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 24-JAN-2024, entry version 162. 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}. 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; 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 GlyGen; Q6NS52; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6NS52; -. DR PhosphoSitePlus; Q6NS52; -. DR SwissPalm; Q6NS52; -. DR EPD; Q6NS52; -. DR PaxDb; 10090-ENSMUSP00000037900; -. DR PeptideAtlas; Q6NS52; -. DR ProteomicsDB; 277322; -. [Q6NS52-1] DR ProteomicsDB; 277323; -. [Q6NS52-2] DR Antibodypedia; 25192; 251 antibodies from 31 providers. DR DNASU; 217480; -. DR Ensembl; ENSMUST00000040500.9; ENSMUSP00000037900.8; ENSMUSG00000036095.12. [Q6NS52-2] DR Ensembl; ENSMUST00000220990.2; ENSMUSP00000152378.2; ENSMUSG00000036095.12. [Q6NS52-2] DR GeneID; 217480; -. DR KEGG; mmu:217480; -. DR UCSC; uc007nkj.1; mouse. [Q6NS52-2] DR UCSC; uc007nkn.1; mouse. [Q6NS52-1] DR AGR; MGI:2442474; -. 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; SSXILHE; -. DR OrthoDB; 4642163at2759; -. 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 77 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 132 other cell types or tissues. DR ExpressionAtlas; Q6NS52; baseline and differential. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0099147; C:extrinsic component of postsynaptic density membrane; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IDA:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0008289; F:lipid binding; ISO:MGI. 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; IDA: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; cd20845; C1_DGKbeta_rpt1; 1. DR CDD; cd20891; C1_DGKbeta_rpt2; 1. DR CDD; cd00051; EFh; 1. DR Gene3D; 2.60.200.40; -; 2. DR Gene3D; 3.30.60.20; -; 2. DR Gene3D; 1.10.238.110; Diacylglycerol kinase alpha; 2. DR Gene3D; 1.10.238.10; EF-hand; 1. DR InterPro; IPR017438; ATP-NAD_kinase_N. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR047471; C1_DGKbeta-like_rpt1. DR InterPro; IPR047470; C1_DGKbeta_rpt2. 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; DIACYLGLYCEROL KINASE; 1. DR PANTHER; PTHR11255:SF32; DIACYLGLYCEROL KINASE BETA; 1. DR Pfam; PF00130; C1_1; 2. DR Pfam; PF14513; DAG_kinase_N; 1. 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; SSF57889; Cysteine-rich domain; 2. DR SUPFAM; SSF47473; EF-hand; 2. DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1. 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. DR Genevisible; Q6NS52; MM. 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 //