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 27-MAR-2024, entry version 190.
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. Component of a complex
CC composed of TSC22D1 (via N-terminus), TGFBR1 and TGFBR2; the
CC interaction between TSC22D1 and TGFBR1 is inhibited by SMAD7 and
CC promoted by TGFB1 (By similarity). Interacts with DAXX. Interacts with
CC DYNLT4. Interacts with ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the
CC TGF-beta receptor (By similarity). Interacts with and is activated by
CC SCUBE3; this interaction does not affect TGFB1-binding to TGFBR2 (By
CC similarity). Interacts with VPS39; this interaction is independent of
CC the receptor kinase activity and of the presence of TGF-beta (By
CC 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}.
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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 GlyCosmos; P38438; 2 sites, No reported glycans.
DR GlyGen; P38438; 2 sites.
DR iPTMnet; P38438; -.
DR PhosphoSitePlus; P38438; -.
DR SwissPalm; P38438; -.
DR PaxDb; 10116-ENSRNOP00000035501; -.
DR Ensembl; ENSRNOT00000116107.1; ENSRNOP00000093892.1; ENSRNOG00000013265.7.
DR Ensembl; ENSRNOT00055010808; ENSRNOP00055008392; ENSRNOG00055006638.
DR Ensembl; ENSRNOT00060053114; ENSRNOP00060044162; ENSRNOG00060030566.
DR Ensembl; ENSRNOT00065005407; ENSRNOP00065003934; ENSRNOG00065003711.
DR GeneID; 81810; -.
DR KEGG; rno:81810; -.
DR UCSC; RGD:69651; rat.
DR AGR; RGD:69651; -.
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 OrthoDB; 3900892at2759; -.
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 cell types or 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:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO: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:0019209; F:kinase activator activity; 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:0060090; F:molecular adaptor activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; TAS:RGD.
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:0009887; P:animal organ morphogenesis; IMP:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0035909; P:aorta morphogenesis; ISO:RGD.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0048844; P:artery morphogenesis; 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: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:0001837; P:epithelial to mesenchymal transition; 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; ISO:RGD.
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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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: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:0060391; P:positive regulation of SMAD protein signal transduction; ISO: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: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:2000736; P:regulation of stem cell differentiation; ISO:RGD.
DR GO; GO:0072091; P:regulation of stem cell proliferation; ISO:RGD.
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:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0062009; P:secondary palate development; ISO:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; 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 CDD; cd14055; STKc_TGFbR2_like; 1.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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:SF55; TGF-BETA RECEPTOR TYPE-2; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 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; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57302; Snake toxin-like; 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
//
