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NRX3A_HUMAN
ID   NRX3A_HUMAN             Reviewed;        1643 AA.
AC   Q9Y4C0; A6NGR4; A7MD34; O95378; Q8IUE3; Q9NS47; Q9P1V3; Q9P1V6; Q9UIE2;
AC   Q9UIE3; Q9ULA5; Q9Y486;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 4.
DT   03-AUG-2022, entry version 202.
DE   RecName: Full=Neurexin-3;
DE   AltName: Full=Neurexin III-alpha;
DE   AltName: Full=Neurexin-3-alpha;
DE   Flags: Precursor;
GN   Name=NRXN3; Synonyms=C14orf60, KIAA0743;
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] (ISOFORM 4A), AND TISSUE SPECIFICITY.
RC   TISSUE=Heart;
RX   PubMed=12379233; DOI=10.1016/s0006-291x(02)02403-8;
RA   Occhi G., Rampazzo A., Beffagna G., Antonio Danieli G.;
RT   "Identification and characterization of heart-specific splicing of human
RT   neurexin 3 mRNA (NRXN3).";
RL   Biochem. Biophys. Res. Commun. 298:151-155(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX   PubMed=11944992; DOI=10.1006/geno.2002.6734;
RA   Rowen L., Young J., Birditt B., Kaur A., Madan A., Philipps D.L., Qin S.,
RA   Minx P., Wilson R.K., Hood L., Graveley B.R.;
RT   "Analysis of the human neurexin genes: alternative splicing and the
RT   generation of protein diversity.";
RL   Genomics 79:587-597(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3A).
RC   TISSUE=Brain;
RX   PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XI. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:277-286(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3A).
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   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=19926856; DOI=10.1073/pnas.0809510106;
RA   Bottos A., Destro E., Rissone A., Graziano S., Cordara G., Assenzio B.,
RA   Cera M.R., Mascia L., Bussolino F., Arese M.;
RT   "The synaptic proteins neurexins and neuroligins are widely expressed in
RT   the vascular system and contribute to its functions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:20782-20787(2009).
CC   -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC       recognition and cell adhesion. May mediate intracellular signaling.
CC   -!- SUBUNIT: The laminin G-like domain 2 binds to NXPH1. Specific isoforms
CC       bind to alpha-dystroglycan. The cytoplasmic C-terminal region binds to
CC       CASK (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
CC         Comment=A number of isoforms, alpha-type and beta-type, are produced
CC         by alternative promoter usage. Beta-type isoforms differ from
CC         alpha-type isoforms in their N-terminus. Additional isoforms produced
CC         by alternative splicing seem to exist. {ECO:0000269|PubMed:11944992};
CC       Name=1a;
CC         IsoId=Q9Y4C0-1; Sequence=Displayed;
CC       Name=3a;
CC         IsoId=Q9Y4C0-3; Sequence=VSP_036463, VSP_036464;
CC       Name=4a;
CC         IsoId=Q9Y4C0-4; Sequence=VSP_041699, VSP_041700, VSP_041701,
CC                                  VSP_041702, VSP_041703, VSP_041704;
CC       Name=1b;
CC         IsoId=Q9HDB5-1; Sequence=External;
CC       Name=2b;
CC         IsoId=Q9HDB5-2; Sequence=External;
CC       Name=3b;
CC         IsoId=Q9HDB5-3; Sequence=External;
CC       Name=4b;
CC         IsoId=Q9HDB5-4; Sequence=External;
CC   -!- TISSUE SPECIFICITY: Expressed in the blood vessel walls (at protein
CC       level). Highly expressed in brain, lung, and pancreas; a lower level of
CC       expression is detectable in heart, placenta, liver, and kidney, whereas
CC       no expression can be observed in skeletal muscle. Isoform 4a is heart-
CC       specific. {ECO:0000269|PubMed:12379233, ECO:0000269|PubMed:19926856}.
CC   -!- MISCELLANEOUS: [Isoform 3a]: Produced by alternative splicing.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4a]: Produced by alternative splicing.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA34463.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ316284; CAC87720.2; -; mRNA.
DR   EMBL; AF099810; AAC68909.1; -; Genomic_DNA.
DR   EMBL; AF123462; AAD13621.1; -; Genomic_DNA.
