TENS3_MOUSE
ID TENS3_MOUSE Reviewed; 1440 AA.
AC Q5SSZ5; Q3TZ54; Q8BJA7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Tensin-3;
DE AltName: Full=Tensin-like SH2 domain-containing protein 1;
GN Name=Tns3; Synonyms=Tens1;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-624 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15733665; DOI=10.1016/j.ydbio.2004.12.027;
RA Chiang M.-K., Liao Y.-C., Kuwabara Y., Lo S.H.;
RT "Inactivation of tensin3 in mice results in growth retardation and
RT postnatal lethality.";
RL Dev. Biol. 279:368-377(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687; SER-690 AND SER-769, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-361; SER-370;
RP SER-571; SER-648; SER-690; SER-769; SER-894 AND SER-960, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in actin remodeling. Involved in the
CC dissociation of the integrin-tensin-actin complex. EGF activates TNS4
CC and down-regulates TNS3 which results in capping the tail of ITGB1.
CC Seems to be involved in mammary cell migration (By similarity). May be
CC involved in cell migration and bone development. {ECO:0000250,
CC ECO:0000269|PubMed:15733665}.
CC -!- SUBUNIT: EGF promotes the interaction with EGFR. Interacts with
CC PTK2/FAK1 and BCAR1. Tyrosine phosphorylation is critical for these
CC interactions (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SSZ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SSZ5-2; Sequence=VSP_027128;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung, liver, spleen,
CC kidney, stomach, small intestine, skeletal muscle, skin, thymus,
CC testis, uterus, placenta, aorta and trachea.
CC {ECO:0000269|PubMed:15733665}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 13.5 dpc in lung, liver, spleen,
CC stomach, aorta, trachea, and perichondrium.
CC {ECO:0000269|PubMed:15733665}.
CC -!- DISRUPTION PHENOTYPE: Mice display growth retardation and incomplete
CC development of small intestine, lung, and bone. Postnatal lethality is
CC detected in one third of the homozygous mutants.
CC {ECO:0000269|PubMed:15733665}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305}.
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DR EMBL; AK089717; BAC40948.1; -; mRNA.
DR EMBL; AK158101; BAE34356.1; -; mRNA.
DR EMBL; AL603845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36109.1; -. [Q5SSZ5-1]
DR RefSeq; NP_001077056.1; NM_001083587.1. [Q5SSZ5-1]
DR RefSeq; XP_006514804.1; XM_006514741.2. [Q5SSZ5-1]
DR RefSeq; XP_011242030.1; XM_011243728.2. [Q5SSZ5-1]
DR RefSeq; XP_017170096.1; XM_017314607.1.
DR AlphaFoldDB; Q5SSZ5; -.
DR SMR; Q5SSZ5; -.
DR BioGRID; 235637; 7.
DR IntAct; Q5SSZ5; 1.
DR STRING; 10090.ENSMUSP00000020695; -.
DR iPTMnet; Q5SSZ5; -.
DR PhosphoSitePlus; Q5SSZ5; -.
DR SwissPalm; Q5SSZ5; -.
DR jPOST; Q5SSZ5; -.
DR MaxQB; Q5SSZ5; -.
DR PaxDb; Q5SSZ5; -.
DR PeptideAtlas; Q5SSZ5; -.
DR PRIDE; Q5SSZ5; -.
DR ProteomicsDB; 262869; -. [Q5SSZ5-1]
DR ProteomicsDB; 262870; -. [Q5SSZ5-2]
DR Antibodypedia; 1019; 146 antibodies from 26 providers.
DR DNASU; 319939; -.
DR Ensembl; ENSMUST00000020695; ENSMUSP00000020695; ENSMUSG00000020422. [Q5SSZ5-1]
DR GeneID; 319939; -.
DR KEGG; mmu:319939; -.
DR UCSC; uc007hzj.1; mouse. [Q5SSZ5-2]
DR UCSC; uc007hzk.1; mouse. [Q5SSZ5-1]
DR CTD; 64759; -.
DR MGI; MGI:2443012; Tns3.
DR VEuPathDB; HostDB:ENSMUSG00000020422; -.
DR eggNOG; KOG1930; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000156328; -.
DR HOGENOM; CLU_002189_1_0_1; -.
DR InParanoid; Q5SSZ5; -.
DR OMA; STHTWVC; -.
DR OrthoDB; 172407at2759; -.
DR PhylomeDB; Q5SSZ5; -.
DR TreeFam; TF315996; -.
DR Reactome; R-MMU-8875513; MET interacts with TNS proteins.
DR BioGRID-ORCS; 319939; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Tns3; mouse.
DR PRO; PR:Q5SSZ5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SSZ5; protein.
DR Bgee; ENSMUSG00000020422; Expressed in humerus cartilage element and 244 other tissues.
