DGKZ_HUMAN
ID DGKZ_HUMAN Reviewed; 928 AA.
AC Q13574; B7Z2M9; B7Z6M3; E9PPW4; F6UCU9; G3V0F6; J3KNJ6; O00542; Q6ZVG7;
AC Q8IVW9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 4.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Diacylglycerol kinase zeta {ECO:0000303|PubMed:8626588};
DE Short=DAG kinase zeta;
DE EC=2.7.1.107 {ECO:0000269|PubMed:15544348, ECO:0000269|PubMed:18004883, ECO:0000269|PubMed:19744926, ECO:0000269|PubMed:22108654, ECO:0000269|PubMed:22627129, ECO:0000269|PubMed:8626588, ECO:0000269|PubMed:9159104};
DE AltName: Full=Diglyceride kinase zeta;
DE Short=DGK-zeta;
GN Name=DGKZ {ECO:0000312|HGNC:HGNC:2857}; Synonyms=DAGK6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, SUBSTRATE SPECIFICITY, AND TISSUE SPECIFICITY.
RC TISSUE=Endothelial cell;
RX PubMed=8626588; DOI=10.1074/jbc.271.17.10237;
RA Bunting M., Tang W., Zimmerman G.A., McIntyre T.M., Prescott S.M.;
RT "Molecular cloning and characterization of a novel human diacylglycerol
RT kinase zeta.";
RL J. Biol. Chem. 271:10230-10236(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX PubMed=9159104; DOI=10.1073/pnas.94.11.5519;
RA Ding L., Bunting M., Topham M.K., McIntyre T.M., Zimmerman G.A.,
RA Prescott S.M.;
RT "Alternative splicing of the human diacylglycerol kinase zeta gene in
RT muscle.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5519-5524(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 6), AND PARTIAL
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT LYS-523.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=9716136; DOI=10.1038/29337;
RA Topham M.K., Bunting M., Zimmerman G.A., McIntyre T.M., Blackshear P.J.,
RA Prescott S.M.;
RT "Protein kinase C regulates the nuclear localization of diacylglycerol
RT kinase-zeta.";
RL Nature 394:697-700(1998).
RN [9]
RP INTERACTION WITH SNTG1, MUTAGENESIS OF 926-THR-ALA-927, DOMAIN, AND MOTIF.
RX PubMed=11352924; DOI=10.1074/jbc.m104156200;
RA Hogan A., Shepherd L., Chabot J., Quenneville S., Prescott S.M.,
RA Topham M.K., Gee S.H.;
RT "Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta.
RT Regulation of nuclear localization by PDZ interactions.";
RL J. Biol. Chem. 276:26526-26533(2001).
RN [10]
RP FUNCTION AS A RASGRP1 REGULATOR (ISOFORMS 1 AND 2), IDENTIFICATION IN A
RP COMPLEX WITH RASGRP1 AND HRAS, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=11257115; DOI=10.1083/jcb.152.6.1135;
RA Topham M.K., Prescott S.M.;
RT "Diacylglycerol kinase zeta regulates Ras activation by a novel
RT mechanism.";
RL J. Cell Biol. 152:1135-1143(2001).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=15544348; DOI=10.1021/bi0484724;
RA Epand R.M., Kam A., Bridgelal N., Saiga A., Topham M.K.;
RT "The alpha isoform of diacylglycerol kinase exhibits arachidonoyl
RT specificity with alkylacylglycerol.";
RL Biochemistry 43:14778-14783(2004).
RN [12]
RP FUNCTION, INTERACTION WITH PIP5K1A, AND SUBCELLULAR LOCATION.
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).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18004883; DOI=10.1021/bi701584v;
RA Epand R.M., Shulga Y.V., Timmons H.C., Perri A.L., Belani J.D.,
RA Perinpanathan K., Johnson-McIntire L.B., Bajjalieh S., Dicu A.O., Elias C.,
RA Rychnovsky S.D., Topham M.K.;
RT "Substrate chirality and specificity of diacylglycerol kinases and the
RT multisubstrate lipid kinase.";
RL Biochemistry 46:14225-14231(2007).
RN [14]
RP INTERACTION WITH SNX27, DOMAIN, AND MOTIF.
