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DNER_HUMAN
ID   DNER_HUMAN              Reviewed;         737 AA.
AC   Q8NFT8; A6NP39; Q53R88; Q53TP7; Q53TQ5; Q8IYT0; Q8TB42; Q9NTF1; Q9UDM2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Delta and Notch-like epidermal growth factor-related receptor;
DE   Flags: Precursor;
GN   Name=DNER; Synonyms=BET; ORFNames=UNQ262/PRO299;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   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 [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-433.
RC   TISSUE=Brain;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-737.
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   TISSUE SPECIFICITY.
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   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-223.
RC   TISSUE=Saliva;
RX   PubMed=16740002; DOI=10.1021/pr050492k;
RA   Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT   "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT   capture and mass spectrometry.";
RL   J. Proteome Res. 5:1493-1503(2006).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC   -!- FUNCTION: Activator of the NOTCH1 pathway. May mediate neuron-glia
CC       interaction during astrocytogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with AP1G1. Interacts with NOTCH1 (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8NFT8; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-2682727, EBI-350517;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Note=Present on the membrane of dendrites and cell bodies but
CC       excluded from axonal membrane. Also found in early endosomes in the
CC       somatodendritic region (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, spinal cord and adrenal gland.
CC       {ECO:0000269|PubMed:11997712}.
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DR   EMBL; AF442487; AAM21557.1; -; mRNA.
DR   EMBL; AY358891; AAQ89250.1; -; mRNA.
DR   EMBL; AC007559; AAY14939.1; -; Genomic_DNA.
DR   EMBL; AC007748; AAY24263.1; -; Genomic_DNA.
DR   EMBL; AC008273; AAF19247.2; -; Genomic_DNA.
DR   EMBL; AC093384; AAY14680.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70893.1; -; Genomic_DNA.
DR   EMBL; BC024766; AAH24766.2; -; mRNA.
DR   EMBL; BC035009; AAH35009.1; -; mRNA.
DR   EMBL; AL137311; CAB70690.1; -; mRNA.
DR   CCDS; CCDS33390.1; -.
DR   PIR; T46247; T46247.
DR   RefSeq; NP_620711.3; NM_139072.3.
DR   AlphaFoldDB; Q8NFT8; -.
DR   SMR; Q8NFT8; -.
DR   BioGRID; 124973; 2.
DR   DIP; DIP-46249N; -.
DR   IntAct; Q8NFT8; 4.
DR   STRING; 9606.ENSP00000345229; -.
DR   GlyGen; Q8NFT8; 3 sites.
DR   iPTMnet; Q8NFT8; -.
DR   PhosphoSitePlus; Q8NFT8; -.
DR   BioMuta; DNER; -.
DR   DMDM; 74730301; -.
DR   EPD; Q8NFT8; -.
DR   jPOST; Q8NFT8; -.
DR   MassIVE; Q8NFT8; -.
DR   MaxQB; Q8NFT8; -.
DR   PaxDb; Q8NFT8; -.
DR   PeptideAtlas; Q8NFT8; -.
DR   PRIDE; Q8NFT8; -.
DR   ProteomicsDB; 73354; -.
DR   Antibodypedia; 2715; 232 antibodies from 30 providers.
DR   DNASU; 92737; -.
DR   Ensembl; ENST00000341772.5; ENSP00000345229.4; ENSG00000187957.8.
DR   GeneID; 92737; -.
DR   KEGG; hsa:92737; -.
DR   MANE-Select; ENST00000341772.5; ENSP00000345229.4; NM_139072.4; NP_620711.3.
DR   UCSC; uc002vpv.4; human.
DR   CTD; 92737; -.
DR   DisGeNET; 92737; -.
DR   GeneCards; DNER; -.
DR   HGNC; HGNC:24456; DNER.
DR   HPA; ENSG00000187957; Tissue enhanced (adrenal gland, brain, choroid plexus).
DR   MIM; 607299; gene.
DR   neXtProt; NX_Q8NFT8; -.
DR   OpenTargets; ENSG00000187957; -.
DR   PharmGKB; PA162383959; -.
