位置:首页 > 蛋白库 > EPHA3_MOUSE
EPHA3_MOUSE
ID   EPHA3_MOUSE             Reviewed;         983 AA.
AC   P29319;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 186.
DE   RecName: Full=Ephrin type-A receptor 3;
DE            EC=2.7.10.1;
DE   AltName: Full=EPH-like kinase 4;
DE            Short=EK4;
DE            Short=mEK4;
DE   AltName: Full=Tyrosine-protein kinase TYRO4;
DE   AltName: Full=Tyrosine-protein kinase receptor ETK1;
DE   Flags: Precursor;
GN   Name=Epha3; Synonyms=Etk1, Mek4, Tyro4;
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] (ISOFORMS LONG AND SHORT).
RC   STRAIN=ICR X Swiss Webster; TISSUE=Embryo;
RX   PubMed=1657122;
RA   Sajjadi F.G., Pasquale E.B., Subramani S.;
RT   "Identification of a new eph-related receptor tyrosine kinase gene from
RT   mouse and chicken that is developmentally regulated and encodes at least
RT   two forms of the receptor.";
RL   New Biol. 3:769-778(1991).
RN   [2]
RP   INTERACTION WITH CRK.
RX   PubMed=11870224; DOI=10.1242/jcs.115.5.1059;
RA   Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M., Down M.,
RA   Boyd A.W., Alewood P.F., Lackmann M.;
RT   "Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing
RT   293T and melanoma cells by CrkII and Rho-mediated signalling.";
RL   J. Cell Sci. 115:1059-1072(2002).
RN   [3]
RP   DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=14585969; DOI=10.1128/mcb.23.22.8092-8098.2003;
RA   Vaidya A., Pniak A., Lemke G., Brown A.;
RT   "EphA3 null mutants do not demonstrate motor axon guidance defects.";
RL   Mol. Cell. Biol. 23:8092-8098(2003).
RN   [4]
RP   DISRUPTION PHENOTYPE, FUNCTION IN HEART DEVELOPMENT, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=17046737; DOI=10.1016/j.ydbio.2006.08.058;
RA   Stephen L.J., Fawkes A.L., Verhoeve A., Lemke G., Brown A.;
RT   "A critical role for the EphA3 receptor tyrosine kinase in heart
RT   development.";
RL   Dev. Biol. 302:66-79(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-937, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [6]
RP   FUNCTION IN MOTOR AND SENSORY AXONS SEGREGATION.
RX   PubMed=18403711; DOI=10.1126/science.1153758;
RA   Gallarda B.W., Bonanomi D., Mueller D., Brown A., Alaynick W.A.,
RA   Andrews S.E., Lemke G., Pfaff S.L., Marquardt T.;
RT   "Segregation of axial motor and sensory pathways via heterotypic trans-
RT   axonal signaling.";
RL   Science 320:233-236(2008).
RN   [7]
RP   FUNCTION IN CELL MIGRATION, AND INTERACTION WITH NCK1.
RX   PubMed=19505147; DOI=10.1021/bi900831k;
RA   Hu T., Shi G., Larose L., Rivera G.M., Mayer B.J., Zhou R.;
RT   "Regulation of process retraction and cell migration by EphA3 is mediated
RT   by the adaptor protein Nck1.";
RL   Biochemistry 48:6369-6378(2009).
RN   [8]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA   Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA   Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT   "Gene expression profiling of muscle stem cells identifies novel regulators
RT   of postnatal myogenesis.";
RL   Front. Cell Dev. Biol. 4:58-58(2016).