RX PubMed=17351151; DOI=10.1074/mcp.m700047-mcp200;
RA Rincon E., Santos T., Avila-Flores A., Albar J.P., Lalioti V., Lei C.,
RA Hong W., Merida I.;
RT "Proteomics identification of sorting nexin 27 as a diacylglycerol kinase
RT zeta-associated protein: new diacylglycerol kinase roles in endocytic
RT recycling.";
RL Mol. Cell. Proteomics 6:1073-1087(2007).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RX PubMed=19744926; DOI=10.1074/jbc.m109.050617;
RA Lung M., Shulga Y.V., Ivanova P.T., Myers D.S., Milne S.B., Brown H.A.,
RA Topham M.K., Epand R.M.;
RT "Diacylglycerol kinase epsilon is selective for both acyl chains of
RT phosphatidic acid or diacylglycerol.";
RL J. Biol. Chem. 284:31062-31073(2009).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=22108654; DOI=10.1016/j.febslet.2011.11.016;
RA Shulga Y.V., Topham M.K., Epand R.M.;
RT "Substrate specificity of diacylglycerol kinase-epsilon and the
RT phosphatidylinositol cycle.";
RL FEBS Lett. 585:4025-4028(2011).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=22627129; DOI=10.1016/j.bbrc.2012.05.077;
RA Gellett A.M., Kharel Y., Sunkara M., Morris A.J., Lynch K.R.;
RT "Biosynthesis of alkyl lysophosphatidic acid by diacylglycerol kinases.";
RL Biochem. Biophys. Res. Commun. 422:758-763(2012).
RN [18]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23949095; DOI=10.1159/000351849;
RA Sato M., Liu K., Sasaki S., Kunii N., Sakai H., Mizuno H., Saga H.,
RA Sakane F.;
RT "Evaluations of the selectivities of the diacylglycerol kinase inhibitors
RT R59022 and R59949 among diacylglycerol kinase isozymes using a new non-
RT radioactive assay method.";
RL Pharmacology 92:99-107(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-705 AND SER-781, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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 (PubMed:9159104, PubMed:15544348,
CC PubMed:18004883, PubMed:19744926, PubMed:22108654, PubMed:22627129,
CC PubMed:23949095). Thereby, acts as a central switch between the
CC signaling pathways activated by these second messengers with different
CC cellular targets and opposite effects in numerous biological processes
CC (PubMed:9159104, PubMed:15544348, PubMed:18004883, PubMed:19744926,
CC PubMed:22108654, PubMed:22627129, PubMed:23949095). Also plays an
CC important role in the biosynthesis of complex lipids (Probable). Does
CC not exhibit an acyl chain-dependent substrate specificity among
CC diacylglycerol species (PubMed:9159104, PubMed:19744926,
CC PubMed:22108654). Can also phosphorylate 1-alkyl-2-acylglycerol in
CC vitro but less efficiently and with a preference for alkylacylglycerols
CC containing an arachidonoyl group (PubMed:15544348, PubMed:19744926,
CC PubMed:22627129). The biological processes it is involved in include T
CC cell 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 (PubMed:15157668). Through the same
CC mechanism could also positively regulate insulin-induced translocation
CC of SLC2A4 to the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q80UP3, ECO:0000269|PubMed:15157668,
CC ECO:0000269|PubMed:15544348, ECO:0000269|PubMed:18004883,
CC ECO:0000269|PubMed:19744926, ECO:0000269|PubMed:22108654,
CC ECO:0000269|PubMed:22627129, ECO:0000269|PubMed:23949095,
CC ECO:0000269|PubMed:9159104, ECO:0000305|PubMed:8626588}.
CC -!- FUNCTION: [Isoform 1]: Regulates RASGRP1 activity.
CC {ECO:0000269|PubMed:11257115}.
CC -!- FUNCTION: [Isoform 2]: Does not regulate RASGRP1 activity.
CC {ECO:0000269|PubMed:11257115}.
