ID NOTC3_MOUSE Reviewed; 2318 AA. AC Q61982; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 14-OCT-2015, entry version 159. DE RecName: Full=Neurogenic locus notch homolog protein 3; DE Short=Notch 3; DE Contains: DE RecName: Full=Notch 3 extracellular truncation; DE Contains: DE RecName: Full=Notch 3 intracellular domain; DE Flags: Precursor; GN Name=Notch3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ICR X Swiss Webster; RX PubMed=7918097; DOI=10.1016/0925-4773(94)90081-7; RA Lardelli M., Dalstrand J., Lendahl U.; RT "The novel Notch homologue mouse Notch 3 lacks specific epidermal RT growth factor-repeats and is expressed in proliferating RT neuroepithelium."; RL Mech. Dev. 46:123-136(1994). RN [2] RP PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF MET-1664. RX PubMed=11518718; DOI=10.1074/jbc.M107234200; RA Saxena M.T., Schroeter E.H., Mumm J.S., Kopan R.; RT "Murine notch homologs (N1-4) undergo presenilin-dependent RT proteolysis."; RL J. Biol. Chem. 276:40268-40273(2001). RN [3] RP PROTEOLYTIC PROCESSING. RX PubMed=11459941; DOI=10.1073/pnas.161269998; RA Mizutani T., Taniguchi Y., Aoki T., Hashimoto N., Honjo T.; RT "Conservation of the biochemical mechanisms of signal transduction RT among mammalian Notch family members."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9026-9031(2001). RN [4] RP INTERACTION WITH MAML1. RX PubMed=15019995; DOI=10.1016/j.gene.2003.12.007; RA Wu L., Kobayashi K., Sun T., Gao P., Liu J., Nakamura M., Weisberg E., RA Mukhopadhyay N.K., Griffin J.D.; RT "Cloning and functional characterization of the murine mastermind-like RT 1 (Maml1) gene."; RL Gene 328:153-165(2004). RN [5] RP INTERACTION WITH HIF1AN. RX PubMed=17573339; DOI=10.1074/jbc.M704102200; RA Coleman M.L., McDonough M.A., Hewitson K.S., Coles C., Mecinovic J., RA Edelmann M., Cook K.M., Cockman M.E., Lancaster D.E., Kessler B.M., RA Oldham N.J., Ratcliffe P.J., Schofield C.J.; RT "Asparaginyl hydroxylation of the Notch ankyrin repeat domain by RT factor inhibiting hypoxia-inducible factor."; RL J. Biol. Chem. 282:24027-24038(2007). RN [6] RP HYDROXYLATION BY HIF1AN. RX PubMed=18299578; DOI=10.1073/pnas.0711591105; RA Zheng X., Linke S., Dias J.M., Zheng X., Gradin K., Wallis T.P., RA Hamilton B.R., Gustafsson M., Ruas J.L., Wilkins S., Bilton R.L., RA Brismar K., Whitelaw M.L., Pereira T., Gorman J.J., Ericson J., RA Peet D.J., Lendahl U., Poellinger L.; RT "Interaction with factor inhibiting HIF-1 defines an additional mode RT of cross-coupling between the Notch and hypoxia signaling pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3368-3373(2008). CC -!- FUNCTION: Functions as a receptor for membrane-bound ligands CC Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. CC Upon ligand activation through the released notch intracellular CC domain (NICD) it forms a transcriptional activator complex with CC RBPJ/RBPSUH and activates genes of the enhancer of split locus. CC Affects the implementation of differentiation, proliferation and CC apoptotic programs (By similarity). May play a role during CNS CC development. {ECO:0000250}. CC -!