ATP = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:40403, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77184, ChEBI:CHEBI:77186,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40404;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-O-
CC hexadecyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40407, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77185, ChEBI:CHEBI:77187, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40408;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycerol + ATP = 1-O-hexadecyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:41672, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:34115, ChEBI:CHEBI:77580,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673;
CC Evidence={ECO:0000250|UniProtKB:Q13574};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000250|UniProtKB:Q13574}.
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with the PDZ domain of the
CC syntrophin SNTG1 and that of SNX27 (By similarity). Interacts with IRS1
CC in the absence of insulin; insulin stimulation decreases this
CC interaction (By similarity). Found in a ternary complex with IRS1 and
CC PIP5K1A in the absence of insulin (By similarity). Interacts with
CC PIP5K1A (PubMed:15157668). Forms a signaling complex with RASGRP1 and
CC HRAS (By similarity). {ECO:0000250|UniProtKB:Q13574,
CC ECO:0000250|UniProtKB:Q80UP3, ECO:0000269|PubMed:15157668}.
CC -!- INTERACTION:
CC O08560; Q62696: Dlg1; NbExp=4; IntAct=EBI-8570505, EBI-389325;
CC O08560; Q63622: Dlg2; NbExp=4; IntAct=EBI-8570505, EBI-396947;
CC O08560; Q62936: Dlg3; NbExp=4; IntAct=EBI-8570505, EBI-349596;
CC O08560; P31016: Dlg4; NbExp=6; IntAct=EBI-8570505, EBI-375655;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8855332}. Cytoplasm,
CC cytosol {ECO:0000250|UniProtKB:Q13574}. Cell membrane
CC {ECO:0000250|UniProtKB:Q13574}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q13574}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with PDZ domain-
CC containing proteins like SNTG1 and SNX27.
CC {ECO:0000250|UniProtKB:Q13574}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; D78588; BAA18942.1; -; mRNA.
DR PIR; JC6124; JC6124.
DR RefSeq; NP_112405.1; NM_031143.1.
DR AlphaFoldDB; O08560; -.
DR SMR; O08560; -.
DR BioGRID; 249679; 4.
DR IntAct; O08560; 6.
DR MINT; O08560; -.
DR STRING; 10116.ENSRNOP00000024280; -.
DR iPTMnet; O08560; -.
DR PhosphoSitePlus; O08560; -.
DR PaxDb; O08560; -.
DR PRIDE; O08560; -.
DR Ensembl; ENSRNOT00000024280; ENSRNOP00000024280; ENSRNOG00000017737.
DR GeneID; 81821; -.
DR KEGG; rno:81821; -.
DR UCSC; RGD:70929; rat.
DR CTD; 8525; -.
DR RGD; 70929; Dgkz.
DR eggNOG; KOG0782; Eukaryota.
DR GeneTree; ENSGT00940000156152; -.
DR InParanoid; O08560; -.
DR OMA; GEPCKLT; -.
DR OrthoDB; 274339at2759; -.
DR BRENDA; 2.7.1.107; 5301.
DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR UniPathway; UPA00230; -.
DR PRO; PR:O08560; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000017737; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; O08560; baseline and differential.
DR Genevisible; O08560; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:RGD.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0046486; P:glycerolipid metabolic process; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; ISS:UniProtKB.
DR GO; GO:0099562; P:maintenance of postsynaptic density structure; ISO:RGD.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0090216; P:positive regulation of 1-phosphatidylinositol-4-phosphate 5-kinase activity; ISS:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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 InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; PTHR11255; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50146; DAGK; 1.
PE 1: Evidence at protein level;
KW ANK repeat; ATP-binding; Cell membrane; Cell projection; Cytoplasm; Kinase;
KW Lipid metabolism; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..929
FT /note="Diacylglycerol kinase zeta"
FT /id="PRO_0000218470"
FT DOMAIN 292..426
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT REPEAT 823..853
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 858..887
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT ZN_FING 98..153
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 173..231
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..417
FT /note="Mediates interaction with RASGRP1"
FT /evidence="ECO:0000250|UniProtKB:Q13574"
FT REGION 421..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 362..370
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q80UP3"
FT MOTIF 925..929
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q13574"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13574"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13574"
SQ SEQUENCE 929 AA; 104009 MW; 6279872004F5F38D CRC64;
MEPRDPSPEA RSSDSESASA SSSGSERDAD PEPDKAPRRL TKRRFPGLRL FGHRKAITKS
GLQHLAPPPP TPGAPCGESE RQIRSTVDWS ESAAYGEHIW FETNVSGDFC YVGEQYCVAK
MLPKSAPRRK CAACKIVVHT PCIGQLEKIN FRCKPSFRES GSRNVREPTF VRHHWVHRRR
QDGKCRHCGK GFQQKFTFHS KEIVAISCSW CKQAYHSKVS CFMLQQIEEP CSLGVHAAVV
IPPTWILRAR RPQNTLKASK KKKRASFKRR SSKKGPEEGR WRPFIIRPTP SPLMKPLLVF
VNPKSGGNQG AKIIQSFLWY LNPRQVFDLS QGGPREALEM YRKVHNLRIL ACGGDGTVGW
ILSTLDQLRL KPPPPVAILP LGTGNDLART LNWGGGYTDE PVSKILSHVE EGNVVQLDRW
DLRAEPNPEA GPEERDDGAT DRLPLDVFNN YFSLGFDAHV TLEFHESREA NPEKFNSRFR
NKMFYAGTAF SDFLMGSSKD LAKHIRVVCD GMDLTPKIQD LKPQCIVFLN IPRYCAGTMP
WGHPGEHHDF EPQRHDDGYL EVIGFTMTSL AALQVGGHGE RLTQCREVLL TTAKAIPVQV
DGEPCKLAAS RIRIALRNQA TMVQKAKRRS TAPLHSDQQP VPEQLRIQVS RVSMHDYEAL
HYDKEQLKEA SVPLGTVVVP GDSDLELCRA HIERLQQEPD GAGAKSPMCH PLSSKWCFLD
ATTASRFYRI DRAQEHLNYV TEIAQDEIYI LDPELLGASA RPDLPTPTSP LPASPCSPTP
GSLQGDAALP QGEELIEAAK RNDFCKLQEL HRAGGDLMHR DHQSRTLLHH AVSTGSKEVV
RYLLDHAPPE ILDAVEENGE TCLHQAAALG QRTICHYIVE AGASLMKTDQ QGDTPRQRAE
KAQDTELAAY LENRQHYQMI QREDQETAV
