位置:首页 > 蛋白库 > TGFR2_RAT
TGFR2_RAT
ID   TGFR2_RAT               Reviewed;         567 AA.
AC   P38438;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=TGF-beta receptor type-2;
DE            Short=TGFR-2;
DE            EC=2.7.11.30;
DE   AltName: Full=TGF-beta type II receptor;
DE   AltName: Full=Transforming growth factor-beta receptor type II;
DE            Short=TGF-beta receptor type II;
DE            Short=TbetaR-II;
DE   Flags: Precursor;
GN   Name=Tgfbr2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Pituitary;
RX   PubMed=8385453; DOI=10.1006/bbrc.1993.1286;
RA   Tsuchida K., Lewis K.A., Mathews L.S., Vale W.W.;
RT   "Molecular characterization of rat transforming growth factor-beta type II
RT   receptor.";
RL   Biochem. Biophys. Res. Commun. 191:790-795(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8264154; DOI=10.1038/ki.1993.336;
RA   Choi M.E., Kim E.G., Huang Q., Ballermann B.J.;
RT   "Rat mesangial cell hypertrophy in response to transforming growth factor-
RT   beta 1.";
RL   Kidney Int. 44:948-958(1993).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-
CC       beta type I serine/threonine kinase receptor, TGFBR1, the non-
CC       promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3.
CC       Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to
CC       the cytoplasm and is thus regulating a plethora of physiological and
CC       pathological processes including cell cycle arrest in epithelial and
CC       hematopoietic cells, control of mesenchymal cell proliferation and
CC       differentiation, wound healing, extracellular matrix production,
CC       immunosuppression and carcinogenesis. The formation of the receptor
CC       complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound
CC       to the cytokine dimer results in the phosphorylation and the activation
CC       of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1
CC       phosphorylates SMAD2 which dissociates from the receptor and interacts
CC       with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the
CC       nucleus where it modulates the transcription of the TGF-beta-regulated
CC       genes. This constitutes the canonical SMAD-dependent TGF-beta signaling
CC       cascade. Also involved in non-canonical, SMAD-independent TGF-beta
CC       signaling pathways (By similarity). {ECO:0000250|UniProtKB:P37173}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC         L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC         COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC         seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC         Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.30;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric
CC       ligands assemble a functional receptor composed of two TGFBR1 and
CC       TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The
CC       respective affinity of TGFRB1 and TGFRB2 for the ligands may modulate
CC       the kinetics of assembly of the receptor and may explain the different
CC       biological activities of TGFB1, TGFB2 and TGFB3. Interacts with DAXX.
CC       Interacts with DYNLT4. Interacts with ZFYVE9; ZFYVE9 recruits SMAD2 and
CC       SMAD3 to the TGF-beta receptor (By similarity). Interacts with and is
CC       activated by SCUBE3; this interaction does not affect TGFB1-binding to
CC       TGFBR2 (By similarity). Interacts with VPS39; this interaction is
CC       independent of the receptor kinase activity and of the presence of TGF-
CC       beta (By similarity). Interacts with CLU (By similarity).
CC       {ECO:0000250|UniProtKB:P37173}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P37173};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:P37173}.
CC       Membrane raft {ECO:0000250|UniProtKB:P37173}.
CC   -!- PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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; L09653; AAA42237.1; -; mRNA.
DR   EMBL; S67770; AAB29352.2; -; mRNA.
DR   PIR; JN0459; JN0459.
DR   RefSeq; NP_112394.3; NM_031132.3.
DR   AlphaFoldDB; P38438; -.
DR   SMR; P38438; -.
DR   BioGRID; 249668; 3.
DR   CORUM; P38438; -.
DR   IntAct; P38438; 1.
DR   STRING; 10116.ENSRNOP00000035501; -.
DR   GlyGen; P38438; 2 sites.
DR   iPTMnet; P38438; -.
DR   PhosphoSitePlus; P38438; -.
DR   PaxDb; P38438; -.
DR   PRIDE; P38438; -.
DR   Ensembl; ENSRNOT00000116107; ENSRNOP00000093892; ENSRNOG00000013265.
DR   GeneID; 81810; -.
DR   KEGG; rno:81810; -.
DR   UCSC; RGD:69651; rat.