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:0000269|PubMed:15544348, ECO:0000269|PubMed:18004883,
CC ECO:0000269|PubMed:19744926, ECO:0000269|PubMed:22108654,
CC ECO:0000269|PubMed:22627129, ECO:0000269|PubMed:23949095,
CC ECO:0000269|PubMed:8626588, ECO:0000269|PubMed:9159104};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:15544348};
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:0000269|PubMed:8626588};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000305|PubMed:8626588};
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:0000269|PubMed:8626588, ECO:0000269|PubMed:9159104};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43445;
CC Evidence={ECO:0000305|PubMed:8626588};
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:0000269|PubMed:8626588, ECO:0000269|PubMed:9159104};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43417;
CC Evidence={ECO:0000305|PubMed:8626588};
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:0000269|PubMed:19744926};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40336;
CC Evidence={ECO:0000305|PubMed:19744926};
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:0000269|PubMed:8626588, ECO:0000269|PubMed:9159104};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43425;
CC Evidence={ECO:0000305|PubMed:8626588};
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:0000269|PubMed:15544348,
CC ECO:0000269|PubMed:18004883, ECO:0000269|PubMed:19744926,
CC ECO:0000269|PubMed:22108654, ECO:0000269|PubMed:8626588,
CC ECO:0000269|PubMed:9159104};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000305|PubMed:15544348};
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:0000269|PubMed:22108654};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40360;
CC Evidence={ECO:0000305|PubMed:22108654};
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:0000269|PubMed:15544348, ECO:0000269|PubMed:18004883,
CC ECO:0000269|PubMed:19744926, ECO:0000269|PubMed:22108654,
CC ECO:0000269|PubMed:22627129, ECO:0000269|PubMed:23949095,
CC ECO:0000269|PubMed:8626588, ECO:0000269|PubMed:9159104};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000305|PubMed:8626588};
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:0000269|PubMed:8626588, ECO:0000269|PubMed:9159104};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43421;
CC Evidence={ECO:0000305|PubMed:8626588};
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:0000269|PubMed:19744926};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40332;
CC Evidence={ECO:0000305|PubMed:19744926};
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:0000269|PubMed:22108654};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40352;
CC Evidence={ECO:0000305|PubMed:22108654};
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:0000269|PubMed:15544348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073;
CC Evidence={ECO:0000269|PubMed:15544348};
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:0000269|PubMed:22627129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677;
CC Evidence={ECO:0000305|PubMed:22627129};
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:0000269|PubMed:15544348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40404;
CC Evidence={ECO:0000305|PubMed:15544348};
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:0000269|PubMed:15544348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40408;
CC Evidence={ECO:0000305|PubMed:15544348};
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:0000269|PubMed:22627129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673;
CC Evidence={ECO:0000305|PubMed:22627129};
CC -!- ACTIVITY REGULATION: Activated by 1,2-diacyl-sn-glycero-3-
CC phosphate/phosphatidic acid irrespective of its acyl chain composition.
CC {ECO:0000269|PubMed:19744926}.
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:8626588}.
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with the PDZ domain of the
CC syntrophin SNTG1 and that of SNX27 (PubMed:11352924, PubMed:17351151).
CC Interacts with IRS1 in the absence of insulin; insulin stimulation
CC decreases this interaction (By similarity). Found in a ternary complex
CC with IRS1 and PIP5K1A in the absence of insulin (By similarity).
CC Interacts with PIP5K1A (PubMed:15157668).
CC {ECO:0000250|UniProtKB:Q80UP3, ECO:0000269|PubMed:11352924,
CC ECO:0000269|PubMed:15157668, ECO:0000269|PubMed:17351151}.
CC -!- SUBUNIT: [Isoform 1]: Forms a signaling complex with RASGRP1 and HRAS.
CC {ECO:0000269|PubMed:11257115}.
CC -!- INTERACTION:
CC Q13574-2; P06400: RB1; NbExp=6; IntAct=EBI-715527, EBI-491274;
CC Q13574-2; P28749: RBL1; NbExp=2; IntAct=EBI-715527, EBI-971402;
CC Q13574-2; Q08999: RBL2; NbExp=2; IntAct=EBI-715527, EBI-971439;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11257115,
CC ECO:0000269|PubMed:15157668, ECO:0000269|PubMed:9159104,
CC ECO:0000269|PubMed:9716136}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:11257115, ECO:0000269|PubMed:22627129}. Cell
CC membrane {ECO:0000269|PubMed:11257115}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:15157668}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=Short;
CC IsoId=Q13574-2; Sequence=Displayed;
CC Name=2; Synonyms=Long, zeta2;
CC IsoId=Q13574-1; Sequence=VSP_060599;
CC Name=3;
CC IsoId=Q13574-3; Sequence=VSP_060598;
CC Name=4;
CC IsoId=Q13574-4; Sequence=VSP_060601;
CC Name=5;
CC IsoId=Q13574-5; Sequence=VSP_060601, VSP_060603;
CC Name=6;
CC IsoId=Q13574-6; Sequence=VSP_060601, VSP_060602;
CC Name=7;
CC IsoId=Q13574-7; Sequence=VSP_060597, VSP_060600, VSP_060601;
CC -!- TISSUE SPECIFICITY: Highest levels in brain, and substantial levels in
CC skeletal muscle, heart, and pancreas. {ECO:0000269|PubMed:8626588}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Predominantly expressed in muscle.
