GenomeNet

Database: UniProt
Entry: O35516
LinkDB: O35516
Original site: O35516 
ID   NOTC2_MOUSE             Reviewed;        2473 AA.
AC   O35516; G5E8J0; Q06008; Q60941;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 2.
DT   10-APR-2019, entry version 198.
DE   RecName: Full=Neurogenic locus notch homolog protein 2 {ECO:0000250|UniProtKB:Q04721};
DE            Short=Notch 2;
DE   AltName: Full=Motch B {ECO:0000303|PubMed:8440332};
DE   Contains:
DE     RecName: Full=Notch 2 extracellular truncation;
DE   Contains:
DE     RecName: Full=Notch 2 intracellular domain;
DE   Flags: Precursor;
GN   Name=Notch2 {ECO:0000312|MGI:MGI:97364};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RA   Hamada Y., Higuchi M., Tsujimoto Y.;
RT   "Complete amino acid sequence and mutliform transcripts encoded by a
RT   single copy of mouse Notch2 gene.";
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 318-1520.
RC   STRAIN=C57BL/6 X CBA; TISSUE=Embryo;
RX   PubMed=8440332; DOI=10.1006/excr.1993.1044;
RA   Lardelli M., Lendahl U.;
RT   "Motch A and Motch B-two mouse Notch homologues coexpressed in a wide
RT   variety of tissues.";
RL   Exp. Cell Res. 204:364-372(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1768-2156.
RX   PubMed=8917536; DOI=10.1073/pnas.93.23.13014;
RA   Milner L.A., Bigas A., Kopan R., Brashem-Stein C., Bernstein I.D.,
RA   Martin D.I.;
RT   "Inhibition of granulocytic differentiation by mNotch1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:13014-13019(1996).
RN   [6]
RP   FUNCTION.
RX   PubMed=10393120;
RA   Hamada Y., Kadokawa Y., Okabe M., Ikawa M., Coleman J.R.,
RA   Tsujimoto Y.;
RT   "Mutation in ankyrin repeats of the mouse Notch2 gene induces early
RT   embryonic lethality.";
RL   Development 126:3415-3424(1999).
RN   [7]
RP   DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
RX   PubMed=7609614; DOI=10.1016/0169-328X(94)00257-F;
RA   Higuchi M., Kiyama H., Hayakawa T., Hamada Y., Tsujimoto Y.;
RT   "Differential expression of Notch1 and Notch2 in developing and adult
RT   mouse brain.";
RL   Brain Res. Mol. Brain Res. 29:263-272(1995).
RN   [8]
RP   PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF MET-1701.
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   [9]
RP   PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF MET-1701.
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   [10]
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   [11]
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   [12]
RP   FUNCTION AS POSITIVE REGULATOR OF OSTEOCLASTOGENESIS, AND INTERACTION
RP   WITH RELA.
RX   PubMed=18710934; DOI=10.1128/MCB.00299-08;
RA   Fukushima H., Nakao A., Okamoto F., Shin M., Kajiya H., Sakano S.,
RA   Bigas A., Jimi E., Okabe K.;
RT   "The association of Notch2 and NF-kappaB accelerates RANKL-induced
RT   osteoclastogenesis.";
RL   Mol. Cell. Biol. 28:6402-6412(2008).
RN   [13]
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).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1780; SER-1843 AND
RP   SER-1846, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Liver;
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [16]
RP   GLYCOSYLATION AT SER-613, AND MUTAGENESIS OF SER-614.
RX   PubMed=21949356; DOI=10.1073/pnas.1109696108;
RA   Takeuchi H., Fernandez-Valdivia R.C., Caswell D.S., Nita-Lazar A.,
RA   Rana N.A., Garner T.P., Weldeghiorghis T.K., Macnaughtan M.A.,
RA   Jafar-Nejad H., Haltiwanger R.S.;
RT   "Rumi functions as both a protein O-glucosyltransferase and a protein
RT   O-xylosyltransferase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:16600-16605(2011).
