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NECT1_MOUSE
ID   NECT1_MOUSE             Reviewed;         515 AA.
AC   Q9JKF6; Q6P9M9; Q9ERL5; Q9JI17;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=Nectin-1;
DE   AltName: Full=Herpes virus entry mediator C;
DE            Short=Herpesvirus entry mediator C;
DE            Short=HveC;
DE   AltName: Full=Nectin cell adhesion molecule 1 {ECO:0000250|UniProtKB:Q15223};
DE   AltName: Full=Poliovirus receptor-related protein 1;
DE   AltName: CD_antigen=CD111;
DE   Flags: Precursor;
GN   Name=Nectin1 {ECO:0000250|UniProtKB:Q15223}; Synonyms=Hvec, Prr1, Pvrl1;
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].
RX   PubMed=10781093; DOI=10.1073/pnas.97.9.4867;
RA   Menotti L., Lopez M., Avitabile E., Stefan A., Cocchi F., Adelaide J.,
RA   Lecocq E., Dubreuil P., Campadelli-Fiume G.;
RT   "The murine homolog of human nectin1 delta serves as a species nonspecific
RT   mediator for entry of human and animal alpha herpesviruses in a pathway
RT   independent of detectable binding to gD.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:4867-4872(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11090177; DOI=10.1128/jvi.74.24.11773-11781.2000;
RA   Shukla D., Dal Canto M.C., Rowe C.L., Spear P.G.;
RT   "Striking similarity of murine nectin-1alpha to human nectin-1alpha (HveC)
RT   in sequence and activity as a glycoprotein D receptor for alphaherpesvirus
RT   entry.";
RL   J. Virol. 74:11773-11781(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster;
RA   Zhan J., Wimmer E.;
RT   "Mouse nectin-1 (mPRR1), a herpesvirus receptor, is expressed in the floor
RT   plate during embryogenesis, suggesting a role in neural development.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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   [5]
RP   INTERACTION WITH NECTIN3.
RX   PubMed=10744716; DOI=10.1074/jbc.275.14.10291;
RA   Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M., Nishimura M.,
RA   Tachibana K., Mizoguchi A., Takai Y.;
RT   "Nectin-3: a new member of immunoglobulin-like cell adhesion molecules that
RT   shows homophilic and heterophilic cell-cell adhesion activities.";
RL   J. Biol. Chem. 275:10291-10299(2000).
RN   [6]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=11827984; DOI=10.1083/jcb.200103113;
RA   Mizoguchi A., Nakanishi H., Kimura K., Matsubara K., Ozaki-Kuroda K.,
RA   Katata T., Honda T., Kiyohara Y., Heo K., Higashi M., Tsutsumi T.,
RA   Sonoda S., Ide C., Takai Y.;
RT   "Nectin: an adhesion molecule involved in formation of synapses.";
RL   J. Cell Biol. 156:555-565(2002).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-434, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE 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   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202 AND ASN-286.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202; ASN-286 AND ASN-332.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421; SER-433; TYR-435 AND
RP   SER-509, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Lung;
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).
RN   [13]
RP   STRUCTURE BY NMR OF 241-334, FUNCTION, SUBUNIT, IG-LIKE DOMAIN, AND
RP   DISULFIDE BOND.
RX   PubMed=22955284; DOI=10.1074/jbc.m112.345215;
RA   Bojesen K.B., Clausen O., Rohde K., Christensen C., Zhang L., Li S.,
RA   Kohler L., Nielbo S., Nielsen J., Gjorlund M.D., Poulsen F.M., Bock E.,
RA   Berezin V.;
RT   "Nectin-1 binds and signals through the fibroblast growth factor
RT   receptor.";
RL   J. Biol. Chem. 287:37420-37433(2012).
CC   -!- FUNCTION: Involved in cell adhesion and synaptogegesis. Has some
CC       neurite outgrowth-promoting activity. Receptor for alphaherpesvirus
CC       (HSV-1, HSV-2 and pseudorabies virus) entry into cells.
CC       {ECO:0000269|PubMed:11827984, ECO:0000269|PubMed:22955284}.