- SUBUNIT: Interacts with PSMA1 (By similarity). Heterodimer of a C- CC terminal fragment N(TM) and a N-terminal fragment N(EC) which are CC probably linked by disulfide bonds. Interacts with MAML1, MAML2 CC and MAML3 which act as transcriptional coactivators for NOTCH3. CC Interacts with HIF1AN. {ECO:0000250, ECO:0000269|PubMed:15019995, CC ECO:0000269|PubMed:17573339}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. CC -!- SUBCELLULAR LOCATION: Notch 3 intracellular domain: Nucleus. CC Note=Following proteolytical processing NICD is translocated to CC the nucleus. CC -!- TISSUE SPECIFICITY: Proliferating neuroepithelium. CC -!- DEVELOPMENTAL STAGE: CNS development. CC -!- PTM: Synthesized in the endoplasmic reticulum as an inactive form CC which is proteolytically cleaved by a furin-like convertase in the CC trans-Golgi network before it reaches the plasma membrane to yield CC an active, ligand-accessible form. Cleavage results in a C- CC terminal fragment N(TM) and a N-terminal fragment N(EC). Following CC ligand binding, it is cleaved by TNF-alpha converting enzyme CC (TACE) to yield a membrane-associated intermediate fragment called CC notch extracellular truncation (NEXT). This fragment is then CC cleaved by presenilin dependent gamma-secretase to release a CC notch-derived peptide containing the intracellular domain (NICD) CC from the membrane. {ECO:0000269|PubMed:11459941, CC ECO:0000269|PubMed:11518718}. CC -!- PTM: Phosphorylated. CC -!- PTM: Hydroxylated by HIF1AN. {ECO:0000269|PubMed:18299578}. CC -!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}. CC -!- SIMILARITY: Contains 5 ANK repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00023}. CC -!- SIMILARITY: Contains 34 EGF-like domains. {ECO:0000255|PROSITE- CC ProRule:PRU00076}. CC -!- SIMILARITY: Contains 3 LNR (Lin/Notch) repeats. CC {ECO:0000255|PROSITE-ProRule:PRU00525}. 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; X74760; CAA52776.1; -; mRNA. DR CCDS; CCDS28614.1; -. DR PIR; S45306; S45306. DR RefSeq; NP_032742.1; NM_008716.2. DR UniGene; Mm.439741; -. DR ProteinModelPortal; Q61982; -. DR SMR; Q61982; 392-506, 1792-2027. DR BioGrid; 201811; 5. DR IntAct; Q61982; 3. DR MINT; MINT-1955915; -. DR STRING; 10090.ENSMUSP00000085016; -. DR PhosphoSite; Q61982; -. DR MaxQB; Q61982; -. DR PaxDb; Q61982; -. DR PRIDE; Q61982; -. DR Ensembl; ENSMUST00000087723; ENSMUSP00000085016; ENSMUSG00000038146. DR GeneID; 18131; -. DR KEGG; mmu:18131; -. DR UCSC; uc008bvx.1; mouse. DR CTD; 4854; -. DR MGI; MGI:99460; Notch3. DR eggNOG; COG0666; -. DR GeneTree; ENSGT00810000125346; -. DR HOGENOM; HOG000234369; -. DR HOVERGEN; HBG052650; -. DR InParanoid; Q61982; -. DR KO; K02599; -. DR OMA; ADHFADG; -. DR OrthoDB; EOG7992RD; -. DR PhylomeDB; Q61982; -. DR TreeFam; TF351641; -. DR Reactome; R-MMU-1912399; Pre-NOTCH Processing in the Endoplasmic Reticulum. DR Reactome; R-MMU-1912420; Pre-NOTCH Processing in Golgi. DR Reactome; R-MMU-1980148; Signaling by NOTCH3. DR Reactome; R-MMU-350054; Notch-HLH transcription pathway. DR NextBio; 293368; -. DR PRO; PR:Q61982; -. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; Q61982; -. DR CleanEx; MM_NOTCH3; -. DR Genevisible; Q61982; MM. DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005887; C:integral component of plasma membrane; IC:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0043235; C:receptor complex; ISO:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0048844; P:artery morphogenesis; IMP:MGI. DR GO; GO:0030900; P:forebrain development; IGI:MGI. DR GO; GO:0072104; P:glomerular capillary formation; IEP:UniProtKB. DR GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI. DR GO; GO:0048663; P:neuron fate commitment; IGI:MGI. DR GO; GO:0007219; P:Notch signaling pathway; IDA:UniProtKB. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.20; -; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR020683; Ankyrin_rpt-contain_dom. DR InterPro; IPR024600; DUF3454_notch. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR009030; Growth_fac_rcpt_N_dom. DR InterPro; IPR022331; Notch_3. DR InterPro; IPR000800; Notch_dom. DR InterPro; IPR010660; Notch_NOD_dom. DR InterPro; IPR011656; Notch_NODP_dom. DR PANTHER; PTHR24033:SF47; PTHR24033:SF47; 1. DR Pfam; PF12796; Ank_2; 1. DR Pfam; PF11936; DUF3454; 1. DR Pfam; PF00008; EGF; 18. DR Pfam; PF07645; EGF_CA; 7. DR Pfam; PF12661; hEGF; 3. DR Pfam; PF06816; NOD; 1. DR Pfam; PF07684; NODP; 1. DR Pfam; PF00066; Notch; 3. DR PRINTS; PR01452; LNOTCHREPEAT. DR PRINTS; PR01986; NOTCH3. DR SMART; SM00248; ANK; 6. DR SMART; SM00181; EGF; 15. DR SMART; SM00179; EGF_CA; 19. DR SMART; SM00004; NL; 3. DR SUPFAM; SSF48403; SSF48403; 1. DR SUPFAM; SSF57184; SSF57184; 5. DR SUPFAM; SSF90193; SSF90193; 3. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 4. DR PROSITE; PS00010; ASX_HYDROXYL; 18. DR PROSITE; PS00022; EGF_1; 33. DR PROSITE; PS01186; EGF_2; 27. DR PROSITE; PS50026; EGF_3; 34. DR PROSITE; PS01187; EGF_CA; 16. DR PROSITE; PS50258; LNR; 3. PE 1: Evidence at protein level; KW Activator; ANK repeat; Cell membrane; Complete proteome; KW Developmental protein; Differentiation; Disulfide bond; KW EGF-like domain; Glycoprotein; Membrane; Notch signaling pathway; KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; KW Transcription; Transcription regulation; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 39 {ECO:0000255}. FT CHAIN 40 2318 Neurogenic locus notch homolog protein 3. FT /FTId=PRO_0000007695. FT CHAIN 1630 2318 Notch 3 extracellular truncation. FT /FTId=PRO_0000007696. FT CHAIN 1663 2318 Notch 3 intracellular domain. FT /FTId=PRO_0000007697. FT TOPO_DOM 40 1643 Extracellular. FT TRANSMEM 1644 1664 Helical. {ECO:0000255}. FT TOPO_DOM 1665 2318 Cytoplasmic. FT DOMAIN 40 78 EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 79 119 EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 120 157 EGF-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 159 196 EGF-like 4; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 198 235 EGF-like 5. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 237 273 EGF-like 6; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 275 313 EGF-like 7. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 315 351 EGF-like 8; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 352 390 EGF-like 9. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 392 430 EGF-like 10; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 432 468 EGF-like 11; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 470 506 EGF-like 12; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 508 544 EGF-like 13; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 546 581 EGF-like 14; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 583 619 EGF-like 15; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 621 656 EGF-like 16; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 658 694 EGF-like 17; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 696 731 EGF-like 18. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 735 771 EGF-like 19. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 772 809 EGF-like 20. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 811 848 EGF-like 21; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 850 886 EGF-like 22; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 888 923 EGF-like 23; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 925 961 EGF-like 24. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 963 999 EGF-like 25. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1001 1035 EGF-like 26. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1037 1083 EGF-like 27. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1085 1121 EGF-like 28. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1123 1159 EGF-like 29; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 1161 1204 EGF-like 30; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DOMAIN 1206 1245 EGF-like 31. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1247 1288 EGF-like 32. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1290 1326 EGF-like 33. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1336 1374 EGF-like 34. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT REPEAT 1388 1428 LNR 1. FT REPEAT 1429 1466 LNR 2. FT REPEAT 1468 1506 LNR 3. FT REPEAT 1839 1868 ANK 1. FT REPEAT 1872 1902 ANK 2. FT REPEAT 1906 1935 ANK 3. FT REPEAT 1939 1968 ANK 4. FT REPEAT 1972 2001 ANK 5. FT REGION 2242 2261 PEST-like. FT SITE 1572 1573 Cleavage; by furin-like protease. FT {ECO:0000250}. FT CARBOHYD 1180 1180 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 1337 1337 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 1439 1439 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 43 55 {ECO:0000250}. FT DISULFID 49 66 {ECO:0000250}. FT DISULFID 68 77 {ECO:0000250}. FT DISULFID 83 94 {ECO:0000250}. FT DISULFID 88 107 {ECO:0000250}. FT DISULFID 109 118 {ECO:0000250}. FT DISULFID 124 135 {ECO:0000250}. FT DISULFID 129 145 {ECO:0000250}. FT DISULFID 147 156 {ECO:0000250}. FT DISULFID 163 175 {ECO:0000250}. FT DISULFID 169 184 {ECO:0000250}. FT DISULFID 186 195 {ECO:0000250}. FT DISULFID 202 213 {ECO:0000250}. FT DISULFID 207 223 {ECO:0000250}. FT DISULFID 225 234 {ECO:0000250}. FT DISULFID 241 252 {ECO:0000250}. FT DISULFID 246 261 {ECO:0000250}. FT DISULFID 263 272 {ECO:0000250}. FT DISULFID 279 292 {ECO:0000250}. FT DISULFID 286 301 {ECO:0000250}. FT DISULFID 303 312 {ECO:0000250}. FT DISULFID 319 330 {ECO:0000250}. FT DISULFID 324 339 {ECO:0000250}. FT DISULFID 341 350 {ECO:0000250}. FT DISULFID 356 367 {ECO:0000250}. FT DISULFID 361 378 {ECO:0000250}. FT DISULFID 380 389 {ECO:0000250}. FT DISULFID 396 409 {ECO:0000250}. FT DISULFID 403 418 {ECO:0000250}. FT DISULFID 420 429 {ECO:0000250}. FT DISULFID 436 447 {ECO:0000250}. FT DISULFID 441 456 {ECO:0000250}. FT DISULFID 458 467 {ECO:0000250}. FT DISULFID 474 485 {ECO:0000250}. FT DISULFID 479 494 {ECO:0000250}. FT DISULFID 496 505 {ECO:0000250}. FT DISULFID 512 523 {ECO:0000250}. FT DISULFID 517 532 {ECO:0000250}. FT DISULFID 534 543 {ECO:0000250}. FT DISULFID 550 560 {ECO:0000250}. FT DISULFID 555 569 {ECO:0000250}. FT DISULFID 571 580 {ECO:0000250}. FT DISULFID 587 598 {ECO:0000250}. FT DISULFID 592 607 {ECO:0000250}. FT DISULFID 609 618 {ECO:0000250}. FT DISULFID 625 635 {ECO:0000250}. FT DISULFID 630 644 {ECO:0000250}. FT DISULFID 646 655 {ECO:0000250}. FT DISULFID 662 673 {ECO:0000250}. FT DISULFID 667 682 {ECO:0000250}. FT DISULFID 684 693 {ECO:0000250}. FT DISULFID 700 710 {ECO:0000250}. FT DISULFID 705 719 {ECO:0000250}. FT DISULFID 721 730 {ECO:0000250}. FT DISULFID 739 750 {ECO:0000250}. FT DISULFID 744 759 {ECO:0000250}. FT DISULFID 761 770 {ECO:0000250}. FT DISULFID 776 787 {ECO:0000250}. FT DISULFID 781 797 {ECO:0000250}. FT DISULFID 799 808 {ECO:0000250}. FT DISULFID 815 827 {ECO:0000250}. FT DISULFID 821 836 {ECO:0000250}. FT DISULFID 838 847 {ECO:0000250}. FT DISULFID 854 865 {ECO:0000250}. FT DISULFID 859 874 {ECO:0000250}. FT DISULFID 876 885 {ECO:0000250}. FT DISULFID 892 902 {ECO:0000250}. FT DISULFID 897 911 {ECO:0000250}. FT DISULFID 913 922 {ECO:0000250}. FT DISULFID 929 940 {ECO:0000250}. FT DISULFID 934 949 {ECO:0000250}. FT DISULFID 951 960 {ECO:0000250}. FT DISULFID 967 978 {ECO:0000250}. FT DISULFID 972 987 {ECO:0000250}. FT DISULFID 989 998 {ECO:0000250}. FT DISULFID 1005 1016 {ECO:0000250}. FT DISULFID 1010 1023 {ECO:0000250}. FT DISULFID 1025 1034 {ECO:0000250}. FT DISULFID 1041 1062 {ECO:0000250}. FT DISULFID 1056 1071 {ECO:0000250}. FT DISULFID 1073 1082 {ECO:0000250}. FT DISULFID 1089 1100 {ECO:0000250}. FT DISULFID 1094 1109 {ECO:0000250}. FT DISULFID 1111 1120 {ECO:0000250}. FT DISULFID 1127 1138 {ECO:0000250}. FT DISULFID 1132 1147 {ECO:0000250}. FT DISULFID 1149 1158 {ECO:0000250}. FT DISULFID 1165 1183 {ECO:0000250}. FT DISULFID 1177 1192 {ECO:0000250}. FT DISULFID 1194 1203 {ECO:0000250}. FT DISULFID 1210 1223 {ECO:0000250}. FT DISULFID 1215 1233 {ECO:0000250}. FT DISULFID 1235 1244 {ECO:0000250}. FT DISULFID 1251 1262 {ECO:0000250}. FT DISULFID 1256 1276 {ECO:0000250}. FT DISULFID 1278 1287 {ECO:0000250}. FT DISULFID 1294 1305 {ECO:0000250}. FT DISULFID 1299 1314 {ECO:0000250}. FT DISULFID 1316 1325 {ECO:0000250}. FT DISULFID 1340 1351 {ECO:0000250}. FT DISULFID 1345 