CC   -!- FUNCTION: Functions as a receptor for membrane-bound ligands
CC       Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate
CC       cell-fate determination (PubMed:10393120). Upon ligand activation
CC       through the released notch intracellular domain (NICD) it forms a
CC       transcriptional activator complex with RBPJ/RBPSUH and activates
CC       genes of the enhancer of split locus (PubMed:10393120,
CC       PubMed:18710934). Affects the implementation of differentiation,
CC       proliferation and apoptotic programs (PubMed:10393120,
CC       PubMed:18710934). May play an essential role in postimplantation
CC       development, probably in some aspect of cell specification and/or
CC       differentiation (By similarity). In collaboration with RELA/p65
CC       enhances NFATc1 promoter activity and positively regulates RANKL-
CC       induced osteoclast differentiation (PubMed:18710934). Positively
CC       regulates self-renewal of liver cancer cells (By similarity).
CC       {ECO:0000250|UniProtKB:Q04721, ECO:0000269|PubMed:10393120,
CC       ECO:0000269|PubMed:18710934}.
CC   -!- SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and an N-
CC       terminal fragment N(EC) which are probably linked by disulfide
CC       bonds. Interacts with MAML1, MAML2 and MAML3 which act as
CC       transcriptional coactivators for NOTCH2. Interacts with RELA/p65.
CC       Interacts with HIF1AN. Interacts (via ANK repeats) with TCIM, the
CC       interaction inhibits the nuclear translocation of NOTCH2 N2ICD (By
CC       similarity). Interacts with CUL1, RBX1, SKP1 and FBXW7 that are
CC       SCF(FBXW7) E3 ubiquitin-protein ligase complex components.
CC       Interacts with MINAR1; this interaction increases MINAR1 stability
CC       and function (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q04721, ECO:0000269|PubMed:15019995,
CC       ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:18710934}.
CC   -!- SUBCELLULAR LOCATION: Notch 2 extracellular truncation: Cell
CC       membrane {ECO:0000250|UniProtKB:Q04721}; Single-pass type I
CC       membrane protein {ECO:0000250|UniProtKB:Q04721}.
CC   -!- SUBCELLULAR LOCATION: Notch 2 intracellular domain: Nucleus
CC       {ECO:0000250|UniProtKB:Q04721}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q04721}. Note=Following proteolytical
CC       processing NICD is translocated to the nucleus. Retained at the
CC       cytoplasm by TCIM. {ECO:0000250|UniProtKB:Q04721}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O35516-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O35516-2; Sequence=VSP_001405;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, liver, kidney,
CC       neuroepithelia, somites, optic vesicles and branchial arches, but
CC       not heart.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the embryonic ventricular zone,
CC       the postnatal ependymal cells, and the choroid plexus throughout
CC       embryonic and postnatal development. {ECO:0000269|PubMed:7609614}.
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 (PubMed:11459941,
CC       PubMed:11518718). Cleavage results in a C-terminal fragment N(TM)
CC       and a N-terminal fragment N(EC) (PubMed:11459941,
CC       PubMed:11518718). Following ligand binding, it is cleaved by TNF-
CC       alpha converting enzyme (TACE) to yield a membrane-associated
CC       intermediate fragment called notch extracellular truncation (NEXT)
CC       (By similarity). This fragment is then cleaved by presenilin
CC       dependent gamma-secretase to release a notch-derived peptide
CC       containing the intracellular domain (NICD) from the membrane
CC       (PubMed:11459941, PubMed:11518718). {ECO:0000250|UniProtKB:Q01705,
CC       ECO:0000269|PubMed:11459941, ECO:0000269|PubMed:11518718}.
CC   -!- PTM: Hydroxylated by HIF1AN. {ECO:0000269|PubMed:18299578}.
CC   -!- PTM: Can be either O-glucosylated or O-xylosylated at Ser-613 by
CC       POGLUT1. {ECO:0000269|PubMed:21949356}.
CC   -!- PTM: Phosphorylated by GSK3. GSK3-mediated phosphorylation is
CC       necessary for NOTCH2 recognition by FBXW7, ubiquitination and
CC       degradation via the ubiquitin proteasome pathway.
CC       {ECO:0000250|UniProtKB:Q04721}.
CC   -!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA22094.1; Type=Frameshift; Positions=1706, 1716; Evidence={ECO:0000305};
DR   EMBL; D32210; BAA22094.1; ALT_FRAME; mRNA.