CC {ECO:0000269|PubMed:9159104}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with PDZ domain-
CC containing proteins like SNTG1 and SNX27. {ECO:0000269|PubMed:11352924,
CC ECO:0000269|PubMed:17351151}.
CC -!- PTM: Phosphorylation of the MARCKS homology domain by PKC reduces
CC nuclear accumulation of DGK-zeta. {ECO:0000269|PubMed:9716136}.
CC -!- MISCELLANEOUS: [Isoform 2]: Minor isoform.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60859.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U51477; AAC50478.1; -; mRNA.
DR EMBL; U94905; AAB60859.1; ALT_FRAME; mRNA.
DR EMBL; AK124594; BAC85894.1; -; mRNA.
DR EMBL; AK294888; BAH11915.1; -; mRNA.
DR EMBL; AK300577; BAH13309.1; -; mRNA.
DR EMBL; AK225774; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC116021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68008.1; -; Genomic_DNA.
DR EMBL; BC041770; AAH41770.1; -; mRNA.
DR CCDS; CCDS41640.1; -. [Q13574-1]
DR CCDS; CCDS44579.2; -. [Q13574-7]
DR CCDS; CCDS44580.1; -. [Q13574-4]
DR CCDS; CCDS55757.1; -. [Q13574-5]
DR CCDS; CCDS55758.1; -. [Q13574-6]
DR CCDS; CCDS55759.1; -. [Q13574-2]
DR CCDS; CCDS7918.1; -. [Q13574-3]
DR RefSeq; NP_001099010.1; NM_001105540.1. [Q13574-1]
DR RefSeq; NP_001186195.1; NM_001199266.1. [Q13574-5]
DR RefSeq; NP_001186196.1; NM_001199267.1. [Q13574-2]
DR RefSeq; NP_001186197.1; NM_001199268.1. [Q13574-6]
DR RefSeq; NP_003637.2; NM_003646.3. [Q13574-4]
DR RefSeq; NP_963290.1; NM_201532.2. [Q13574-3]
DR RefSeq; NP_963291.2; NM_201533.3. [Q13574-7]
DR PDB; 5ELQ; X-ray; 1.10 A; C/P=921-928.
DR PDBsum; 5ELQ; -.
DR AlphaFoldDB; Q13574; -.
DR SMR; Q13574; -.
DR BioGRID; 114095; 78.
DR CORUM; Q13574; -.
DR IntAct; Q13574; 23.
DR MINT; Q13574; -.
DR STRING; 9606.ENSP00000412178; -.
DR ChEMBL; CHEMBL4105942; -.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR SwissLipids; SLP:000000547; -.
DR SwissLipids; SLP:000000921; -. [Q13574-1]
DR SwissLipids; SLP:000000922; -. [Q13574-2]
DR iPTMnet; Q13574; -.
DR MetOSite; Q13574; -.
DR PhosphoSitePlus; Q13574; -.
DR BioMuta; DGKZ; -.
DR DMDM; 215274170; -.
DR EPD; Q13574; -.
DR jPOST; Q13574; -.
DR MassIVE; Q13574; -.
DR MaxQB; Q13574; -.
DR PaxDb; Q13574; -.
DR PeptideAtlas; Q13574; -.
DR PRIDE; Q13574; -.
DR ProteomicsDB; 22840; -.
DR ProteomicsDB; 32183; -.
DR ProteomicsDB; 59578; -. [Q13574-1]
DR ProteomicsDB; 59579; -. [Q13574-2]
DR ProteomicsDB; 59580; -. [Q13574-3]
DR ProteomicsDB; 6789; -.
DR Antibodypedia; 26268; 250 antibodies from 31 providers.
DR DNASU; 8525; -.