CC   -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-
CC       bound ephrin family ligands residing on adjacent cells, leading to
CC       contact-dependent bidirectional signaling into neighboring cells. The
CC       signaling pathway downstream of the receptor is referred to as forward
CC       signaling while the signaling pathway downstream of the ephrin ligand
CC       is referred to as reverse signaling. Highly promiscuous for ephrin-A
CC       ligands it binds preferentially EFNA5. Upon activation by EFNA5
CC       regulates cell-cell adhesion, cytoskeletal organization and cell
CC       migration. Plays a role in cardiac cells migration and differentiation
CC       and regulates the formation of the atrioventricular canal and septum
CC       during development probably through activation by EFNA1. Involved in
CC       the retinotectal mapping of neurons. May also control the segregation
CC       but not the guidance of motor and sensory axons during neuromuscular
CC       circuit development. {ECO:0000269|PubMed:17046737,
CC       ECO:0000269|PubMed:18403711, ECO:0000269|PubMed:19505147}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer
CC       is composed of an ephrin dimer and a receptor dimer. Oligomerization is
CC       probably required to induce biological responses. Forms a ternary
CC       EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain
CC       shedding by ADAM10 which regulates the EFNA5-EPHA3 complex
CC       internalization and function. Interacts (phosphorylated) with PTPN1;
CC       dephosphorylates EPHA3 and may regulate its trafficking and function
CC       (By similarity). Interacts (phosphorylated) with CRK; mediates EFNA5-
CC       EPHA3 signaling through RHOA GTPase activation. Interacts with NCK1
CC       (via SH2 domain); mediates EFNA5-EPHA3 signaling. {ECO:0000250,
CC       ECO:0000269|PubMed:11870224, ECO:0000269|PubMed:19505147}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane
CC       {ECO:0000250|UniProtKB:P29320}; Single-pass type I membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Short]: Secreted
CC       {ECO:0000250|UniProtKB:P29320}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P29319-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P29319-3; Sequence=VSP_041882, VSP_041883;
CC   -!- TISSUE SPECIFICITY: Greatest levels of expression occurring in the
CC       brain, also detected in testis. Expressed in myogenic progenitor cells
CC       (PubMed:27446912). {ECO:0000269|PubMed:27446912}.
CC   -!- DEVELOPMENTAL STAGE: Specifically expressed in heart during its
CC       development by mesenchymal cells of the endocardial cushions. Expressed
CC       in motor neurons at 11.5 dpc. In myogenic progenitor cells, highly
CC       expressed, at least as early as 11.5 dpc, expression decreases until 4
CC       weeks after birth (PubMed:27446912). {ECO:0000269|PubMed:14585969,
CC       ECO:0000269|PubMed:17046737, ECO:0000269|PubMed:27446912}.
CC   -!- PTM: Autophosphorylates upon activation by EFNA5. Phosphorylation on
CC       Tyr-602 mediates interaction with NCK1. Dephosphorylated by PTPN1 (By
CC       similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice die perinatally due to cardiac failure.
CC       {ECO:0000269|PubMed:14585969, ECO:0000269|PubMed:17046737}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M68513; AAA39521.1; -; mRNA.
DR   EMBL; M68515; AAA39522.1; -; mRNA.
DR   PIR; A45583; A45583.
DR   AlphaFoldDB; P29319; -.
DR   SMR; P29319; -.
DR   STRING; 10090.ENSMUSP00000066554; -.
DR   BindingDB; P29319; -.
DR   ChEMBL; CHEMBL2034794; -.
DR   GuidetoPHARMACOLOGY; 1823; -.
DR   GlyGen; P29319; 5 sites.
DR   iPTMnet; P29319; -.
DR   PhosphoSitePlus; P29319; -.
DR   MaxQB; P29319; -.
DR   PaxDb; P29319; -.
DR   PRIDE; P29319; -.
DR   ProteomicsDB; 275753; -. [P29319-1]
DR   ProteomicsDB; 275754; -. [P29319-3]
DR   MGI; MGI:99612; Epha3.
DR   eggNOG; KOG0196; Eukaryota.
DR   InParanoid; P29319; -.
DR   PhylomeDB; P29319; -.
DR   BRENDA; 2.7.10.1; 3474.
DR   Reactome; R-MMU-2682334; EPH-Ephrin signaling.
DR   Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR   ChiTaRS; Epha3; mouse.
DR   PRO; PR:P29319; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P29319; protein.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098793; C:presynapse; IDA:SynGO.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005003; F:ephrin receptor activity; IDA:MGI.
DR   GO; GO:0005004; F:GPI-linked ephrin receptor activity; ISS:UniProtKB.
DR   GO; GO:0019838; F:growth factor binding; IPI:ARUK-UCL.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IDA:MGI.