DR   EMBL; AC154173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC164091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466620; EDL38950.1; -; Genomic_DNA.
DR   EMBL; X68279; CAA48340.1; -; mRNA.
DR   EMBL; U31881; AAC52924.1; -; mRNA.
DR   PIR; A49175; A49175.
DR   RefSeq; NP_035058.2; NM_010928.2.
DR   UniGene; Mm.485843; -.
DR   ProteinModelPortal; O35516; -.
DR   SMR; O35516; -.
DR   BioGrid; 201809; 6.
DR   CORUM; O35516; -.
DR   DIP; DIP-6008N; -.
DR   IntAct; O35516; 2.
DR   STRING; 10090.ENSMUSP00000078741; -.
DR   iPTMnet; O35516; -.
DR   PhosphoSitePlus; O35516; -.
DR   SwissPalm; O35516; -.
DR   jPOST; O35516; -.
DR   MaxQB; O35516; -.
DR   PaxDb; O35516; -.
DR   PeptideAtlas; O35516; -.
DR   PRIDE; O35516; -.
DR   Ensembl; ENSMUST00000079812; ENSMUSP00000078741; ENSMUSG00000027878.
DR   GeneID; 18129; -.
DR   KEGG; mmu:18129; -.
DR   UCSC; uc008qpo.1; mouse.
DR   CTD; 4853; -.
DR   MGI; MGI:97364; Notch2.
DR   eggNOG; ENOG410IR7G; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   GeneTree; ENSGT00940000155030; -.
DR   HOGENOM; HOG000234369; -.
DR   HOVERGEN; HBG052650; -.
DR   InParanoid; O35516; -.
DR   KO; K20994; -.
DR   OMA; RLCQHSG; -.
DR   OrthoDB; 7525at2759; -.
DR   PhylomeDB; O35516; -.
DR   TreeFam; TF351641; -.
DR   Reactome; R-MMU-1912420; Pre-NOTCH Processing in Golgi.
DR   Reactome; R-MMU-2197563; NOTCH2 intracellular domain regulates transcription.
DR   Reactome; R-MMU-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
DR   Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR   ChiTaRS; Notch2; mouse.
DR   PRO; PR:O35516; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Proteomes; UP000000589; Unplaced.
DR   Bgee; ENSMUSG00000027878; Expressed in 347 organ(s), highest expression level in blood.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO: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:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0009887; P:animal organ morphogenesis; TAS:UniProtKB.
DR   GO; GO:0060413; P:atrial septum morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0046849; P:bone remodeling; ISO:MGI.
DR   GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
DR   GO; GO:0001709; P:cell fate determination; ISO:MGI.
DR   GO; GO:1990705; P:cholangiocyte proliferation; IMP:MGI.
DR   GO; GO:0061073; P:ciliary body morphogenesis; IMP:MGI.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
DR   GO; GO:0072104; P:glomerular capillary formation; IEP:UniProtKB.
DR   GO; GO:0072015; P:glomerular visceral epithelial cell development; IEP:UniProtKB.
DR   GO; GO:0001947; P:heart looping; IGI:BHF-UCL.
DR   GO; GO:0072574; P:hepatocyte proliferation; IMP:MGI.
DR   GO; GO:0006959; P:humoral immune response; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0002437; P:inflammatory response to antigenic stimulus; IGI:MGI.
DR   GO; GO:0072602; P:interleukin-4 secretion; IGI:MGI.
DR   GO; GO:0035622; P:intrahepatic bile duct development; IMP:MGI.
DR   GO; GO:0070986; P:left/right axis specification; IGI:BHF-UCL.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0072576; P:liver morphogenesis; IMP:MGI.
DR   GO; GO:0002315; P:marginal zone B cell differentiation; IMP:UniProtKB.
DR   GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0045967; P:negative regulation of growth rate; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; ISS:UniProtKB.
DR   GO; GO:0060674; P:placenta blood vessel development; IMP:MGI.
DR   GO; GO:0001890; P:placenta development; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:UniProtKB.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0072014; P:proximal tubule development; IEP:UniProtKB.
DR   GO; GO:0003184; P:pulmonary valve morphogenesis; ISO:MGI.