DR Ensembl; ENST00000318201.12; ENSP00000320340.8; ENSG00000149091.15. [Q13574-6]
DR Ensembl; ENST00000343674.10; ENSP00000343065.6; ENSG00000149091.15. [Q13574-3]
DR Ensembl; ENST00000421244.6; ENSP00000391021.2; ENSG00000149091.15. [Q13574-4]
DR Ensembl; ENST00000454345.5; ENSP00000412178.1; ENSG00000149091.15. [Q13574-1]
DR Ensembl; ENST00000456247.6; ENSP00000395684.2; ENSG00000149091.15. [Q13574-2]
DR Ensembl; ENST00000527911.5; ENSP00000436291.1; ENSG00000149091.15. [Q13574-5]
DR Ensembl; ENST00000532868.6; ENSP00000436273.2; ENSG00000149091.15. [Q13574-7]
DR GeneID; 8525; -.
DR KEGG; hsa:8525; -.
DR MANE-Select; ENST00000456247.7; ENSP00000395684.2; NM_001199267.2; NP_001186196.1.
DR UCSC; uc001nch.2; human. [Q13574-2]
DR CTD; 8525; -.
DR DisGeNET; 8525; -.
DR GeneCards; DGKZ; -.
DR HGNC; HGNC:2857; DGKZ.
DR HPA; ENSG00000149091; Tissue enhanced (brain).
DR MIM; 601441; gene.
DR neXtProt; NX_Q13574; -.
DR OpenTargets; ENSG00000149091; -.
DR PharmGKB; PA27318; -.
DR VEuPathDB; HostDB:ENSG00000149091; -.
DR eggNOG; KOG0782; Eukaryota.
DR GeneTree; ENSGT00940000156152; -.
DR InParanoid; Q13574; -.
DR OMA; GEPCKLT; -.
DR OrthoDB; 274339at2759; -.
DR PhylomeDB; Q13574; -.
DR TreeFam; TF312817; -.
DR BRENDA; 2.7.1.107; 2681.
DR PathwayCommons; Q13574; -.
DR Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR SignaLink; Q13574; -.
DR SIGNOR; Q13574; -.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 8525; 14 hits in 1084 CRISPR screens.
DR ChiTaRS; DGKZ; human.
DR GeneWiki; DGKZ; -.
DR GenomeRNAi; 8525; -.
DR Pharos; Q13574; Tchem.
DR PRO; PR:Q13574; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13574; protein.
DR Bgee; ENSG00000149091; Expressed in right frontal lobe and 99 other tissues.
DR ExpressionAtlas; Q13574; baseline and differential.
DR Genevisible; Q13574; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IDA:BHF-UCL.
DR GO; GO:0001727; F:lipid kinase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; NAS:UniProtKB.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0046486; P:glycerolipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IDA:UniProtKB.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IGI:UniProtKB.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IGI:UniProtKB.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0090216; P:positive regulation of 1-phosphatidylinositol-4-phosphate 5-kinase activity; IMP: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 3D-structure; Alternative splicing; ANK repeat; ATP-binding; Cell membrane;
KW Cell projection; Cytoplasm; Kinase; Lipid metabolism; Membrane;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..928
FT /note="Diacylglycerol kinase zeta"
FT /id="PRO_0000218468"
FT DOMAIN 291..425
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT REPEAT 822..852
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 857..886
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT ZN_FING 98..152
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 172..230
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..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..273
FT /note="MARCKS homology"
FT REGION 278..416
FT /note="Mediates interaction with RASGRP1"
