DNER_MOUSE
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 03-AUG-2022, entry version 157.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 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 novel
RT EGF-like repeat-containing protein targeted to dendrites of developing and
RT 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., 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 [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 project:
RT 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 SER-722, 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).
CC -!- FUNCTION: Mediates neuron-glia interaction during astrocytogenesis. May
CC promote differentiation of Bergmann glia during cerebellar development
CC by activating DELTEX-dependent NOTCH1 signaling.
CC {ECO:0000269|PubMed:15965470, 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 excluded
CC from axonal membrane. Also found in early endosomes in the
CC somatodendritic region.
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain neurons (at protein
CC level). {ECO:0000269|PubMed:11950833, ECO:0000269|PubMed:11997712}.
CC -!- DEVELOPMENTAL STAGE: Expression in the central nervous system starts at
CC 11 dpc, peaks during postnatal development and declines in the adult
CC brain. At P7 and P20, present in several types of post-mitotic neurons,
CC including cortical and hippocampal pyramidal neurons, cerebellar
CC granule cells and Purkinje cells. Absent from mitotic neuroblasts in
CC the ventricular zones. {ECO:0000269|PubMed:11950833,
CC ECO:0000269|PubMed:11997712}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11997712}.
CC -!- DISRUPTION PHENOTYPE: Mice show no obvious abnormality and no apparent
CC survival disadvantage. However, they have delayed cerebellar
CC histogenesis and exhibit motor discoordination at adult stages.
CC {ECO:0000269|PubMed:16298139}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE31470.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE31828.1; Type=Frameshift; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q8JZM4; -.
DR SMR; Q8JZM4; -.
DR BioGRID; 230612; 1.
DR STRING; 10090.ENSMUSP00000042927; -.
DR GlyConnect; 2251; 4 N-Linked glycans (2 sites).
DR GlyGen; Q8JZM4; 4 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q8JZM4; -.
DR PhosphoSitePlus; Q8JZM4; -.
DR MaxQB; Q8JZM4; -.
DR PaxDb; Q8JZM4; -.
DR PeptideAtlas; Q8JZM4; -.
DR PRIDE; Q8JZM4; -.
DR ProteomicsDB; 279740; -.
DR Antibodypedia; 2715; 232 antibodies from 30 providers.
DR DNASU; 227325; -.
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 VEuPathDB; HostDB:ENSMUSG00000036766; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000158872; -.
DR HOGENOM; CLU_019513_0_0_1; -.
DR InParanoid; Q8JZM4; -.
DR OMA; YKCTELS; -.
DR OrthoDB; 7525at2759; -.
DR PhylomeDB; Q8JZM4; -.
DR TreeFam; TF351322; -.
DR BioGRID-ORCS; 227325; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dner; mouse.
DR PRO; PR:Q8JZM4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8JZM4; protein.
DR Bgee; ENSMUSG00000036766; Expressed in cerebellum lobe and 199 other tissues.
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; IPR045769; DNER_C.
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; PF19330; DNER_C; 1.
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; Developmental protein; Differentiation;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Notch signaling pathway; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..737
FT /note="Delta and Notch-like epidermal growth factor-related
FT receptor"
FT /id="PRO_0000253558"
FT TOPO_DOM 26..640
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..737
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 44..92
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 94..133
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 309..348
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 349..390
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 392..428
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 430..466
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 468..503
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 505..541
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 543..579
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 581..617
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 44..133
FT /note="Interaction with NOTCH1"
FT /evidence="ECO:0000269|PubMed:15965470"
FT REGION 677..680
FT /note="Interaction with AP1G1 and somatodendritic
FT targeting"
FT /evidence="ECO:0000269|PubMed:11950833"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 711
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 714
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 721
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 53..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 82..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 98..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 103..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 123..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 319..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 338..347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 353..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 358..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 380..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 396..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 401..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 418..427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 434..445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 439..454
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 456..465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 472..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 477..491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 493..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 509..520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 514..529
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 531..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 547..558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 552..567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 569..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 585..596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 590..605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 607..616
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 677
FT /note="Y->A: Fails to be restricted to the somatodendritic
FT compartment."
FT /evidence="ECO:0000269|PubMed:11950833"
FT CONFLICT 424
FT /note="G -> A (in Ref. 2; BAB72175)"
FT /evidence="ECO:0000305"
FT CONFLICT 509..510
FT /note="CL -> SV (in Ref. 1; AAM14419)"
FT /evidence="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
