GenomeNet

Database: UniProt
Entry: Q8JZM4
LinkDB: Q8JZM4
Original site: Q8JZM4 
ID   DNER_MOUSE              Reviewed;         737 AA.
AC   Q8JZM4; Q3U697; Q8R226; Q8R4T6; Q8VD97;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   13-FEB-2019, entry version 140.
DE   RecName: Full=Delta and Notch-like epidermal growth factor-related receptor;
DE   AltName: Full=Brain EGF repeat-containing transmembrane protein;
DE   Flags: Precursor;
GN   Name=Dner; Synonyms=Bet, Bret;
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-677, AND INTERACTION WITH
RP   AP1G1.
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=11950833; DOI=10.1074/jbc.M110793200;
RA   Eiraku M., Hirata Y., Takeshima H., Hirano T., Kengaku M.;
RT   "Delta/notch-like epidermal growth factor (EGF)-related receptor, a
RT   novel EGF-like repeat-containing protein targeted to dendrites of
RT   developing and adult central nervous system neurons.";
RL   J. Biol. Chem. 277:25400-25407(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=11997712; DOI=10.1097/00001756-200205070-00035;
RA   Nishizumi H., Komiyama T., Miyabayashi T., Sakano S., Sakano H.;
RT   "BET, a novel neuronal transmembrane protein with multiple EGF-like
RT   motifs.";
RL   NeuroReport 13:909-915(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Retina;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH NOTCH1, AND FUNCTION.
RX   PubMed=15965470; DOI=10.1038/nn1492;
RA   Eiraku M., Tohgo A., Ono K., Kaneko M., Fujishima K., Hirano T.,
RA   Kengaku M.;
RT   "DNER acts as a neuron-specific Notch ligand during Bergmann glial
RT   development.";
RL   Nat. Neurosci. 8:873-880(2005).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16298139; DOI=10.1016/j.mcn.2005.10.003;
RA   Tohgo A., Eiraku M., Miyazaki T., Miura E., Kawaguchi S.Y., Nishi M.,
RA   Watanabe M., Hirano T., Kengaku M., Takeshima H.;
RT   "Impaired cerebellar functions in mutant mice lacking DNER.";
RL   Mol. Cell. Neurosci. 31:326-333(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-711 AND TYR-721, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685; THR-714 AND
RP   SER-722, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Mediates neuron-glia interaction during
CC       astrocytogenesis. May promote differentiation of Bergmann glia
CC       during cerebellar development by activating DELTEX-dependent
CC       NOTCH1 signaling. {ECO:0000269|PubMed:15965470,
CC       ECO:0000269|PubMed:16298139}.
CC   -!- SUBUNIT: Interacts with AP1G1. Interacts with NOTCH1.
CC       {ECO:0000269|PubMed:11950833, ECO:0000269|PubMed:15965470}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11950833,
CC       ECO:0000269|PubMed:11997712}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:11950833, ECO:0000269|PubMed:11997712}.
CC       Note=Present on the membrane of dendrites and cell bodies but
CC       excluded from axonal membrane. Also found in early endosomes in
CC       the somatodendritic region.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in brain neurons (at
CC       protein level). {ECO:0000269|PubMed:11950833,
CC       ECO:0000269|PubMed:11997712}.
CC   -!- DEVELOPMENTAL STAGE: Expression in the central nervous system
CC       starts at 11 dpc, peaks during postnatal development and declines
CC       in the adult brain. At P7 and P20, present in several types of
CC       post-mitotic neurons, including cortical and hippocampal pyramidal
CC       neurons, cerebellar granule cells and Purkinje cells. Absent from
CC       mitotic neuroblasts in the ventricular zones.
CC       {ECO:0000269|PubMed:11950833, ECO:0000269|PubMed:11997712}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11997712}.
CC   -!- DISRUPTION PHENOTYPE: Mice show no obvious abnormality and no
CC       apparent survival disadvantage. However, they have delayed
CC       cerebellar histogenesis and exhibit motor discoordination at adult
CC       stages. {ECO:0000269|PubMed:16298139}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE31470.1; Type=Frameshift; Positions=631; Evidence={ECO:0000305};
CC       Sequence=BAE31828.1; Type=Frameshift; Positions=631; Evidence={ECO:0000305};
DR   EMBL; AY032924; AAK50342.1; -; mRNA.
DR   EMBL; AF370126; AAM14419.1; -; mRNA.
DR   EMBL; AB067650; BAB72175.1; -; mRNA.
DR   EMBL; AK044597; BAC31995.1; -; mRNA.
DR   EMBL; AK152755; BAE31470.1; ALT_FRAME; mRNA.
DR   EMBL; AK153235; BAE31828.1; ALT_FRAME; mRNA.
DR   EMBL; BC022636; AAH22636.1; -; mRNA.
DR   EMBL; BC034634; AAH34634.1; -; mRNA.
DR   CCDS; CCDS15105.1; -.
DR   RefSeq; NP_690879.1; NM_152915.1.
DR   UniGene; Mm.292560; -.
DR   ProteinModelPortal; Q8JZM4; -.
DR   SMR; Q8JZM4; -.
DR   BioGrid; 230612; 1.
DR   STRING; 10090.ENSMUSP00000042927; -.
DR   iPTMnet; Q8JZM4; -.
DR   PhosphoSitePlus; Q8JZM4; -.
DR   MaxQB; Q8JZM4; -.
DR   PaxDb; Q8JZM4; -.
DR   PeptideAtlas; Q8JZM4; -.
DR   PRIDE; Q8JZM4; -.