DR   GO; GO:2001204; P:regulation of osteoclast development; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0042060; P:wound healing; IDA:UniProtKB.
DR   CDD; cd00204; ANK; 2.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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_cys_sf.
DR   InterPro; IPR008297; Notch.
DR   InterPro; IPR035993; Notch-like_dom_sf.
DR   InterPro; IPR022336; Notch_2.
DR   InterPro; IPR000800; Notch_dom.
DR   InterPro; IPR010660; Notch_NOD_dom.
DR   InterPro; IPR011656; Notch_NODP_dom.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF11936; DUF3454; 1.
DR   Pfam; PF00008; EGF; 24.
DR   Pfam; PF07645; EGF_CA; 5.
DR   Pfam; PF12661; hEGF; 2.
DR   Pfam; PF06816; NOD; 1.
DR   Pfam; PF07684; NODP; 1.
DR   Pfam; PF00066; Notch; 3.
DR   PIRSF; PIRSF002279; Notch; 1.
DR   PRINTS; PR01452; LNOTCHREPEAT.
DR   PRINTS; PR01985; NOTCH2.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM01334; DUF3454; 1.
DR   SMART; SM00181; EGF; 35.
DR   SMART; SM00179; EGF_CA; 33.
DR   SMART; SM00004; NL; 3.
DR   SMART; SM01338; NOD; 1.
DR   SMART; SM01339; NODP; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF57184; SSF57184; 5.
DR   SUPFAM; SSF90193; SSF90193; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 22.
DR   PROSITE; PS00022; EGF_1; 33.
DR   PROSITE; PS01186; EGF_2; 27.
DR   PROSITE; PS50026; EGF_3; 35.
DR   PROSITE; PS01187; EGF_CA; 22.
DR   PROSITE; PS50258; LNR; 3.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; ANK repeat; Cell membrane;
KW   Complete proteome; Cytoplasm; Developmental protein; Differentiation;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Notch signaling pathway; Nucleus; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26   2473       Neurogenic locus notch homolog protein 2.
FT                                /FTId=PRO_0000007686.
FT   CHAIN      1668   2473       Notch 2 extracellular truncation.
FT                                {ECO:0000250|UniProtKB:Q01705}.
FT                                /FTId=PRO_0000007687.
FT   CHAIN      1699   2473       Notch 2 intracellular domain.
FT                                {ECO:0000305|PubMed:11459941,
FT                                ECO:0000305|PubMed:11518718}.
FT                                /FTId=PRO_0000007688.
FT   TOPO_DOM     26   1679       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1680   1700       Helical. {ECO:0000255}.
FT   TOPO_DOM   1701   2473       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       26     63       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       64    102       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      105    143       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      144    180       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      182    219       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      221    258       EGF-like 6; incomplete.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      260    296       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      298    336       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      338    374       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      375    413       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      415    454       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      456    492       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      494    530       EGF-like 13; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      532    568       EGF-like 14; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      570    605       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      607    643       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      645    680       EGF-like 17; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      682    718       EGF-like 18; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      720    755       EGF-like 19. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      757    793       EGF-like 20; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      795    831       EGF-like 21; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      833    871       EGF-like 22. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      873    909       EGF-like 23; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      911    947       EGF-like 24; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      949    985       EGF-like 25; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      987   1023       EGF-like 26; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1025   1061       EGF-like 27; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1063   1099       EGF-like 28. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1112   1147       EGF-like 29. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1149   1185       EGF-like 30; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1187   1223       EGF-like 31; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1225   1262       EGF-like 32; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1264   1302       EGF-like 33. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1304   1343       EGF-like 34. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1375   1412       EGF-like 35. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1425   1465       LNR 1.
FT   REPEAT     1466   1502       LNR 2.
FT   REPEAT     1503   1544       LNR 3.
FT   REPEAT     1828   1872       ANK 1.
FT   REPEAT     1877   1906       ANK 2.
FT   REPEAT     1910   1940       ANK 3.
FT   REPEAT     1944   1973       ANK 4.
FT   REPEAT     1977   2006       ANK 5.
FT   REPEAT     2010   2039       ANK 6.
FT   REGION     1425   1679       Negative regulatory region (NRR).
FT                                {ECO:0000250}.
