DGKB_MOUSE
ID DGKB_MOUSE Reviewed; 802 AA.
AC Q6NS52; Q80TT5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Diacylglycerol kinase beta;
DE Short=DAG kinase beta;
DE EC=2.7.1.107 {ECO:0000269|PubMed:20657643};
DE AltName: Full=Diglyceride kinase beta;
DE Short=DGK-beta;
GN Name=Dgkb; Synonyms=Kiaa0718;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-802 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-117; SER-418 AND SER-791, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY,
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND REGION.
RX PubMed=20657643; DOI=10.1371/journal.pone.0011602;
RA Shirai Y., Kouzuki T., Kakefuda K., Moriguchi S., Oyagi A., Horie K.,
RA Morita S.Y., Shimazawa M., Fukunaga K., Takeda J., Saito N., Hara H.;
RT "Essential role of neuron-enriched diacylglycerol kinase (DGK), DGKbeta in
RT neurite spine formation, contributing to cognitive function.";
RL PLoS ONE 5:e11602-e11602(2010).
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:20657643). Thereby, acts as a
CC central switch between the signaling pathways activated by these second
CC messengers with different cellular targets and opposite effects in
CC numerous biological processes (Probable). Has a higher activity with
CC long-chain diacylglycerols like 1,2-di-(9Z-octadecenoyl)-sn-glycerol
CC compared to 1,2-didecanoyl-sn-glycerol (By similarity). Specifically
CC expressed in brain, it regulates neuron-specific morphological changes
CC including neurite branching and neurite spine formation
CC (PubMed:20657643). {ECO:0000250|UniProtKB:P49621,
CC ECO:0000269|PubMed:20657643, ECO:0000305}.
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:20657643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000269|PubMed:20657643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + ATP =
CC 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:40339, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P49621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340;
CC Evidence={ECO:0000250|UniProtKB:P49621};
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:P49621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000250|UniProtKB:P49621};
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:P49621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000250|UniProtKB:P49621};
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:P49621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000250|UniProtKB:P49621};
CC -!- ACTIVITY REGULATION: Activated by calcium.
CC {ECO:0000250|UniProtKB:P49621}.
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:20657643}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:20657643}; Peripheral membrane protein
CC {ECO:0000305|PubMed:20657643}. Cell membrane
CC {ECO:0000269|PubMed:20657643}; Peripheral membrane protein
CC {ECO:0000305|PubMed:20657643}. Cytoplasm {ECO:0000305|PubMed:20657643}.
CC Note=Translocation to the plasma membrane is induced by phorbol esters.
CC {ECO:0000250|UniProtKB:Q9Y6T7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NS52-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NS52-2; Sequence=VSP_021900;
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus, cerebral cortex, and
CC caudate putamen (at protein level). {ECO:0000269|PubMed:20657643}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice are viable and fertile
CC with no significant difference in weight (PubMed:20657643). However,
CC long-term potentiation (LTP) and cognitive functions including spatial
CC and long-term memory are affected in these mice (PubMed:20657643). A
CC decrease in the total length of neurites and branches together with a
CC reduced number of neurite spines are observed (PubMed:20657643).
CC {ECO:0000269|PubMed:20657643}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; AK139408; BAE23997.1; -; mRNA.
DR EMBL; BC070461; AAH70461.1; -; mRNA.
DR EMBL; AK122355; BAC65637.1; -; mRNA.
DR CCDS; CCDS25889.1; -. [Q6NS52-2]
DR RefSeq; NP_848796.2; NM_178681.4. [Q6NS52-2]
DR RefSeq; XP_006515132.1; XM_006515069.2.
DR RefSeq; XP_006515135.1; XM_006515072.3.
DR RefSeq; XP_017170508.1; XM_017315019.1. [Q6NS52-1]
DR AlphaFoldDB; Q6NS52; -.
DR BioGRID; 229919; 1.
DR STRING; 10090.ENSMUSP00000037900; -.
DR iPTMnet; Q6NS52; -.
DR PhosphoSitePlus; Q6NS52; -.
DR SwissPalm; Q6NS52; -.
DR EPD; Q6NS52; -.
DR PaxDb; Q6NS52; -.
DR PeptideAtlas; Q6NS52; -.
DR PRIDE; Q6NS52; -.