DR   VEuPathDB; HostDB:ENSG00000187957; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   GeneTree; ENSGT00940000158872; -.
DR   HOGENOM; CLU_019513_0_0_1; -.
DR   InParanoid; Q8NFT8; -.
DR   OMA; LNGFTCQ; -.
DR   OrthoDB; 7525at2759; -.
DR   PhylomeDB; Q8NFT8; -.
DR   TreeFam; TF351322; -.
DR   PathwayCommons; Q8NFT8; -.
DR   Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   SignaLink; Q8NFT8; -.
DR   SIGNOR; Q8NFT8; -.
DR   BioGRID-ORCS; 92737; 9 hits in 1071 CRISPR screens.
DR   ChiTaRS; DNER; human.
DR   GeneWiki; DNER; -.
DR   GenomeRNAi; 92737; -.
DR   Pharos; Q8NFT8; Tbio.
DR   PRO; PR:Q8NFT8; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q8NFT8; protein.
DR   Bgee; ENSG00000187957; Expressed in lateral nuclear group of thalamus and 148 other tissues.
DR   Genevisible; Q8NFT8; HS.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR   GO; GO:0030276; F:clathrin binding; TAS:UniProtKB.
DR   GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; IEP:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR   GO; GO:0010001; P:glial cell differentiation; IEA:Ensembl.
DR   GO; GO:0001764; P:neuron migration; NAS:UniProtKB.
DR   GO; GO:0007220; P:Notch receptor processing; IEA:Ensembl.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR   GO; GO:0007416; P:synapse assembly; NAS:UniProtKB.
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; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Notch signaling pathway; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..737
FT                   /note="Delta and Notch-like epidermal growth factor-related
FT                   receptor"
FT                   /id="PRO_0000253557"
FT   TOPO_DOM        35..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          546..568
FT                   /note="Follistatin-like"
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:0000250"
FT   REGION          677..680
FT                   /note="Interaction with AP1G1 and somatodendritic
FT                   targeting"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         685
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JZM4"
FT   MOD_RES         711
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JZM4"
FT   MOD_RES         721
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JZM4"
FT   MOD_RES         722
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JZM4"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16740002"
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   VARIANT         433
FT                   /note="P -> L (in dbSNP:rs17853365)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_028380"
SQ   SEQUENCE   737 AA;  78475 MW;  25A8A8A3044308BE CRC64;
     MQPRRAQAPG AQLLPALALL LLLLGAGPRG SSLANPVPAA PLSAPGPCAA QPCRNGGVCT
     SRPEPDPQHP APAGEPGYSC TCPAGISGAN CQLVADPCAS NPCHHGNCSS SSSSSSDGYL
     CICNEGYEGP NCEQALPSLP ATGWTESMAP RQLQPVPATQ EPDKILPRSQ ATVTLPTWQP
     KTGQKVVEMK WDQVEVIPDI ACGNASSNSS AGGRLVSFEV PQNTSVKIRQ DATASLILLW
     KVTATGFQQC SLIDGRSVTP LQASGGLVLL EEMLALGNNH FIGFVNDSVT KSIVALRLTL
     VVKVSTCVPG ESHANDLECS GKGKCTTKPS EATFSCTCEE QYVGTFCEEY DACQRKPCQN
     NASCIDANEK QDGSNFTCVC LPGYTGELCQ SKIDYCILDP CRNGATCISS LSGFTCQCPE
     GYFGSACEEK VDPCASSPCQ NNGTCYVDGV HFTCNCSPGF TGPTCAQLID FCALSPCAHG
     TCRSVGTSYK CLCDPGYHGL YCEEEYNECL SAPCLNAATC RDLVNGYECV CLAEYKGTHC
     ELYKDPCANV SCLNGATCDS DGLNGTCICA PGFTGEECDI DINECDSNPC HHGGSCLDQP
     NGYNCHCPHG WVGANCEIHL QWKSGHMAES LTNMPRHSLY IIIGALCVAF ILMLIILIVG
     ICRISRIEYQ GSSRPAYEEF YNCRSIDSEF SNAIASIRHA RFGKKSRPAM YDVSPIAYED
     YSPDDKPLVT LIKTKDL
 
 
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