CC   -!- SUBUNIT: Cis- and trans-homodimer. Can form trans-heterodimers with
CC       NECTIN3. Interaction between NECTIN1 and NECTIN3 on the pre- and
CC       postsynaptic sites, respectively, initiates the formation of puncta
CC       adherentia junctions between axons and dendrites. Interacts (via Ig-
CC       like C2-type domain 2) with FGFR1, FGFR2 and FGFR3. Interacts (via
CC       Cytoplasmic domain) with AFDN, providing a connection with the actin
CC       cytoskeleton. Interacts with HSV glycoprotein D (gD).
CC       {ECO:0000269|PubMed:10744716, ECO:0000269|PubMed:11827984,
CC       ECO:0000269|PubMed:22955284}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11827984};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:11827984}.
CC       Presynaptic cell membrane {ECO:0000269|PubMed:11827984}.
CC   -!- DOMAIN: Ig-like C2-type 2 mediates neurite outgrowth through binding,
CC       induction of phosphorylation, and activation of FGFR.
CC   -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR   EMBL; AF239762; AAF60333.1; -; mRNA.
DR   EMBL; AF270977; AAF76195.1; -; mRNA.
DR   EMBL; AF297665; AAG22808.1; -; mRNA.
DR   EMBL; BC060694; AAH60694.1; -; mRNA.
DR   CCDS; CCDS23092.1; -.
DR   RefSeq; NP_067399.2; NM_021424.2.
DR   PDB; 2L7J; NMR; -; A=241-334.
DR   PDB; 5B21; X-ray; 2.24 A; A/B=31-144.
DR   PDBsum; 2L7J; -.
DR   PDBsum; 5B21; -.
DR   AlphaFoldDB; Q9JKF6; -.
DR   BMRB; Q9JKF6; -.
DR   SMR; Q9JKF6; -.
DR   BioGRID; 208408; 1.
DR   DIP; DIP-41728N; -.
DR   MINT; Q9JKF6; -.
DR   STRING; 10090.ENSMUSP00000034510; -.
DR   GlyConnect; 2528; 15 N-Linked glycans (1 site).
DR   GlyGen; Q9JKF6; 7 sites, 15 N-linked glycans (1 site).
DR   iPTMnet; Q9JKF6; -.
DR   PhosphoSitePlus; Q9JKF6; -.
DR   CPTAC; non-CPTAC-3660; -.
DR   jPOST; Q9JKF6; -.
DR   MaxQB; Q9JKF6; -.
DR   PaxDb; Q9JKF6; -.
DR   PeptideAtlas; Q9JKF6; -.
DR   PRIDE; Q9JKF6; -.
DR   ProteomicsDB; 252802; -.
DR   Antibodypedia; 4247; 439 antibodies from 38 providers.
DR   DNASU; 58235; -.
DR   Ensembl; ENSMUST00000034510; ENSMUSP00000034510; ENSMUSG00000032012.
DR   GeneID; 58235; -.
DR   KEGG; mmu:58235; -.
DR   UCSC; uc009pbj.1; mouse.
DR   CTD; 5818; -.
DR   MGI; MGI:1926483; Nectin1.
DR   VEuPathDB; HostDB:ENSMUSG00000032012; -.
DR   eggNOG; ENOG502QVRJ; Eukaryota.
DR   GeneTree; ENSGT00940000156933; -.
DR   HOGENOM; CLU_029618_3_1_1; -.
DR   InParanoid; Q9JKF6; -.
DR   OrthoDB; 509401at2759; -.
DR   PhylomeDB; Q9JKF6; -.
DR   TreeFam; TF331051; -.
DR   Reactome; R-MMU-418990; Adherens junctions interactions.
DR   Reactome; R-MMU-420597; Nectin/Necl trans heterodimerization.
DR   BioGRID-ORCS; 58235; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Nectin1; mouse.
DR   PRO; PR:Q9JKF6; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9JKF6; protein.
DR   Bgee; ENSMUSG00000032012; Expressed in lip and 140 other tissues.
DR   ExpressionAtlas; Q9JKF6; baseline and differential.
DR   Genevisible; Q9JKF6; MM.
DR   GO; GO:0005912; C:adherens junction; IDA:MGI.
DR   GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0044291; C:cell-cell contact zone; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0032584; C:growth cone membrane; ISO:MGI.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR   GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR   GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR   GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC-UCL.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR   GO; GO:0046790; F:virion binding; ISO:MGI.