DR   EMBL; AB018286; BAA34463.2; ALT_INIT; mRNA.
DR   EMBL; AC008056; AAF09143.1; -; Genomic_DNA.
DR   EMBL; AC012099; AAF15058.1; -; Genomic_DNA.
DR   EMBL; AC009396; AAF21147.1; -; Genomic_DNA.
DR   EMBL; AC008045; AAF28465.1; -; Genomic_DNA.
DR   EMBL; AC011440; AAF61277.1; -; Genomic_DNA.
DR   EMBL; AC026888; AAF87841.1; -; Genomic_DNA.
DR   EMBL; CH471061; EAW81316.1; -; Genomic_DNA.
DR   EMBL; BC152457; AAI52458.1; -; mRNA.
DR   CCDS; CCDS9870.1; -. [Q9Y4C0-3]
DR   RefSeq; NP_004787.2; NM_004796.5. [Q9Y4C0-3]
DR   AlphaFoldDB; Q9Y4C0; -.
DR   SMR; Q9Y4C0; -.
DR   BioGRID; 114770; 22.
DR   ELM; Q9Y4C0; -.
DR   IntAct; Q9Y4C0; 2.
DR   GlyGen; Q9Y4C0; 6 sites.
DR   iPTMnet; Q9Y4C0; -.
DR   PhosphoSitePlus; Q9Y4C0; -.
DR   BioMuta; NRXN3; -.
DR   DMDM; 224471902; -.
DR   EPD; Q9Y4C0; -.
DR   jPOST; Q9Y4C0; -.
DR   MassIVE; Q9Y4C0; -.
DR   MaxQB; Q9Y4C0; -.
DR   PaxDb; Q9Y4C0; -.
DR   PeptideAtlas; Q9Y4C0; -.
DR   PRIDE; Q9Y4C0; -.
DR   ProteomicsDB; 86154; -. [Q9Y4C0-1]
DR   ProteomicsDB; 86155; -. [Q9Y4C0-3]
DR   ProteomicsDB; 86156; -. [Q9Y4C0-4]
DR   Antibodypedia; 106; 252 antibodies from 31 providers.
DR   DNASU; 9369; -.
DR   Ensembl; ENST00000554719.5; ENSP00000451648.1; ENSG00000021645.20. [Q9Y4C0-3]
DR   Ensembl; ENST00000554738.5; ENSP00000450683.1; ENSG00000021645.20. [Q9Y4C0-4]
DR   GeneID; 9369; -.
DR   UCSC; uc001xun.5; human. [Q9Y4C0-1]
DR   CTD; 9369; -.
DR   DisGeNET; 9369; -.
DR   GeneCards; NRXN3; -.
DR   HGNC; HGNC:8010; NRXN3.
DR   HPA; ENSG00000021645; Tissue enhanced (brain, retina).
DR   MIM; 600567; gene.
DR   neXtProt; NX_Q9Y4C0; -.
DR   OpenTargets; ENSG00000021645; -.
DR   PharmGKB; PA31788; -.
DR   VEuPathDB; HostDB:ENSG00000021645; -.
DR   eggNOG; KOG3514; Eukaryota.
DR   GeneTree; ENSGT00940000154618; -.
DR   HOGENOM; CLU_001710_0_1_1; -.
DR   InParanoid; Q9Y4C0; -.
DR   PhylomeDB; Q9Y4C0; -.
DR   TreeFam; TF321302; -.
DR   PathwayCommons; Q9Y4C0; -.
DR   Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR   SignaLink; Q9Y4C0; -.
DR   SIGNOR; Q9Y4C0; -.
DR   BioGRID-ORCS; 9369; 10 hits in 1067 CRISPR screens.
DR   ChiTaRS; NRXN3; human.
DR   GenomeRNAi; 9369; -.
DR   Pharos; Q9Y4C0; Tbio.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9Y4C0; protein.
DR   Bgee; ENSG00000021645; Expressed in cerebellar vermis and 162 other tissues.
DR   ExpressionAtlas; Q9Y4C0; baseline and differential.
DR   Genevisible; Q9Y4C0; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0050839; F:cell adhesion molecule binding; TAS:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0097109; F:neuroligin family protein binding; TAS:BHF-UCL.
