ID SMAD7_MOUSE Reviewed; 426 AA. AC O35253; O88709; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 204. DE RecName: Full=Mothers against decapentaplegic homolog 7; DE Short=MAD homolog 7; DE Short=Mothers against DPP homolog 7; DE AltName: Full=Mothers against decapentaplegic homolog 8; DE Short=MAD homolog 8; DE Short=Mothers against DPP homolog 8; DE AltName: Full=SMAD family member 7; DE Short=SMAD 7; DE Short=Smad7; GN Name=Smad7; Synonyms=Madh7, Madh8; 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] (ISOFORM A). RC TISSUE=Placenta; RX PubMed=9335507; DOI=10.1038/39369; RA Nakao A., Afrakhte M., Moren A., Nakayama T., Christian J.L., Heuchel R., RA Itoh S., Kawabata M., Heldin N.-E., Heldin C.-H., ten Dijke P.; RT "Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta RT signalling."; RL Nature 389:631-635(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RC TISSUE=Embryo; RA Kitamura K., Okazaki K.; RT "Characterization of a novel mouse homologue of Mad, Smad7, that can RT mediate TGF-beta family signalling."; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B). RC TISSUE=Embryo; RA Kitamura K., Okazaki K.; RT "Isolation of cDNAs encoding mouse homologues of Mad (Smad7 and Smad7B) RT that can mediate TGF-beta family signalling."; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B). RX PubMed=10828018; RA Kitamura K., Aota S., Sakamoto R., Yoshikawa S.I., Okazaki K.; RT "Smad7 selectively interferes with different pathways of activin signaling RT and inhibits erythroid leukemia cell differentiation."; RL Blood 95:3371-3379(2000). RN [5] RP PHOSPHORYLATION AT SER-249, MUTAGENESIS OF SER-249, AND SUBCELLULAR RP LOCATION. RX PubMed=11278814; DOI=10.1074/jbc.m011019200; RA Pulaski L., Landstrom M., Heldin C.-H., Souchelnytskyi S.; RT "Phosphorylation of Smad7 at Ser-249 does not interfere with its inhibitory RT role in transforming growth factor-beta-dependent signaling but affects RT Smad7-dependent transcriptional activation."; RL J. Biol. Chem. 276:14344-14349(2001). RN [6] RP INTERACTION WITH RNF111, AND UBIQUITINATION. RX PubMed=14657019; DOI=10.1093/emboj/cdg632; RA Koinuma D., Shinozaki M., Komuro A., Goto K., Saitoh M., Hanyu A., RA Ebina M., Nukiwa T., Miyazawa K., Imamura T., Miyazono K.; RT "Arkadia amplifies TGF-beta superfamily signaling through degradation of RT Smad7."; RL EMBO J. 22:6458-6470(2003). RN [7] RP INTERACTION WITH WWP1, AND UBIQUITINATION. RX PubMed=15221015; DOI=10.1038/sj.onc.1207885; RA Komuro A., Imamura T., Saitoh M., Yoshida Y., Yamori T., Miyazono K., RA Miyazawa K.; RT "Negative regulation of transforming growth factor-beta (TGF-beta) RT signaling by WW domain-containing protein 1 (WWP1)."; RL Oncogene 23:6914-6923(2004). RN [8] RP INTERACTION WITH NEDD4L, AND SUBCELLULAR LOCATION. RX PubMed=15496141; DOI=10.1042/bj20040738; RA Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K., Miyazono K., RA Imamura T.; RT "NEDD4-2 (neural precursor cell expressed, developmentally down-regulated RT 4-2) negatively regulates TGF-beta (transforming growth factor-beta) RT signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta RT type I receptor."; RL Biochem. J. 386:461-470(2005). RN [9] RP UBIQUITINATION. RX PubMed=23610558; DOI=10.1371/journal.pbio.1001538; RA Kelly C.E., Thymiakou E., Dixon J.E., Tanaka S., Godwin J., Episkopou V.; RT "Rnf165/Ark2C enhances BMP-Smad signaling to mediate motor axon RT extension."; RL PLoS Biol. 11:E1001538-E1001538(2013). CC -!- FUNCTION: Antagonist of signaling by TGF-beta (transforming growth CC factor) type 1 receptor superfamily members; has been shown to inhibit CC TGF-beta (Transforming growth factor) and activin signaling by CC associating with their receptors thus preventing SMAD2 access. CC Functions as an adapter to recruit SMURF2 to the TGF-beta receptor CC complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, CC which promotes its dephosphorylation. Positively regulates PDPK1 kinase CC activity by stimulating its dissociation from the 14-3-3 protein YWHAQ CC which acts as a negative regulator. {ECO:0000250|UniProtKB:O15105}. CC -!