DR   CTD; 7048; -.
DR   RGD; 69651; Tgfbr2.
DR   eggNOG; KOG3653; Eukaryota.
DR   GeneTree; ENSGT00940000157527; -.
DR   HOGENOM; CLU_000288_8_3_1; -.
DR   InParanoid; P38438; -.
DR   OMA; MCSCSAE; -.
DR   OrthoDB; 426838at2759; -.
DR   PhylomeDB; P38438; -.
DR   BRENDA; 2.7.10.2; 5301.
DR   Reactome; R-RNO-2173788; Downregulation of TGF-beta receptor signaling.
DR   Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
DR   Reactome; R-RNO-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR   PRO; PR:P38438; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000013265; Expressed in lung and 18 other tissues.
DR   ExpressionAtlas; P38438; baseline and differential.
DR   Genevisible; P38438; RN.
DR   GO; GO:0005901; C:caveola; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0043235; C:receptor complex; ISO:RGD.
DR   GO; GO:0070021; C:transforming growth factor beta ligand-receptor complex; ISO:RGD.
DR   GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR   GO; GO:0017002; F:activin receptor activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005539; F:glycosaminoglycan binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; TAS:RGD.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; TAS:RGD.
DR   GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR   GO; GO:0050431; F:transforming growth factor beta binding; ISO:RGD.
DR   GO; GO:0005024; F:transforming growth factor beta receptor activity; ISO:RGD.
DR   GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IMP:RGD.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISO:RGD.
DR   GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISO:RGD.
DR   GO; GO:0032147; P:activation of protein kinase activity; ISO:RGD.
DR   GO; GO:0007568; P:aging; IEP:RGD.
DR   GO; GO:0009887; P:animal organ morphogenesis; IMP:RGD.
DR   GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR   GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR   GO; GO:0003181; P:atrioventricular valve morphogenesis; ISO:RGD.
DR   GO; GO:0007420; P:brain development; ISO:RGD.
DR   GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
DR   GO; GO:0060433; P:bronchus development; ISO:RGD.
DR   GO; GO:0060434; P:bronchus morphogenesis; ISO:RGD.
DR   GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISO:RGD.
DR   GO; GO:0051216; P:cartilage development; ISO:RGD.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR   GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IDA:RGD.
DR   GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR   GO; GO:0007566; P:embryo implantation; IEP:RGD.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:RGD.
DR   GO; GO:0035162; P:embryonic hemopoiesis; ISO:RGD.
DR   GO; GO:0003274; P:endocardial cushion fusion; ISO:RGD.
DR   GO; GO:0007369; P:gastrulation; ISO:RGD.
DR   GO; GO:0003430; P:growth plate cartilage chondrocyte growth; ISO:RGD.
DR   GO; GO:0003417; P:growth plate cartilage development; ISO:RGD.
DR   GO; GO:0007507; P:heart development; ISO:RGD.
DR   GO; GO:0001947; P:heart looping; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:1905317; P:inferior endocardial cushion morphogenesis; ISO:RGD.
DR   GO; GO:0061520; P:Langerhans cell differentiation; IEA:Ensembl.
DR   GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
DR   GO; GO:1990086; P:lens fiber cell apoptotic process; ISO:RGD.
DR   GO; GO:0030324; P:lung development; IEP:RGD.
DR   GO; GO:0060463; P:lung lobe morphogenesis; ISO:RGD.
DR   GO; GO:0060425; P:lung morphogenesis; ISO:RGD.
DR   GO; GO:0060443; P:mammary gland morphogenesis; ISO:RGD.
DR   GO; GO:0003149; P:membranous septum morphogenesis; ISO:RGD.
DR   GO; GO:1990428; P:miRNA transport; ISO:RGD.
DR   GO; GO:0043011; P:myeloid dendritic cell differentiation; ISO:RGD.
DR   GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR   GO; GO:0003151; P:outflow tract morphogenesis; ISO:RGD.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; ISO:RGD.
DR   GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISO:RGD.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR   GO; GO:0002663; P:positive regulation of B cell tolerance induction; ISO:RGD.
DR   GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; ISO:RGD.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD.
DR   GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISO:RGD.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:RGD.
DR   GO; GO:0051138; P:positive regulation of NK T cell differentiation; ISO:RGD.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:RGD.