DR   Ensembl; ENSMUST00000049126; ENSMUSP00000042927; ENSMUSG00000036766.
DR   GeneID; 227325; -.
DR   KEGG; mmu:227325; -.
DR   UCSC; uc007bsw.1; mouse.
DR   CTD; 92737; -.
DR   MGI; MGI:2152889; Dner.
DR   eggNOG; ENOG410IR71; Eukaryota.
DR   eggNOG; ENOG410ZUAK; LUCA.
DR   GeneTree; ENSGT00940000158872; -.
DR   HOGENOM; HOG000112241; -.
DR   HOVERGEN; HBG060866; -.
DR   InParanoid; Q8JZM4; -.
DR   OMA; CESYKDP; -.
DR   OrthoDB; 243316at2759; -.
DR   PhylomeDB; Q8JZM4; -.
DR   TreeFam; TF351322; -.
DR   ChiTaRS; Dner; mouse.
DR   PRO; PR:Q8JZM4; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000036766; Expressed in 233 organ(s), highest expression level in cerebellum lobe.
DR   ExpressionAtlas; Q8JZM4; baseline and differential.
DR   Genevisible; Q8JZM4; MM.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005112; F:Notch binding; IPI:MGI.
DR   GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR   GO; GO:0010001; P:glial cell differentiation; IDA:MGI.
DR   GO; GO:0007220; P:Notch receptor processing; IDA:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IDA:MGI.
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   Pfam; PF00008; EGF; 6.
DR   Pfam; PF12661; hEGF; 1.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00179; EGF_CA; 7.
DR   SUPFAM; SSF57184; SSF57184; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00022; EGF_1; 10.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 10.
DR   PROSITE; PS01187; EGF_CA; 2.
PE   1: Evidence at protein level;
KW   Activator; Calcium; Cell membrane; Complete proteome;
KW   Developmental protein; Differentiation; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Notch signaling pathway;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26    737       Delta and Notch-like epidermal growth
FT                                factor-related receptor.
FT                                /FTId=PRO_0000253558.
FT   TOPO_DOM     26    640       Extracellular. {ECO:0000255}.
FT   TRANSMEM    641    661       Helical. {ECO:0000255}.
FT   TOPO_DOM    662    737       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       44     92       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       94    133       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      309    348       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      349    390       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      392    428       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      430    466       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      468    503       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      505    541       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      543    579       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      581    617       EGF-like 10; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REGION       44    133       Interaction with NOTCH1.
FT                                {ECO:0000269|PubMed:15965470}.
FT   REGION      677    680       Interaction with AP1G1 and
FT                                somatodendritic targeting.
FT                                {ECO:0000269|PubMed:11950833}.
FT   MOD_RES     685    685       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     711    711       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:18034455}.
FT   MOD_RES     714    714       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     721    721       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:18034455}.
FT   MOD_RES     722    722       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD    204    204       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    564    564       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     48     59       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     53     80       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     82     91       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     98    108       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    103    121       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    123    132       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    319    336       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    338    347       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    353    364       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    358    378       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    380    389       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    396    407       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    401    416       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    418    427       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    434    445       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    439    454       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    456    465       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    472    482       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    477    491       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    493    502       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    509    520       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    514    529       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    531    540       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    547    558       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    552    567       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    569    578       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    585    596       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    590    605       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    607    616       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   MUTAGEN     677    677       Y->A: Fails to be restricted to the
FT                                somatodendritic compartment.
FT                                {ECO:0000269|PubMed:11950833}.
FT   CONFLICT    424    424       G -> A (in Ref. 2; BAB72175).
FT                                {ECO:0000305}.
FT   CONFLICT    509    510       CL -> SV (in Ref. 1; AAM14419).
FT                                {ECO:0000305}.
SQ   SEQUENCE   737 AA;  78747 MW;  8C85694EB7420756 CRC64;
     MPPRRAQAPG APLLPVLALL PLLLGAGPQS GCLASPVSAA PLPAPGPCAS QPCRNGGVCT
     PRSVTDQEHP AADAEPRYSC TCPAGVSGTY CQFVADPCAS NPCHHGNCSS SSSSSSDSYL
     CICNDGYEGL NCEQPLPSIP TSGWTESTAP RQLQPVPATQ EPDIILPRSQ ATVTLPTWQP
     KTGQKVVEMK WDQVEVVPDV ACGNASSNNS AGGRLVSFEV PQNTSVKIRQ DANSLLILLW
     KVTATGFQQC SLIDGRSVTP LQAPGGLVLL EEMLALGPNH FIGFVNDSVA KSIVALRLTL
     VVKASNCVPG DSHSNDLECS GKGKCATKPS EATFSCTCQD QYIGTFCEEF DACQRKPCQN
     EASCIDANEK QDGSNFTCLC LPGYTGELCQ SKIDYCVLDP CRNGATCVSS LSGFTCQCLE
     GYFGSACEEK VDPCMSSPCQ NNGTCYVDGV HFTCSCSPGF TGPTCAQLVD FCALSPCAHG
     MCRSVGTSYK CLCDPGYHGL YCEEEYNECL SAPCLNAATC RDLINGYECV CLAEYKGTHC
     ELYKDPCANI SCLNGGTCDS EGLNGTCICA PGFTGEECDI DINECDSNPC HHAGTCLDQP
     NGYTCHCPHG WVGANCEIHL QWKSGHMAES LTNMPRHSLY IIIGALCVAF ILMLIILIVG
     ICRISRIEYQ GSSRPAYEEF YNCRSIDSEF SNAIASIRHA RFGKKSRPAM YDVTPIAYED
     YSPDDKPLVT LIKTKDL
//
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