- SUBUNIT: Interacts with COPS5. Interacts with STAMBP. Interacts with CC PPP1R15A (By similarity). Interacts with NEDD4L. Interacts with RNF111, CC AXIN1 and AXIN2. Interacts with ACVR1B, SMURF1, SMURF2 and TGFBR1; CC SMAD7 recruits SMURF1 and SMURF2 to the TGF-beta receptor and regulates CC its degradation (By similarity). Interacts with WWP1. Interacts with CC PDPK1 (via PH domain) (By similarity). Ubiquitinated by WWP1. Interacts CC with TSC22D1/TSC-22; the interaction requires TGF-beta and the CC interaction is inhibited by TGFBR1 (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:14657019, CC ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:15496141}. CC -!- INTERACTION: CC O35253; O35625: Axin1; NbExp=2; IntAct=EBI-5274835, EBI-2365912; CC O35253; Q923E4: Sirt1; NbExp=6; IntAct=EBI-5274835, EBI-1802585; CC O35253; Q9C0C9: UBE2O; Xeno; NbExp=2; IntAct=EBI-5274835, EBI-2339946; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11278814, CC ECO:0000269|PubMed:15496141}. Cytoplasm {ECO:0000269|PubMed:11278814, CC ECO:0000269|PubMed:15496141}. Note=Interaction with NEDD4L or RNF111 CC induces translocation from the nucleus to the cytoplasm CC (PubMed:15496141). TGF-beta stimulates its translocation from the CC nucleus to the cytoplasm. PDPK1 inhibits its translocation from the CC nucleus to the cytoplasm in response to TGF-beta (By similarity). CC {ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:15496141}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=O35253-1; Sequence=Displayed; CC Name=B; CC IsoId=O35253-2; Sequence=VSP_006181; CC -!- TISSUE SPECIFICITY: Ubiquitous in various organs, with higher levels in CC brain and kidney. CC -!- PTM: Phosphorylation on Ser-249 does not affect its stability, nuclear CC localization or inhibitory function in TGFB signaling; however it CC affects its ability to regulate transcription (PubMed:11278814). CC Phosphorylated by PDPK1 (By similarity). {ECO:0000250|UniProtKB:O15105, CC ECO:0000269|PubMed:11278814}. CC -!- PTM: Ubiquitinated by WWP1 (PubMed:15221015). Polyubiquitinated by CC RNF111, which is enhanced by AXIN1 and promotes proteasomal degradation CC (PubMed:14657019). In response to TGF-beta, ubiquitinated by SMURF1; CC which promotes its degradation (By similarity). Ubiquitinated by ARK2C, CC promoting proteasomal degradation, leading to enhance the BMP-Smad CC signaling (PubMed:23610558). {ECO:0000250|UniProtKB:O15105, CC ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:15221015, CC ECO:0000269|PubMed:23610558}. CC -!- PTM: Acetylation prevents ubiquitination and degradation mediated by CC SMURF1. {ECO:0000250|UniProtKB:O15105}. CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {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; AF015260; AAB81353.1; -; mRNA. DR EMBL; AJ000550; CAA04182.1; -; mRNA. DR EMBL; AJ000551; CAA04183.1; -; mRNA. DR CCDS; CCDS37860.1; -. [O35253-1] DR RefSeq; NP_001036125.1; NM_001042660.1. [O35253-1] DR RefSeq; XP_006525766.1; XM_006525703.2. [O35253-2] DR PDB; 7CD1; X-ray; 1.89 A; A/B/C/D=247-426. DR PDBsum; 7CD1; -. DR AlphaFoldDB; O35253; -. DR BMRB; O35253; -. DR SMR; O35253; -. DR BioGRID; 201280; 27. DR IntAct; O35253; 8. DR MINT; O35253; -. DR STRING; 10090.ENSMUSP00000026999; -. DR iPTMnet; O35253; -. DR PhosphoSitePlus; O35253; -. DR PaxDb; 10090-ENSMUSP00000026999; -. DR ProteomicsDB; 257257; -. [O35253-1] DR ProteomicsDB; 257258; -. [O35253-2] DR Antibodypedia; 9268; 637 antibodies from 39 providers. DR DNASU; 17131; -. DR Ensembl; ENSMUST00000026999.10; ENSMUSP00000026999.4; ENSMUSG00000025880.12. [O35253-1] DR Ensembl; ENSMUST00000168918.8; ENSMUSP00000129322.2; ENSMUSG00000025880.12. [O35253-1] DR