FT   COMPBIAS   1647   1650       Poly-Ala.
FT   COMPBIAS   1995   1998       Poly-Leu.
FT   COMPBIAS   2186   2192       Poly-Ala.
FT   COMPBIAS   2428   2431       Poly-Ser.
FT   COMPBIAS   2448   2453       Poly-Gly.
FT   SITE        614    614       Essential for O-xylosylation.
FT                                {ECO:0000269|PubMed:21949356}.
FT   MOD_RES    1718   1718       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q04721}.
FT   MOD_RES    1780   1780       Phosphoserine.
FT                                {ECO:0000244|PubMed:19144319}.
FT   MOD_RES    1803   1803       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q04721}.
FT   MOD_RES    1805   1805       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q04721}.
FT   MOD_RES    1809   1809       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q04721}.
FT   MOD_RES    1843   1843       Phosphoserine.
FT                                {ECO:0000244|PubMed:19144319}.
FT   MOD_RES    1846   1846       Phosphoserine.
FT                                {ECO:0000244|PubMed:19144319}.
FT   MOD_RES    2071   2071       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q04721}.
FT   MOD_RES    2079   2079       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9QW30}.
FT   MOD_RES    2082   2082       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q04721}.
FT   MOD_RES    2098   2098       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q04721}.
FT   CARBOHYD     46     46       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    155    155       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    613    613       O-linked (Glc...) serine; alternate.
FT                                {ECO:0000269|PubMed:21949356}.
FT   CARBOHYD    613    613       O-linked (Xyl...) serine; alternate.
FT                                {ECO:0000269|PubMed:21949356}.
FT   CARBOHYD    733    733       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1102   1102       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1465   1465       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     28     41       {ECO:0000250}.
FT   DISULFID     35     51       {ECO:0000250}.
FT   DISULFID     53     62       {ECO:0000250}.
FT   DISULFID     68     79       {ECO:0000250}.
FT   DISULFID     73     90       {ECO:0000250}.
FT   DISULFID     92    101       {ECO:0000250}.
FT   DISULFID    109    121       {ECO:0000250}.
FT   DISULFID    115    131       {ECO:0000250}.
FT   DISULFID    133    142       {ECO:0000250}.
FT   DISULFID    148    159       {ECO:0000250}.
FT   DISULFID    153    168       {ECO:0000250}.
FT   DISULFID    170    179       {ECO:0000250}.
FT   DISULFID    186    198       {ECO:0000250}.
FT   DISULFID    192    207       {ECO:0000250}.
FT   DISULFID    209    218       {ECO:0000250}.
FT   DISULFID    230    246       {ECO:0000250}.
FT   DISULFID    248    257       {ECO:0000250}.
FT   DISULFID    264    275       {ECO:0000250}.
FT   DISULFID    269    284       {ECO:0000250}.
FT   DISULFID    286    295       {ECO:0000250}.
FT   DISULFID    302    315       {ECO:0000250}.
FT   DISULFID    309    324       {ECO:0000250}.
FT   DISULFID    326    335       {ECO:0000250}.
FT   DISULFID    342    353       {ECO:0000250}.
FT   DISULFID    347    362       {ECO:0000250}.
FT   DISULFID    364    373       {ECO:0000250}.
FT   DISULFID    379    390       {ECO:0000250}.
FT   DISULFID    384    401       {ECO:0000250}.
FT   DISULFID    403    412       {ECO:0000250}.
FT   DISULFID    419    433       {ECO:0000250}.
FT   DISULFID    427    442       {ECO:0000250}.
FT   DISULFID    444    453       {ECO:0000250}.
FT   DISULFID    460    471       {ECO:0000250}.
FT   DISULFID    465    480       {ECO:0000250}.
FT   DISULFID    482    491       {ECO:0000250}.
FT   DISULFID    498    509       {ECO:0000250}.
FT   DISULFID    503    518       {ECO:0000250}.
FT   DISULFID    520    529       {ECO:0000250}.
FT   DISULFID    536    547       {ECO:0000250}.
FT   DISULFID    541    556       {ECO:0000250}.
FT   DISULFID    558    567       {ECO:0000250}.
FT   DISULFID    574    584       {ECO:0000250}.