DR   GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0030534; P:adult behavior; IGI:BHF-UCL.
DR   GO; GO:0007411; P:axon guidance; TAS:ProtInc.
DR   GO; GO:0007612; P:learning; IGI:BHF-UCL.
DR   GO; GO:0007158; P:neuron cell-cell adhesion; TAS:BHF-UCL.
DR   GO; GO:0035176; P:social behavior; IGI:BHF-UCL.
DR   GO; GO:0071625; P:vocalization behavior; IGI:BHF-UCL.
DR   CDD; cd00110; LamG; 6.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR003585; Neurexin-like.
DR   InterPro; IPR027789; Syndecan/Neurexin_dom.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF02210; Laminin_G_2; 6.
DR   Pfam; PF01034; Syndecan; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00282; LamG; 6.
DR   SUPFAM; SSF49899; SSF49899; 6.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Alternative splicing; Calcium; Cell adhesion;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Metal-binding;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..1643
FT                   /note="Neurexin-3"
FT                   /id="PRO_0000019499"
FT   TOPO_DOM        28..1568
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1569..1589
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1590..1643
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..202
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          198..235
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          258..440
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          447..639
FT                   /note="Laminin G-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          643..680
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          685..857
FT                   /note="Laminin G-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          871..1046
FT                   /note="Laminin G-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          1049..1086
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1090..1260
FT                   /note="Laminin G-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          1294..1318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1611..1643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1294..1317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1625..1643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         304
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         374
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        757
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        202..213
FT                   /evidence="ECO:0000250"
FT   DISULFID        207..222
FT                   /evidence="ECO:0000250"
FT   DISULFID        224..234
FT                   /evidence="ECO:0000250"
FT   DISULFID        404..440
FT                   /evidence="ECO:0000250"
FT   DISULFID        610..639
FT                   /evidence="ECO:0000250"
FT   DISULFID        647..658
FT                   /evidence="ECO:0000250"
FT   DISULFID        652..667
FT                   /evidence="ECO:0000250"
FT   DISULFID        669..679
FT                   /evidence="ECO:0000250"
FT   DISULFID        1018..1046
FT                   /evidence="ECO:0000250"
FT   DISULFID        1053..1064
FT                   /evidence="ECO:0000250"
FT   DISULFID        1058..1073
FT                   /evidence="ECO:0000250"
FT   DISULFID        1075..1085
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..373
FT                   /note="Missing (in isoform 3a)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9872452"
FT                   /id="VSP_036463"
FT   VAR_SEQ         237..242