DR ExpressionAtlas; Q5SSZ5; baseline and differential.
DR Genevisible; Q5SSZ5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035012; Tensin-like_SH2.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR033929; Tensin_PTB.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Phosphoprotein; Reference proteome;
KW SH2 domain.
FT CHAIN 1..1440
FT /note="Tensin-3"
FT /id="PRO_0000295916"
FT DOMAIN 1..170
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 175..301
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 1167..1277
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 358..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..865
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ2"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ2"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 632
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ2"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 773
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ2"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ2"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ2"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ2"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ2"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ2"
FT MOD_RES 1436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68CZ2"
FT VAR_SEQ 1..890
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027128"
FT CONFLICT 910
FT /note="T -> A (in Ref. 1; BAE34356)"
FT /evidence="ECO:0000305"
FT CONFLICT 1025
FT /note="V -> I (in Ref. 1; BAE34356)"
FT /evidence="ECO:0000305"
FT CONFLICT 1051
FT /note="L -> M (in Ref. 1; BAE34356)"
FT /evidence="ECO:0000305"
FT CONFLICT 1067
FT /note="T -> M (in Ref. 1; BAE34356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1440 AA; 155589 MW; 83A07D855EE0D463 CRC64;
MEDSHELDLT YVTERIIAVS FPASCSEESY LHSLQEVTRM LKCKHGDNYL VLNLSEKRYD
LTKLNPKIMD VGWPELHAPP LDKMCTICKA QESWLNNDPQ HVVVIHCRGG KGRIGVVISS
YMHFTNVSAS ADQALDRFAM KKFYDDKISA LMEPSQKRYV QFLSGLLSGA MKMNTSPLFL
HFVIMHGVPS FDTGGACRPF LKLYQAMQPV YTSGIYNVGS ENPSRIRIAI EPAQLLKGDI
MVKCYHKKFR SATRDVIFRL QFHTGAVQGY GLLFGKEELD SACKDDRFPD YGKIELVFSA
TPEKIQGSEH LYSDQGVTVD YNTADPLIRW DSYENMSADG EVLHTQGPVD GSLYAKVRKK
SASDTGIPSS PQGMPATSSP DHGDHTLSVS SDSGHSTASA RTDKTEERLT PGARRGLSPQ
EKAELDQLLS GFGLEDSASS HKDMTDMRSK YSGTRHVVPA QVHVNGDAAL KDRETDILDD
EMPHHDLHSV DSLGTLSSSE GPQSTHLGPF TCLKSSQNSL LSDGFGNGVA EDHNGVLSPD
LGLGVDTLYD RERMCGGREQ KPLQPLLRKP SAPTPVQAYG QSNYSTQTWV RQQQMVAAHQ
YSFASDGEAR LGSRSTVDNT GLAQPPPHIP VTPNRGASSR VAVQRGISNG PNPPDTQQLC
PGKALQPRFQ DDRVTNGVHQ EPNTGSSPGS PTLDIDQSIE QLNRLILELD PTFEPIPTHL
NALGISAVCP DGVGSGLRCS GRLDSVDGPG RSPGRQGDDP IGGRLRKLSI GQYDNDAASQ
VTFSKCGWGK AGVDPAPSLG SFSSPEDIKE TVITAYPSDL NMIDGRIPNS KESSMCLTPS
FPVSPETPYV KTSPRYPPFS PPEPQLSSPA SLHKGREPRG CPEIISHTVG MSESPVGPKP
TMLRADMPAT PNFQQVFASS CTVSSNGPGQ RRESPPSAER QWVESSPKST LTLLGNSHPS
ESPLGTHEFC SSGKDSPGLP CFQSSELQAS FHSHELSMSE PQGALPPAGS QTFLGFNTVT
TATSVLPPGE DAGTLLVNSH GTSPAPGTPL LTTGAADNGF LPHNFLTVSP GASSHHSPGL
QNQNVSLPGQ PPLPEKKRAS EGDRSLGSVS PSSSGFSSPH SGSTMSIPFP NVLPDFCKPS
EVASPLPDSP NDKLVIVKFV QDTSKFWYKA DISREQAIAM LKDKAPGSFI VRDSHSFRGA
YGLAMKVATP PPSVLHLNKK AGDLSNELVR HFLIECTPKG VRLKGCSNEP YFGSLTALVC
QHSITPLALP CKLLIPERDP LEEIAENSPQ TAANSAAELL KQGAACNVWY LNSVEMESLT
GHQAVQKALS MTLVQEPPPV STVVHFKVSA QGITLTDNQR KLFFRRHYPV SSVIFCALDP
QDRKWIKDGP SSKVFGFVAR KQGSATDNVC HLFAEHDPEQ PASAIVNFVS KVMIGSPKKI