FT   DISULFID    579    593       {ECO:0000250}.
FT   DISULFID    595    604       {ECO:0000250}.
FT   DISULFID    611    622       {ECO:0000250}.
FT   DISULFID    616    631       {ECO:0000250}.
FT   DISULFID    633    642       {ECO:0000250}.
FT   DISULFID    649    659       {ECO:0000250}.
FT   DISULFID    654    668       {ECO:0000250}.
FT   DISULFID    670    679       {ECO:0000250}.
FT   DISULFID    686    697       {ECO:0000250}.
FT   DISULFID    691    706       {ECO:0000250}.
FT   DISULFID    708    717       {ECO:0000250}.
FT   DISULFID    724    734       {ECO:0000250}.
FT   DISULFID    729    743       {ECO:0000250}.
FT   DISULFID    745    754       {ECO:0000250}.
FT   DISULFID    761    772       {ECO:0000250}.
FT   DISULFID    766    781       {ECO:0000250}.
FT   DISULFID    783    792       {ECO:0000250}.
FT   DISULFID    799    810       {ECO:0000250}.
FT   DISULFID    804    819       {ECO:0000250}.
FT   DISULFID    821    830       {ECO:0000250}.
FT   DISULFID    837    848       {ECO:0000250}.
FT   DISULFID    842    859       {ECO:0000250}.
FT   DISULFID    861    870       {ECO:0000250}.
FT   DISULFID    877    888       {ECO:0000250}.
FT   DISULFID    882    897       {ECO:0000250}.
FT   DISULFID    899    908       {ECO:0000250}.
FT   DISULFID    915    926       {ECO:0000250}.
FT   DISULFID    920    935       {ECO:0000250}.
FT   DISULFID    937    946       {ECO:0000250}.
FT   DISULFID    953    964       {ECO:0000250}.
FT   DISULFID    958    973       {ECO:0000250}.
FT   DISULFID    975    984       {ECO:0000250}.
FT   DISULFID    991   1002       {ECO:0000250}.
FT   DISULFID    996   1011       {ECO:0000250}.
FT   DISULFID   1013   1022       {ECO:0000250}.
FT   DISULFID   1029   1040       {ECO:0000250}.
FT   DISULFID   1034   1049       {ECO:0000250}.
FT   DISULFID   1051   1060       {ECO:0000250}.
FT   DISULFID   1067   1078       {ECO:0000250}.
FT   DISULFID   1072   1087       {ECO:0000250}.
FT   DISULFID   1089   1098       {ECO:0000250}.
FT   DISULFID   1105   1126       {ECO:0000250}.
FT   DISULFID   1120   1135       {ECO:0000250}.
FT   DISULFID   1137   1146       {ECO:0000250}.
FT   DISULFID   1153   1164       {ECO:0000250}.
FT   DISULFID   1158   1173       {ECO:0000250}.
FT   DISULFID   1175   1184       {ECO:0000250}.
FT   DISULFID   1191   1202       {ECO:0000250}.
FT   DISULFID   1196   1211       {ECO:0000250}.
FT   DISULFID   1213   1222       {ECO:0000250}.
FT   DISULFID   1229   1241       {ECO:0000250}.
FT   DISULFID   1235   1250       {ECO:0000250}.
FT   DISULFID   1252   1261       {ECO:0000250}.
FT   DISULFID   1268   1281       {ECO:0000250}.
FT   DISULFID   1273   1290       {ECO:0000250}.
FT   DISULFID   1292   1301       {ECO:0000250}.
FT   DISULFID   1308   1319       {ECO:0000250}.
FT   DISULFID   1313   1331       {ECO:0000250}.
FT   DISULFID   1333   1346       {ECO:0000250}.
FT   DISULFID   1378   1389       {ECO:0000250}.
FT   DISULFID   1383   1400       {ECO:0000250}.
FT   DISULFID   1402   1411       {ECO:0000250}.
FT   DISULFID   1425   1448       {ECO:0000250}.
FT   DISULFID   1430   1443       {ECO:0000250}.
FT   DISULFID   1439   1455       {ECO:0000250}.
FT   DISULFID   1466   1489       {ECO:0000250}.
FT   DISULFID   1472   1484       {ECO:0000250}.