FT /evidence="ECO:0000269|PubMed:11257115"
FT REGION 759..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 361..369
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q80UP3"
FT MOTIF 924..928
FT /note="PDZ-binding"
FT /evidence="ECO:0000269|PubMed:11352924,
FT ECO:0000269|PubMed:17351151"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..269
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..54
FT /note="MEPRDGSPEARSSDSESASASSSGSERDAGPEPDKAPRRLNKRRFPGLRLFG
FT HR -> MSAPGAGHSAGGSCNESSALGPVEALGTEEGERPGSLRQMWRYRSWDVPQIPS
FT EAPQTQ (in isoform 7)"
FT /id="VSP_060597"
FT VAR_SEQ 1..53
FT /note="MEPRDGSPEARSSDSESASASSSGSERDAGPEPDKAPRRLNKRRFPGLRLFG
FT H -> MAEGQGGGGQRWDWAGGGRAAEEEVVRRRCRRGEEAQVAQPWPEGSRGTAAGPP
FT VEERFRQLHLRKQVSY (in isoform 3)"
FT /id="VSP_060598"
FT VAR_SEQ 3..54
FT /note="PRDGSPEARSSDSESASASSSGSERDAGPEPDKAPRRLNKRRFPGLRLFGHR
FT -> TFFRRHFRGKVPGPGEGQQRPSSVGLPTGKARRRSPAGQASSSLAQRRRSSAQLQG
FT CLLSCGVRAQGSSRRRSSTVPPSCNPRFIVDKVLTPQPTTVGAQLLGAPLLLTGLVGMN
FT EEEGVQEDVVAEASSAIQPGTKTPGPPPPRGAQPLLPLPRYLRRASSHLLPADAVYDHA
FT LWGLHGYYRRLSQRRPSGQHPGPGGRRASGTTAGTMLPTRVRPLSRRRQVALRRKAAGP
FT QAWSALLA (in isoform 2)"
FT /id="VSP_060599"
FT VAR_SEQ 91
FT /note="Missing (in isoform 7)"
FT /id="VSP_060600"
FT VAR_SEQ 122
FT /note="L -> LQ (in isoform 6, isoform 7, isoform 5 and
FT isoform 4)"
FT /id="VSP_060601"
FT VAR_SEQ 167..189
FT /note="Missing (in isoform 6)"
FT /id="VSP_060602"
FT VAR_SEQ 857
FT /note="N -> NPCSPS (in isoform 5)"
FT /id="VSP_060603"
FT VARIANT 523
FT /note="Q -> K (in dbSNP:rs17854149)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_069059"
FT MUTAGEN 926..927
FT /note="TA->NS: Loss of interaction with SNTG1."
FT /evidence="ECO:0000269|PubMed:11352924"
FT CONFLICT 305
FT /note="G -> W (in Ref. 3; BAH11915)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="A -> S (in Ref. 3; BAH11915)"
FT /evidence="ECO:0000305"
FT STRAND 923..927
FT /evidence="ECO:0007829|PDB:5ELQ"
FT VARIANT Q13574-1:21
FT /note="Q -> R (in dbSNP:rs1317826)"
FT /evidence="ECO:0000269|PubMed:9159104"
FT /id="VAR_083552"
FT CONFLICT Q13574-1:159
FT /note="L -> V (in Ref. 2; AAB60859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 928 AA; 103981 MW; 7936A979CB3D35AA CRC64;
MEPRDGSPEA RSSDSESASA SSSGSERDAG PEPDKAPRRL NKRRFPGLRL FGHRKAITKS
GLQHLAPPPP TPGAPCSESE RQIRSTVDWS ESATYGEHIW FETNVSGDFC YVGEQYCVAR
MLKSVSRRKC AACKIVVHTP CIEQLEKINF RCKPSFRESG SRNVREPTFV RHHWVHRRRQ
DGKCRHCGKG FQQKFTFHSK EIVAISCSWC KQAYHSKVSC FMLQQIEEPC SLGVHAAVVI
PPTWILRARR PQNTLKASKK KKRASFKRKS SKKGPEEGRW RPFIIRPTPS PLMKPLLVFV
NPKSGGNQGA KIIQSFLWYL NPRQVFDLSQ GGPKEALEMY RKVHNLRILA CGGDGTVGWI
LSTLDQLRLK PPPPVAILPL GTGNDLARTL NWGGGYTDEP VSKILSHVEE GNVVQLDRWD
LHAEPNPEAG PEDRDEGATD RLPLDVFNNY FSLGFDAHVT LEFHESREAN PEKFNSRFRN
KMFYAGTAFS DFLMGSSKDL AKHIRVVCDG MDLTPKIQDL KPQCVVFLNI PRYCAGTMPW
GHPGEHHDFE PQRHDDGYLE VIGFTMTSLA ALQVGGHGER LTQCREVVLT TSKAIPVQVD
GEPCKLAASR IRIALRNQAT MVQKAKRRSA APLHSDQQPV PEQLRIQVSR VSMHDYEALH
YDKEQLKEAS VPLGTVVVPG DSDLELCRAH IERLQQEPDG AGAKSPTCQK LSPKWCFLDA
TTASRFYRID RAQEHLNYVT EIAQDEIYIL DPELLGASAR PDLPTPTSPL PTSPCSPTPR
SLQGDAAPPQ GEELIEAAKR NDFCKLQELH RAGGDLMHRD EQSRTLLHHA VSTGSKDVVR
YLLDHAPPEI LDAVEENGET CLHQAAALGQ RTICHYIVEA GASLMKTDQQ GDTPRQRAEK
AQDTELAAYL ENRQHYQMIQ REDQETAV