DR   GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
DR   GO; GO:0003197; P:endocardial cushion development; IMP:UniProtKB.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0097156; P:fasciculation of motor neuron axon; IMP:UniProtKB.
DR   GO; GO:0097155; P:fasciculation of sensory neuron axon; IMP:UniProtKB.
DR   GO; GO:0045806; P:negative regulation of endocytosis; ISO:MGI.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IDA:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
DR   GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; IGI:MGI.
DR   GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR   GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd10481; EphR_LBD_A3; 1.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 1.10.150.50; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR027936; Eph_TM.
DR   InterPro; IPR034266; EphA3_rcpt_lig-bd.
DR   InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR   InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR   Pfam; PF14575; EphA2_TM; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF07699; Ephrin_rec_like; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS51550; EPH_LBD; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR   PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Secreted; Signal; Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..983
FT                   /note="Ephrin type-A receptor 3"
FT                   /id="PRO_0000016803"
FT   TOPO_DOM        21..540
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        541..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        565..983
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..206
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT   DOMAIN          324..434
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          435..530
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          621..882
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          911..975
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   MOTIF           981..983
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        746
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         628..633
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         653
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         700..706
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         750..751
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         596
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P29320"
FT   MOD_RES         602
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P29320"
FT   MOD_RES         701
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P29320"
FT   MOD_RES         779
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P29320"
FT   MOD_RES         937
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         531..537
FT                   /note="SFSISGE -> CMYYFSF (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:1657122"
FT                   /id="VSP_041882"
FT   VAR_SEQ         538..983
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:1657122"
FT                   /id="VSP_041883"
SQ   SEQUENCE   983 AA;  109955 MW;  BE44A6655D8107A2 CRC64;
     MDCHLSILVL LGCCVLSCSG ELSPQPSNEV NLLDSKTIQG ELGWISYPSH GWEEISGVDE
     HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK FTLRDCNSIP LVLGTCKETF
     NLYYMESDDH GVKFREHQFT KIDTIAADES FTQMDLGDRI LKLNTEIREV GPVNKKGFYL
     AFQDVGACVA LVSVRVYFKK CPFTVKNLAM FPDTVPMDSQ SLVEVRGSCV NNSKEEDPPR
     MYCSTEGEWL VPIGKCTCNA GYEERGFICQ ACRPGFYKAS DGAAKCAKCP PHSSTQEDGS
     MNCRCENNYF RAEKDPPSMA CARPPSAPRN VISNINETSV ILDWSWPLDT GGRKDITFNI
     ICKKCGWNVR QCEPCSPNVR FLPRQLGLTN TTVTVTDLLA HTNYTFEIDA VNGVSELSSP
     PRQYAAVSIT TNQAAPSPVM TIKKDRTSRN SISLSWQEPE HPNGIILDYE VKYYQKQEQE
     TSYTILRARG TNVTISSLKP DTTYVFQIRA RTAAGYGTNS RKFEFETSPD SFSISGENSH
     VVMIAISAAV AIIVLTVVTY VLVGRFCGYH KSKHSAEEKR LHFGNGHLKL PGLRTYVDPH
     TYEDPTQAVH EFAKELDATN ISIDKVVGAG EFGEVCSGRL KLPSKKEISV AIKTLKVGYT
     EKQRRDFLGE ASIMGQFDHP NIIRLEGVVT KSKPEMIVTE YMENGSLDSF LRKHDAQFTV
     IQLVGMLRGI ASGMKYLSDM GYVHRDLAAR NILINSNLVC KVSDFGLSRV LEDDPEAAYT
     TRGGKIPIRW TSPEAMSYRK FTSASDVWSY GIVLWEVMSY GERPYSQMSN QDVIKAVDER
     YRLPPPMDCP AALYQLMLDC WQKDRNNRPK FEQIVSILDK LIRNPGSLKI ITSAAARPSN
     LLLDQSNVDI ATFHTTGDWL NGMRTAHCKE IFTGVEYSSC DTIAKISTDD MKKVGVTVVG
     PQKKIISTIK ALETQSKNGP VPV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024