DR ProteomicsDB; 277322; -. [Q6NS52-1]
DR ProteomicsDB; 277323; -. [Q6NS52-2]
DR Antibodypedia; 25192; 224 antibodies from 31 providers.
DR DNASU; 217480; -.
DR Ensembl; ENSMUST00000040500; ENSMUSP00000037900; ENSMUSG00000036095. [Q6NS52-2]
DR Ensembl; ENSMUST00000220990; ENSMUSP00000152378; ENSMUSG00000036095. [Q6NS52-2]
DR GeneID; 217480; -.
DR KEGG; mmu:217480; -.
DR UCSC; uc007nkj.1; mouse. [Q6NS52-2]
DR UCSC; uc007nkn.1; mouse. [Q6NS52-1]
DR CTD; 1607; -.
DR MGI; MGI:2442474; Dgkb.
DR VEuPathDB; HostDB:ENSMUSG00000036095; -.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000159770; -.
DR HOGENOM; CLU_003770_1_0_1; -.
DR InParanoid; Q6NS52; -.
DR OMA; FVKRTRN; -.
DR OrthoDB; 633642at2759; -.
DR PhylomeDB; Q6NS52; -.
DR TreeFam; TF313104; -.
DR Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 217480; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Dgkb; mouse.
DR PRO; PR:Q6NS52; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q6NS52; protein.
DR Bgee; ENSMUSG00000036095; Expressed in dorsal striatum and 129 other tissues.
DR ExpressionAtlas; Q6NS52; baseline and differential.
DR Genevisible; Q6NS52; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:MGI.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
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:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR CDD; cd00029; C1; 2.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.110; -; 2.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR029477; DAG_kinase_typeI_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR038199; DGK_typeI_N_sf.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; PTHR11255; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF14513; DAG_kinase_N; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calcium; Cell membrane; Cytoplasm;
KW Kinase; Lipid metabolism; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Synapse; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..802
FT /note="Diacylglycerol kinase beta"
FT /id="PRO_0000264623"
FT DOMAIN 148..183
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 193..228
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 432..566
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 243..293
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 308..357
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 384..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..802
FT /note="Required for association with membranes and function
FT in neurite spine formation"
FT /evidence="ECO:0000269|PubMed:20657643"
FT COMPBIAS 397..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 50..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021900"
SQ SEQUENCE 802 AA; 90272 MW; 2995ECF41057DEF3 CRC64;
MTNQEKWAHL SPSEFSQLQK YAEYSTKKLK DVLEEFHGNG VLAKYNPEGK QDILNQTIDF
EGFKLFMKTF LEAELPDDFT AHLFMSFSNK FPHSSPNVKS KPALLSGGLR MNKGAITPPR
SSPANTCSPE VIHLKDIVCY LSLLERGRPE DKLEFMFRLY DTDGNGFLDS SELENIIGQM
MHVAEYLEWD VTELNPILHE MMEEIDYDRD GTVSLEEWIQ GGMTTIPLLV LLGLENNVKD
DGQHVWRLKH FNKPAYCNLC LNMLIGVGKQ GLCCSFCKYT VHERCVARAP PSCIKTYVKS
KKNTDVMHHY WVEGNCPTKC DKCHKTVKCY QGLTGLHCVW CQTTLHNKCA SHLKPECDCG
PLKDHILPPT TICPVVLTMP SAGASVPEER QSTAKKEKSS SQQPNKATDK NKMQRANSVT
MDGQGLQITP VPGTHPLLVF VNPKSGGKQG ERIYRKFQYL LNPRQVYSLS GNGPMPGLHF
FRDVPDFRVL ACGGDGTVGW ILDCIEKANV VKHPPVAILP LGTGNDLARC LRWGGGYEGE
NLMKILKDIE SSTEIMLDRW KFEVTPNDKD EKGDPVPYSI INNYFSIGVD ASIAHRFHIM
REKHPEKFNS RMKNKFWYFE FGTSETFSAT CKKLHESVEI ECDGVQIDLI NISLEGIAIL
NIPSMHGGSN LWGESKKKRS HRRIEKKGSD KRPTLTDAKE LKFASQDLSD QLLEVVGLEG
AMEMGQIYTG LKSAGRRLAQ CSSVVIRTSK SLPMQIDGEP WMQTPCTIKI THKNQAPMLM
GPPPKTGLFC SLIKRTRNRS KE