FT                   /note="Missing (in isoform 4a)"
FT                   /evidence="ECO:0000303|PubMed:12379233"
FT                   /id="VSP_041699"
FT   VAR_SEQ         252
FT                   /note="Q -> QGRSK (in isoform 4a)"
FT                   /evidence="ECO:0000303|PubMed:12379233"
FT                   /id="VSP_041700"
FT   VAR_SEQ         750..759
FT                   /note="DCIRINCNSS -> G (in isoform 4a)"
FT                   /evidence="ECO:0000303|PubMed:12379233"
FT                   /id="VSP_041701"
FT   VAR_SEQ         1205
FT                   /note="T -> TGNTDNERFQMVKQKIPFKYNRPVEEWLQEK (in isoform
FT                   4a)"
FT                   /evidence="ECO:0000303|PubMed:12379233"
FT                   /id="VSP_041702"
FT   VAR_SEQ         1334..1542
FT                   /note="Missing (in isoform 3a)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9872452"
FT                   /id="VSP_036464"
FT   VAR_SEQ         1335..1373
FT                   /note="TGGELVIPLLVEDPLATPPIATRAPSITLPPTFRPLLTI -> GRSARSSNA
FT                   ARSLRAALTWTWRLTYTFTPIIFISCVVHS (in isoform 4a)"
FT                   /evidence="ECO:0000303|PubMed:12379233"
FT                   /id="VSP_041703"
FT   VAR_SEQ         1374..1643
FT                   /note="Missing (in isoform 4a)"
FT                   /evidence="ECO:0000303|PubMed:12379233"
FT                   /id="VSP_041704"
FT   CONFLICT        1043
FT                   /note="E -> K (in Ref. 3; BAA34463 and 6; AAI52458)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1643 AA;  180599 MW;  E7360348E263C6EC CRC64;
     MSSTLHSVFF TLKVSILLGS LLGLCLGLEF MGLPNQWARY LRWDASTRSD LSFQFKTNVS
     TGLLLYLDDG GVCDFLCLSL VDGRVQLRFS MDCAETAVLS NKQVNDSSWH FLMVSRDRLR
     TVLMLDGEGQ SGELQPQRPY MDVVSDLFLG GVPTDIRPSA LTLDGVQAMP GFKGLILDLK
     YGNSEPRLLG SRGVQMDAEG PCGERPCENG GICFLLDGHP TCDCSTTGYG GKLCSEDVSQ
     DPGLSHLMMS EQAREENVAT FRGSEYLCYD LSQNPIQSSS DEITLSFKTW QRNGLILHTG
     KSADYVNLAL KDGAVSLVIN LGSGAFEAIV EPVNGKFNDN AWHDVKVTRN LRQVTISVDG
     ILTTTGYTQE DYTMLGSDDF FYVGGSPSTA DLPGSPVSNN FMGCLKEVVY KNNDIRLELS
     RLARIADTKM KIYGEVVFKC ENVATLDPIN FETPEAYISL PKWNTKRMGS ISFDFRTTEP
     NGLILFTHGK PQERKDARSQ KNTKVDFFAV ELLDGNLYLL LDMGSGTIKV KATQKKANDG
     EWYHVDIQRD GRSGTISVNS RRTPFTASGE SEILDLEGDM YLGGLPENRA GLILPTELWT
     AMLNYGYVGC IRDLFIDGRS KNIRQLAEMQ NAAGVKSSCS RMSAKQCDSY PCKNNAVCKD
     GWNRFICDCT GTGYWGRTCE REASILSYDG SMYMKIIMPM VMHTEAEDVS FRFMSQRAYG
     LLVATTSRDS ADTLRLELDG GRVKLMVNLD CIRINCNSSK GPETLYAGQK LNDNEWHTVR
     VVRRGKSLKL TVDDDVAEGT MVGDHTRLEF HNIETGIMTE KRYISVVPSS FIGHLQSLMF
     NGLLYIDLCK NGDIDYCELK ARFGLRNIIA DPVTFKTKSS YLSLATLQAY TSMHLFFQFK
     TTSPDGFILF NSGDGNDFIA VELVKGYIHY VFDLGNGPNV IKGNSDRPLN DNQWHNVVIT
     RDNSNTHSLK VDTKVVTQVI NGAKNLDLKG DLYMAGLAQG MYSNLPKLVA SRDGFQGCLA
     SVDLNGRLPD LINDALHRSG QIERGCEGPS TTCQEDSCAN QGVCMQQWEG FTCDCSMTSY
     SGNQCNDPGA TYIFGKSGGL ILYTWPANDR PSTRSDRLAV GFSTTVKDGI LVRIDSAPGL
     GDFLQLHIEQ GKIGVVFNIG TVDISIKEER TPVNDGKYHV VRFTRNGGNA TLQVDNWPVN
     EHYPTGRQLT IFNTQAQIAI GGKDKGRLFQ GQLSGLYYDG LKVLNMAAEN NPNIKINGSV
     RLVGEVPSIL GTTQTTSMPP EMSTTVMETT TTMATTTTRK NRSTASIQPT SDDLVSSAEC
     SSDDEDFVEC EPSTTGGELV IPLLVEDPLA TPPIATRAPS ITLPPTFRPL LTIIETTKDS
     LSMTSEAGLP CLSDQGSDGC DDDGLVISGY GSGETFDSNL PPTDDEDFYT TFSLVTDKSL
     STSIFEGGYK AHAPKWESKD FRPNKVSETS RTTTTSLSPE LIRFTASSSS GMVPKLPAGK
     MNNRDLKPQP DIVLLPLPTA YELDSTKLKS PLITSPMFRN VPTANPTEPG IRRVPGASEV
     IRESSSTTGM VVGIVAAAAL CILILLYAMY KYRNRDEGSY QVDETRNYIS NSAQSNGTLM
     KEKQQSSKSG HKKQKNKDRE YYV
 
 
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