FT   DISULFID   1480   1496       {ECO:0000250}.
FT   DISULFID   1503   1527       {ECO:0000250}.
FT   DISULFID   1509   1522       {ECO:0000250}.
FT   DISULFID   1518   1534       {ECO:0000250}.
FT   DISULFID   1634   1641       {ECO:0000250}.
FT   VAR_SEQ    1304   1510       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_001405.
FT   MUTAGEN     614    614       S->A: No effect on O-glycosylation by
FT                                POGLUT1. Loss of O-xylosylation.
FT                                {ECO:0000269|PubMed:21949356}.
FT   MUTAGEN    1701   1701       M->L: No effect on NICD processing.
FT                                {ECO:0000269|PubMed:11459941,
FT                                ECO:0000269|PubMed:11518718}.
FT   MUTAGEN    1701   1701       M->V: Decreased NICD processing.
FT                                {ECO:0000269|PubMed:11459941,
FT                                ECO:0000269|PubMed:11518718}.
FT   CONFLICT      3      3       A -> D (in Ref. 1; BAA22094).
FT                                {ECO:0000305}.
FT   CONFLICT    210    210       P -> G (in Ref. 1; BAA22094).
FT                                {ECO:0000305}.
FT   CONFLICT    224    228       PCAPS -> RGL (in Ref. 1; BAA22094).
FT                                {ECO:0000305}.
FT   CONFLICT    244    244       F -> L (in Ref. 1; BAA22094).
FT                                {ECO:0000305}.
FT   CONFLICT   1342   1342       C -> L (in Ref. 1; BAA22094).
FT                                {ECO:0000305}.
FT   CONFLICT   1801   1801       R -> S (in Ref. 1; BAA22094).
FT                                {ECO:0000305}.
FT   CONFLICT   1904   1904       A -> R (in Ref. 1; BAA22094).
FT                                {ECO:0000305}.
FT   CONFLICT   1921   1921       A -> G (in Ref. 1; BAA22094).
FT                                {ECO:0000305}.
FT   CONFLICT   2315   2315       G -> R (in Ref. 1; BAA22094).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2473 AA;  265633 MW;  3A9067BBE3B1F480 CRC64;
     MPALRPAALR ALLWLWLCGA GPAHALQCRG GQEPCVNEGT CVTYHNGTGF CRCPEGFLGE
     YCQHRDPCEK NRCQNGGTCV PQGMLGKATC RCAPGFTGED CQYSTSHPCF VSRPCQNGGT
     CHMLSRDTYE CTCQVGFTGK QCQWTDACLS HPCENGSTCT SVASQFSCKC PAGLTGQKCE
     ADINECDIPG RCQHGGTCLN LPGSYRCQCP QGFTGQHCDS PYVPCAPSPC VNGGTCRQTG
     DFTFECNCLP GFEGSTCERN IDDCPNHKCQ NGGVCVDGVN TYNCRCPPQW TGQFCTEDVD
     ECLLQPNACQ NGGTCTNRNG GYGCVCVNGW SGDDCSENID DCAYASCTPG STCIDRVASF
     SCLCPEGKAG LLCHLDDACI SNPCHKGALC DTNPLNGQYI CTCPQGYKGA DCTEDVDECA