1362 {ECO:0000250}. FT DISULFID 1364 1373 {ECO:0000250}. FT DISULFID 1388 1411 {ECO:0000250}. FT DISULFID 1393 1406 {ECO:0000250}. FT DISULFID 1402 1418 {ECO:0000250}. FT DISULFID 1429 1452 {ECO:0000250}. FT DISULFID 1434 1447 {ECO:0000250}. FT DISULFID 1443 1459 {ECO:0000250}. FT DISULFID 1468 1494 {ECO:0000250}. FT DISULFID 1476 1489 {ECO:0000250}. FT DISULFID 1485 1501 {ECO:0000250}. FT MUTAGEN 1664 1664 M->L: No effect on NICD processing. FT {ECO:0000269|PubMed:11518718}. SQ SEQUENCE 2318 AA; 244248 MW; A80D1F75AFF0185A CRC64; MGLGARGRRR RRRLMALPPP PPPMRALPLL LLLAGLGAAA PPCLDGSPCA NGGRCTHQQP SLEAACLCLP GWVGERCQLE DPCHSGPCAG RGVCQSSVVA GTARFSCRCL RGFQGPDCSQ PDPCVSRPCV HGAPCSVGPD GRFACACPPG YQGQSCQSDI DECRSGTTCR HGGTCLNTPG SFRCQCPLGY TGLLCENPVV PCAPSPCRNG GTCRQSSDVT YDCACLPGFE GQNCEVNVDD CPGHRCLNGG TCVDGVNTYN CQCPPEWTGQ FCTEDVDECQ LQPNACHNGG TCFNLLGGHS CVCVNGWTGE SCSQNIDDCA TAVCFHGATC HDRVASFYCA CPMGKTGLLC HLDDACVSNP CHEDAICDTN PVSGRAICTC PPGFTGGACD QDVDECSIGA NPCEHLGRCV NTQGSFLCQC GRGYTGPRCE TDVNECLSGP CRNQATCLDR IGQFTCICMA GFTGTYCEVD IDECQSSPCV NGGVCKDRVN GFSCTCPSGF SGSMCQLDVD ECASTPCRNG AKCVDQPDGY ECRCAEGFEG TLCERNVDDC SPDPCHHGRC VDGIASFSCA CAPGYTGIRC ESQVDECRSQ PCRYGGKCLD LVDKYLCRCP PGTTGVNCEV NIDDCASNPC TFGVCRDGIN RYDCVCQPGF TGPLCNVEIN ECASSPCGEG GSCVDGENGF HCLCPPGSLP PLCLPANHPC AHKPCSHGVC HDAPGGFRCV CEPGWSGPRC SQSLAPDACE SQPCQAGGTC TSDGIGFRCT CAPGFQGHQC EVLSPCTPSL CEHGGHCESD PDRLTVCSCP PGWQGPRCQQ DVDECAGASP CGPHGTCTNL PGNFRCICHR GYTGPFCDQD IDDCDPNPCL HGGSCQDGVG SFSCSCLDGF AGPRCARDVD ECLSSPCGPG TCTDHVASFT CACPPGYGGF HCEIDLPDCS PSSCFNGGTC VDGVSSFSCL CRPGYTGTHC QYEADPCFSR PCLHGGICNP THPGFECTCR EGFTGSQCQN PVDWCSQAPC QNGGRCVQTG AYCICPPGWS GRLCDIQSLP CTEAAAQMGV RLEQLCQEGG KCIDKGRSHY CVCPEGRTGS HCEHEVDPCT AQPCQHGGTC RGYMGGYVCE CPAGYAGDSC EDNIDECASQ PCQNGGSCID LVARYLCSCP PGTLGVLCEI NEDDCDLGPS LDSGVQCLHN GTCVDLVGGF RCNCPPGYTG LHCEADINEC RPGACHAAHT RDCLQDPGGH FRCVCHPGFT GPRCQIALSP CESQPCQHGG QCRHSLGRGG GLTFTCHCVP PFWGLRCERV ARSCRELQCP VGIPCQQTAR GPRCACPPGL SGPSCRVSRA SPSGATNASC ASAPCLHGGS CLPVQSVPFF RCVCAPGWGG PRCETPSAAP EVPEEPRCPR AACQAKRGDQ NCDRECNTPG CGWDGGDCSL NVDDPWRQCE ALQCWRLFNN SRCDPACSSP ACLYDNFDCY SGGRDRTCNP VYEKYCADHF ADGRCDQGCN TEECGWDGLD CASEVPALLA RGVLVLTVLL PPEELLRSSA DFLQRLSAIL RTSLRFRLDA RGQAMVFPYH RPSPGSESRV RRELGPEVIG SVVMLEIDNR LCLQSAENDH CFPDAQSAAD YLGALSAVER LDFPYPLRDV RGEPLEAPEQ SVPLLPLLVA GAVFLLIIFI LGVMVARRKR EHSTLWFPEG FALHKDIAAG HKGRREPVGQ DALGMKNMAK GESLMGEVVT DLNDSECPEA KRLKVEEPGM GAEEPEDCRQ WTQHHLVAAD IRVAPATALT PPQGDADADG VDVNVRGPDG FTPLMLASFC GGALEPMPAE EDEADDTSAS IISDLICQGA QLGARTDRTG ETALHLAARY ARADAAKRLL DAGADTNAQD HSGRTPLHTA VTADAQGVFQ ILIRNRSTDL DARMADGSTA LILAARLAVE GMVEELIASH ADVNAVDELG KSALHWAAAV NNVEATLALL KNGANKDMQD SKEETPLFLA AREGSYEAAK LLLDHLANRE ITDHLDRLPR DVAQERLHQD IVRLLDQPSG PRSPSGPHGL GPLLCPPGAF LPGLKAVQSG TKKSRRPPGK TGLGPQGTRG RGKKLTLACP GPLADSSVTL SPVDSLDSPR PFSGPPASPG GFPLEGPYAT TATAVSLAQL GASRAGPLGR QPPGGCVLSF GLLNPVAVPL DWARLPPPAP PGPSFLLPLA PGPQLLNPGA PVSPQERPPP YLAAPGHGEE YPAAGTRSSP TKARFLRVPS EHPYLTPSPE SPEHWASPSP PSLSDWSDST PSPATATNAT ASGALPAQPH PISVPSLPQS QTQLGPQPEV TPKRQVMA //