DR   GO; GO:0007411; P:axon guidance; ISO:MGI.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR   GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR   GO; GO:0002934; P:desmosome organization; IMP:MGI.
DR   GO; GO:0070166; P:enamel mineralization; IMP:MGI.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:HGNC-UCL.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:HGNC-UCL.
DR   GO; GO:0006826; P:iron ion transport; IMP:MGI.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:1902414; P:protein localization to cell junction; IDA:MGI.
DR   GO; GO:0051963; P:regulation of synapse assembly; ISO:MGI.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:InterPro.
DR   CDD; cd05886; Ig1_Nectin-1_like; 1.
DR   CDD; cd05890; Ig2_Nectin-1_like; 1.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR041849; Nectin-1_Ig1.
DR   InterPro; IPR041850; Nectin-1_Ig2.
DR   InterPro; IPR033314; Nectin1.
DR   PANTHER; PTHR23277:SF69; PTHR23277:SF69; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF13895; Ig_2; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Cell membrane; Cell projection;
KW   Disulfide bond; Glycoprotein; Host-virus interaction;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..515
FT                   /note="Nectin-1"
FT                   /id="PRO_0000015134"
FT   TOPO_DOM        31..354
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        376..515
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..141
FT                   /note="Ig-like V-type"
FT   DOMAIN          145..243
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          247..334
FT                   /note="Ig-like C2-type 2"
FT   REGION          282..299
FT                   /note="Interaction with FGFR"
FT   REGION          399..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         435
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         509
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   DISULFID        51..124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        172..226
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        269..316
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:22955284"
FT   CONFLICT        138
FT                   /note="L -> P (in Ref. 1; AAF60333)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="D -> N (in Ref. 2; AAF76195 and 3; AAG22808)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        342
FT                   /note="P -> PP (in Ref. 2; AAF76195)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        428
FT                   /note="G -> S (in Ref. 1; AAF60333 and 2; AAF76195)"
FT                   /evidence="ECO:0000305"
FT   STRAND          33..42
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   STRAND          61..70
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   STRAND          75..82
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   TURN            83..85
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   TURN            94..96
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   STRAND          120..129
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   STRAND          132..143
FT                   /evidence="ECO:0007829|PDB:5B21"
FT   STRAND          248..253
FT                   /evidence="ECO:0007829|PDB:2L7J"
FT   STRAND          267..272
FT                   /evidence="ECO:0007829|PDB:2L7J"
FT   STRAND          278..284
FT                   /evidence="ECO:0007829|PDB:2L7J"
FT   STRAND          293..296
FT                   /evidence="ECO:0007829|PDB:2L7J"
FT   STRAND          299..305
FT                   /evidence="ECO:0007829|PDB:2L7J"
FT   HELIX           308..310
FT                   /evidence="ECO:0007829|PDB:2L7J"
FT   STRAND          312..320
FT                   /evidence="ECO:0007829|PDB:2L7J"
FT   STRAND          323..331
FT                   /evidence="ECO:0007829|PDB:2L7J"
SQ   SEQUENCE   515 AA;  57035 MW;  A56FA2C7F8B25AFB CRC64;
     MARMGLAGAA GRWWGLALGL TAFFLPGTHT QVVQVNDSMY GFIGTDVVLH CSFANPLPSV
     KITQVTWQKA SNGSKQNMAI YNPTMGVSVL PPYEKRVEFL RPSFIDGTIR LSGLELEDEG
     MYICEFATFP TGNRESQLNL TVMAKPTNWI EGTRAVLRAR KGQDDKVLVA TCTSANGKPP
     SAVSWETRLK GEAEYQEIRN PNGTVTVISR YRLVPSREAH RQSLACIVNY HLDRFRESLT
     LNVQYEPEVT IEGFDGNWYL QRTDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL
     FFRGPITYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP TPEHGRRAGQ MPTAIIGGVA
     GSVLLVLIVV GGIIVALRRR RHTFKGDYST KKHVYGNGYS KAGIPQHHPP MAQNLQYPDD
     SDDEKKAGPL GGSSYEEEEE EEGGGGGERK VGGPHPKYDE DAKRPYFTVD EAEARQDGYG
     DRTLGYQYDP EQLDLAENMV SQNDGSFISK KEWYV
 
 
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