     MANSNPCEHA GKCVNTDGAF HCECLKGYAG PRCEMDINEC HSDPCQNDAT CLDKIGGFTC
     LCMPGFKGVH CELEVNECQS NPCVNNGQCV DKVNRFQCLC PPGFTGPVCQ IDIDDCSSTP
     CLNGAKCIDH PNGYECQCAT GFTGILCDEN IDNCDPDPCH HGQCQDGIDS YTCICNPGYM
     GAICSDQIDE CYSSPCLNDG RCIDLVNGYQ CNCQPGTSGL NCEINFDDCA SNPCMHGVCV
     DGINRYSCVC SPGFTGQRCN IDIDECASNP CRKGATCIND VNGFRCICPE GPHHPSCYSQ
     VNECLSNPCI HGNCTGGLSG YKCLCDAGWV GVNCEVDKNE CLSNPCQNGG TCNNLVNGYR
     CTCKKGFKGY NCQVNIDECA SNPCLNQGTC FDDVSGYTCH CMLPYTGKNC QTVLAPCSPN
     PCENAAVCKE APNFESFSCL CAPGWQGKRC TVDVDECISK PCMNNGVCHN TQGSYVCECP
     PGFSGMDCEE DINDCLANPC QNGGSCVDHV NTFSCQCHPG FIGDKCQTDM NECLSEPCKN
     GGTCSDYVNS YTCTCPAGFH GVHCENNIDE CTESSCFNGG TCVDGINSFS CLCPVGFTGP
     FCLHDINECS SNPCLNAGTC VDGLGTYRCI CPLGYTGKNC QTLVNLCSRS PCKNKGTCVQ
     EKARPHCLCP PGWDGAYCDV LNVSCKAAAL QKGVPVEHLC QHSGICINAG NTHHCQCPLG
     YTGSYCEEQL DECASNPCQH GATCNDFIGG YRCECVPGYQ GVNCEYEVDE CQNQPCQNGG
     TCIDLVNHFK CSCPPGTRGL LCEENIDECA GGPHCLNGGQ CVDRIGGYTC RCLPGFAGER
     CEGDINECLS NPCSSEGSLD CVQLKNNYNC ICRSAFTGRH CETFLDVCPQ KPCLNGGTCA
     VASNMPDGFI CRCPPGFSGA RCQSSCGQVK CRRGEQCIHT DSGPRCFCLN PKDCESGCAS
     NPCQHGGTCY PQRQPPHYSC RCPPSFGGSH CELYTAPTST PPATCQSQYC ADKARDGICD
     EACNSHACQW DGGDCSLTME DPWANCTSTL RCWEYINNQC DEQCNTAECL FDNFECQRNS
     KTCKYDKYCA DHFKDNHCDQ GCNSEECGWD GLDCASDQPE NLAEGTLIIV VLLPPEQLLQ
     DSRSFLRALG TLLHTNLRIK QDSQGALMVY PYFGEKSAAM KKQKMTRRSL PEEQEQEQEV
     IGSKIFLEID NRQCVQDSDQ CFKNTDAAAA LLASHAIQGT LSYPLVSVFS ELESPRNAQL
     LYLLAVAVVI ILFFILLGVI MAKRKRKHGF LWLPEGFTLR RDSSNHKRRE PVGQDAVGLK
     NLSVQVSEAN LIGSGTSEHW VDDEGPQPKK AKAEDEALLS EDDPIDRRPW TQQHLEAADI
     RHTPSLALTP PQAEQEVDVL DVNVRGPDGC TPLMLASLRG GSSDLSDEDE DAEDSSANII
     TDLVYQGASL QAQTDRTGEM ALHLAARYSR ADAAKRLLDA GADANAQDNM GRCPLHAAVA
     ADAQGVFQIL IRNRVTDLDA RMNDGTTPLI LAARLAVEGM VAELINCQAD VNAVDDHGKS
     ALHWAAAVNN VEATLLLLKN GANRDMQDNK EETPLFLAAR EGSYEAAKIL LDHFANRDIT
     DHMDRLPRDV ARDRMHHDIV RLLDEYNVTP SPPGTVLTSA LSPVLCGPNR SFLSLKHTPM
     GKKARRPNTK STMPTSLPNL AKEAKDAKGS RRKKCLNEKV QLSESSVTLS PVDSLESPHT
     YVSDATSSPM ITSPGILQAS PTPLLAAAAP AAPVHTQHAL SFSNLHDMQP LAPGASTVLP
     SVSQLLSHHH IAPPGSSSAG SLGRLHPVPV PADWMNRVEM NETQYSEMFG MVLAPAEGAH
     PGIAAPQSRP PEGKHMSTQR EPLPPIVTFQ LIPKGSIAQA AGAPQTQSSC PPAVAGPLPS
     MYQIPEMPRL PSVAFPPTMM PQQEGQVAQT IVPTYHPFPA SVGKYPTPPS QHSYASSNAA
     ERTPSHGGHL QGEHPYLTPS PESPDQWSSS SPHSASDWSD VTTSPTPGGG GGGQRGPGTH
     MSEPPHSNMQ VYA
//
DBGET integrated database retrieval system