SMAD7_MOUSE
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 03-AUG-2022, entry version 195.
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.
CC {ECO:0000250, ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:15221015,
CC 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
CC RNF165, promoting proteasomal degradation, leading to enhance the BMP-
CC Smad 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}.
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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; O35253; -.
DR PRIDE; O35253; -.
DR ProteomicsDB; 257257; -. [O35253-1]
DR ProteomicsDB; 257258; -. [O35253-2]
DR Antibodypedia; 9268; 536 antibodies from 39 providers.
DR DNASU; 17131; -.
DR Ensembl; ENSMUST00000026999; ENSMUSP00000026999; ENSMUSG00000025880. [O35253-1]
DR Ensembl; ENSMUST00000168918; ENSMUSP00000129322; ENSMUSG00000025880. [O35253-1]
DR GeneID; 17131; -.
DR KEGG; mmu:17131; -.
DR UCSC; uc008fqd.1; mouse. [O35253-1]
DR UCSC; uc008fqe.2; mouse. [O35253-2]
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; HPELVCC; -.
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; 12 hits in 77 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 265 other tissues.
DR ExpressionAtlas; O35253; baseline and differential.
DR Genevisible; O35253; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
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:0048185; F:activin 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070411; F:I-SMAD binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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:0030509; P:BMP signaling pathway; IBA:GO_Central.
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: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:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0030279; P:negative regulation of ossification; IDA:CACAO.
DR GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
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: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; ISO:MGI.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IMP:BHF-UCL.
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:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0031503; P:protein-containing complex localization; ISO:MGI.
DR GO; GO:0032925; P:regulation of activin receptor signaling pathway; 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: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 Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 3.90.520.10; -; 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; PTHR13703; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF03166; MH2; 1.
DR SMART; SM00523; DWA; 1.
DR SMART; SM00524; DWB; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56366; SSF56366; 1.
DR PROSITE; PS51075; MH1; 1.
DR PROSITE; PS51076; MH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; DNA-binding;
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