DR   GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:RGD.
DR   GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; IEP:RGD.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR   GO; GO:0002666; P:positive regulation of T cell tolerance induction; ISO:RGD.
DR   GO; GO:0002651; P:positive regulation of tolerance induction to self antigen; ISO:RGD.
DR   GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IDA:RGD.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR   GO; GO:0072091; P:regulation of stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0070723; P:response to cholesterol; ISO:RGD.
DR   GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR   GO; GO:0009749; P:response to glucose; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR   GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR   GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR   GO; GO:0062009; P:secondary palate development; ISO:RGD.
DR   GO; GO:0007224; P:smoothened signaling pathway; ISO:RGD.
DR   GO; GO:0060440; P:trachea formation; ISO:RGD.
DR   GO; GO:0060439; P:trachea morphogenesis; ISO:RGD.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:RGD.
DR   GO; GO:0003186; P:tricuspid valve morphogenesis; ISO:RGD.
DR   GO; GO:0001570; P:vasculogenesis; IEP:RGD.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; ISO:RGD.
DR   GO; GO:0042060; P:wound healing; IEP:RGD.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   InterPro; IPR017194; Transform_growth_fac-b_typ-2.
DR   InterPro; IPR015013; Transforming_GF_b_rcpt_2_ecto.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF08917; ecTbetaR2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF037393; TGFRII; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; ATP-binding; Cell membrane; Differentiation; Disulfide bond;
KW   Glycoprotein; Growth regulation; Kinase; Magnesium; Manganese; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..567
FT                   /note="TGF-beta receptor type-2"
FT                   /id="PRO_0000024429"
FT   TOPO_DOM        24..166
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..567
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          244..546
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          546..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        379
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         250..258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62312"
FT   MOD_RES         548
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         553
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62312"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..84
FT                   /evidence="ECO:0000250|UniProtKB:P37173"
FT   DISULFID        54..71
FT                   /evidence="ECO:0000250|UniProtKB:P37173"
FT   DISULFID        61..67
FT                   /evidence="ECO:0000250|UniProtKB:P37173"
FT   DISULFID        77..101
FT                   /evidence="ECO:0000250|UniProtKB:P37173"
FT   DISULFID        121..136
FT                   /evidence="ECO:0000250|UniProtKB:P37173"
FT   DISULFID        138..143
FT                   /evidence="ECO:0000250|UniProtKB:P37173"
FT   CONFLICT        388..389
FT                   /note="KN -> RS (in Ref. 2; AAB29352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        403
FT                   /note="R -> G (in Ref. 2; AAB29352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        405
FT                   /note="D -> S (in Ref. 2; AAB29352)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        477
FT                   /note="K -> R (in Ref. 2; AAB29352)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   567 AA;  64241 MW;  EC1D7642A51A3B75 CRC64;
     MGRGLLRGLW PLHIVLWTRI ASTIPPHVPK SVNSDLMAGD NSGAVKLPQL CKFCDVTLST
     CDNQKSCMSN CSVTSICEKP QEVCVAVWRK NDKNITLETV CHDPKFTYHG FTLEDATSPT
     CVMKEKKRAG ETFFMCSCNT EECNDYIIFN EEYTTSSPDL LLVIIQVTGV SLLPPLGIAI
     AVIAIFYCYR VHRQQKLSPS WESSKPRKLM DFSDNCAIIL EDDRSDISST CANNINHNTE
     LLPIELDTLV GKGRFAEVYK AKLKQNTSEQ FETVAVKIFP YEEYSSWKTE KDIFSDINLK
     HENILQFLTA EERKTEMGKQ YWLITAFHAK GNLQEYLTRH VISWEDLRKL GSSLARGIAH
     LHSDHTPCGR PKMPIVHRDL KSSNILVKND LTCCLCDFGL SLRLDPTLSV DDLANSGQVG
     TARYMAPEVL ESRMNLENME SFKQTDVYSM ALVLWEMTSR CNAVGEVKDY EPPFGSKVRE
     HPCVESMKDN VLRDRGRPEI PSFWLNHQGI QIVCETLTEC WDHDPEARLT AQCVAERFSE
     LEHPDRLSGR SCSQEKIPED GSLNTTK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024