GeneID; 17131; -. DR KEGG; mmu:17131; -. DR UCSC; uc008fqd.1; mouse. [O35253-1] DR UCSC; uc008fqe.2; mouse. [O35253-2] DR AGR; MGI:1100518; -. DR CTD; 4092; -. DR MGI; MGI:1100518; Smad7. DR VEuPathDB; HostDB:ENSMUSG00000025880; -. DR eggNOG; KOG3701; Eukaryota. DR GeneTree; ENSGT00940000159872; -. DR HOGENOM; CLU_026736_2_0_1; -. DR InParanoid; O35253; -. DR OMA; GGRGCCM; -. DR OrthoDB; 2916296at2759; -. DR PhylomeDB; O35253; -. DR TreeFam; TF314923; -. DR Reactome; R-MMU-201451; Signaling by BMP. DR Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling. DR Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription. DR Reactome; R-MMU-5689880; Ub-specific processing proteases. DR BioGRID-ORCS; 17131; 13 hits in 82 CRISPR screens. DR ChiTaRS; Smad7; mouse. DR PRO; PR:O35253; -. DR Proteomes; UP000000589; Chromosome 18. DR RNAct; O35253; Protein. DR Bgee; ENSMUSG00000025880; Expressed in molar tooth and 269 other cell types or tissues. DR ExpressionAtlas; O35253; baseline and differential. DR GO; GO:0005912; C:adherens junction; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0001650; C:fibrillar center; ISO:MGI. DR GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0070697; F:activin receptor binding; ISO:MGI. DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI. DR GO; GO:0005518; F:collagen binding; IPI:MGI. DR GO; GO:0070411; F:I-SMAD binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI. DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:MGI. DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISO:MGI. DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISO:MGI. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0034333; P:adherens junction assembly; ISO:MGI. DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central. DR GO; GO:0048844; P:artery morphogenesis; IMP:BHF-UCL. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:BHF-UCL. DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI. DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISO:MGI. DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI. DR GO; GO:1902731; P:negative regulation of chondrocyte proliferation; IDA:CACAO. DR GO; GO:0030279; P:negative regulation of ossification; IDA:CACAO. DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL. DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:BHF-UCL. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI. DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IMP:BHF-UCL. DR GO; GO:0002725; P:negative regulation of T cell cytokine production; IMP:BHF-UCL. DR GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; IMP:BHF-UCL. DR GO; GO:2000317; P:negative regulation of T-helper 17 type immune response; IMP:BHF-UCL. DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:BHF-UCL. DR GO; GO:1903043; P:positive regulation of chondrocyte hypertrophy; IDA:CACAO. DR GO; GO:0050821; P:protein stabilization; ISO:MGI. DR GO; GO:0031503; P:protein-containing complex localization; ISO:MGI. DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL. DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISO:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI. DR GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IC:BHF-UCL. DR GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl. DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI. DR GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB. DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL. DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL. DR CDD; cd10494; MH1_SMAD_7; 1. DR CDD; cd10500; MH2_SMAD_7; 1. DR Gene3D; 2.60.200.10; -; 1. DR Gene3D; 3.90.520.10; SMAD MH1 domain; 1. DR InterPro; IPR013790; Dwarfin. DR InterPro; IPR003619; MAD_homology1_Dwarfin-type. DR InterPro; IPR013019; MAD_homology_MH1. DR InterPro; IPR017855; SMAD-like_dom_sf. DR InterPro; IPR001132; SMAD_dom_Dwarfin-type. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR InterPro; IPR036578; SMAD_MH1_sf. DR PANTHER; PTHR13703:SF44; MOTHERS AGAINST DECAPENTAPLEGIC HOMOLOG 7; 1. DR PANTHER; PTHR13703; SMAD; 1. DR Pfam; PF03165; MH1; 1. DR Pfam; PF03166; MH2; 1. DR SMART; SM00523; DWA; 1. DR SMART; SM00524; DWB; 1. DR SUPFAM; SSF56366; SMAD MH1 domain; 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS51075; MH1; 1. DR PROSITE; PS51076; MH2; 1. DR Genevisible; O35253; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation; Zinc. FT CHAIN 1..426 FT /note="Mothers against decapentaplegic homolog 7" FT /id="PRO_0000090873" FT DOMAIN 64..207 FT /note="MH1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438" FT DOMAIN 261..426 FT /note="MH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439" FT REGION 14..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 67..87 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 208..217 FT /note="Important for interaction with SMURF2" FT /evidence="ECO:0000250" FT MOTIF 208..211 FT /note="PY-motif" FT /evidence="ECO:0000250" FT BINDING 125 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 180 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 192 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 197 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT MOD_RES 64 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:O15105" FT MOD_RES 70 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:O15105" FT MOD_RES 249 FT /note="Phosphoserine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439, FT ECO:0000269|PubMed:11278814" FT CROSSLNK 64 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:O15105" FT CROSSLNK 70 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:O15105" FT VAR_SEQ 223 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|PubMed:10828018, ECO:0000303|Ref.3" FT /id="VSP_006181" FT MUTAGEN 249 FT /note="S->A: No effect on stability, nuclear localization FT or inhibitory function in TGFB signaling. Abolishes FT transcriptional activity." FT /evidence="ECO:0000269|PubMed:11278814" FT MUTAGEN 249 FT /note="S->D: No effect." FT /evidence="ECO:0000269|PubMed:11278814" FT CONFLICT 233 FT /note="A -> V (in Ref. 3 and 4)" FT /evidence="ECO:0000305" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 262..268 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 271..279 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 281..288 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 295..301 FT /evidence="ECO:0007829|PDB:7CD1" FT HELIX 308..317 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 321..326 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 329..334 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 340..343 FT /evidence="ECO:0007829|PDB:7CD1" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 352..354 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 358..360 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 365..369 FT /evidence="ECO:0007829|PDB:7CD1" FT HELIX 371..375 FT /evidence="ECO:0007829|PDB:7CD1" FT HELIX 383..387 FT /evidence="ECO:0007829|PDB:7CD1" FT HELIX 389..393 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 394..400 FT /evidence="ECO:0007829|PDB:7CD1" FT HELIX 412..414 FT /evidence="ECO:0007829|PDB:7CD1" FT STRAND 415..423 FT /evidence="ECO:0007829|PDB:7CD1" SQ SEQUENCE 426 AA; 46442 MW; BEEE751371C0E0CF CRC64; MFRTKRSALV RRLWRSRAPG GEDEEEGVGG GGGGGELRGE GATDGRAYGA GGGGAGRAGC CLGKAVRGAK GHHHPHPPTS GAGAAGGAEA DLKALTHSVL KKLKERQLEL LLQAVESRGG TRTACLLLPG RLDCRLGPGA PASAQPAQPP SSYSLPLLLC KVFRWPDLRH SSEVKRLCCC ESYGKINPEL VCCNPHHLSR LCELESPPPP YSRYPMDFLK PTAGCPDAVP SSAETGGTNY LAPGGLSDSQ LLLEPGDRSH WCVVAYWEEK TRVGRLYCVQ EPSLDIFYDL PQGNGFCLGQ LNSDNKSQLV QKVRSKIGCG IQLTREVDGV WVYNRSSYPI FIKSATLDNP DSRTLLVHKV FPGFSIKAFD YEKAYSLQRP NDHEFMQQPW TGFTVQISFV KGWGQCYTRQ FISSCPCWLE VIFNSR //