ID TSP3_HUMAN Reviewed; 956 AA. AC P49746; B1AVR8; B4DQ20; Q8WV34; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-OCT-2024, entry version 208. DE RecName: Full=Thrombospondin-3; DE Flags: Precursor; GN Name=THBS3; Synonyms=TSP3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=7558000; DOI=10.1006/geno.1995.1050; RA Adolph K.W., Long G.L., Winfield S., Ginns E.I., Bornstein P.; RT "Structure and organization of the human thrombospondin 3 gene (THBS3)."; RL Genomics 27:329-336(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-736. RX PubMed=9331372; DOI=10.1101/gr.7.10.1020; RA Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.; RT "Identification of three additional genes contiguous to the RT glucocerebrosidase locus on chromosome 1q21: implications for Gaucher RT disease."; RL Genome Res. 7:1020-1026(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 365-956. RC TISSUE=Retina; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP VARIANT [LARGE SCALE ANALYSIS] GLY-955. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to- CC matrix interactions. Can bind to fibrinogen, fibronectin, laminin and CC type V collagen. CC -!- SUBUNIT: Oligomer; disulfide-linked. CC -!- INTERACTION: CC P49746; P27797: CALR; NbExp=3; IntAct=EBI-2530931, EBI-1049597; CC P49746; P36957: DLST; NbExp=3; IntAct=EBI-2530931, EBI-351007; CC P49746; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-2530931, EBI-1055945; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P49746-1; Sequence=Displayed; CC Name=2; CC IsoId=P49746-2; Sequence=VSP_045328; CC -!- SIMILARITY: Belongs to the thrombospondin 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; L38969; AAC41762.1; -; mRNA. DR EMBL; AL713999; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF023268; AAC51818.1; -; Genomic_DNA. DR EMBL; AK298592; BAG60782.1; -; mRNA. DR EMBL; CH471121; EAW53110.1; -; Genomic_DNA. DR EMBL; BC018786; AAH18786.1; -; mRNA. DR CCDS; CCDS1099.1; -. [P49746-1] DR CCDS; CCDS58034.1; -. [P49746-2] DR PIR; A57121; A57121. DR RefSeq; NP_001239536.1; NM_001252607.1. DR RefSeq; NP_001239537.1; NM_001252608.1. [P49746-2] DR RefSeq; NP_009043.1; NM_007112.4. [P49746-1] DR AlphaFoldDB; P49746; -. DR SMR; P49746; -. DR BioGRID; 112917; 92. DR ComplexPortal; CPX-1789; Thrombospondin 3 complex. DR IntAct; P49746; 47. DR MINT; P49746; -. DR STRING; 9606.ENSP00000357362; -. DR GlyConnect; 1806; 18 N-Linked glycans (2 sites). DR GlyCosmos; P49746; 4 sites, 18 glycans. DR GlyGen; P49746; 6 sites, 18 N-linked glycans (2 sites), 2 O-linked glycans (2 sites). DR iPTMnet; P49746; -. DR PhosphoSitePlus; P49746; -. DR BioMuta; THBS3; -. DR DMDM; 1717814; -. DR jPOST; P49746; -. DR MassIVE; P49746; -. DR PaxDb; 9606-ENSP00000357362; -. DR PeptideAtlas; P49746; -. DR ProteomicsDB; 4837; -. DR ProteomicsDB; 56059; -. [P49746-1] DR Antibodypedia; 34176; 228 antibodies from 30 providers. DR DNASU; 7059; -. DR Ensembl; ENST00000368378.7; ENSP00000357362.3; ENSG00000169231.13. [P49746-1] DR Ensembl; ENST00000457183.6; ENSP00000392207.2; ENSG00000169231.13. [P49746-2] DR GeneID; 7059; -. DR KEGG; hsa:7059; -. DR MANE-Select; ENST00000368378.7; ENSP00000357362.3; NM_007112.5; NP_009043.1. DR UCSC; uc001fix.4; human. [P49746-1] DR AGR; HGNC:11787; -. DR CTD; 7059; -. DR DisGeNET; 7059; -. DR GeneCards; THBS3; -. DR HGNC; HGNC:11787; THBS3. DR HPA; ENSG00000169231; Low tissue specificity. DR MIM; 188062; gene. DR neXtProt; NX_P49746; -. DR OpenTargets; ENSG00000169231; -. DR PharmGKB; PA36499; -. DR VEuPathDB; HostDB:ENSG00000169231; -. DR eggNOG; ENOG502QRK8; Eukaryota. DR GeneTree; ENSGT00940000159283; -. DR HOGENOM; CLU_009257_1_1_1; -. DR InParanoid; P49746; -. DR OMA; NSMIHRT; -. DR OrthoDB; 5345349at2759; -. DR PhylomeDB; P49746; -. DR TreeFam; TF324917; -. DR PathwayCommons; P49746; -. DR Reactome; R-HSA-186797; Signaling by PDGF. DR SignaLink; P49746; -. DR BioGRID-ORCS; 7059; 24 hits in 1158 CRISPR screens. DR ChiTaRS; THBS3; human. DR GeneWiki; THBS3; -. DR GenomeRNAi; 7059; -. DR Pharos; P49746; Tbio. DR PRO; PR:P49746; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P49746; protein. DR Bgee; ENSG00000169231; Expressed in right uterine tube and 152 other cell types or tissues. DR ExpressionAtlas; P49746; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB. DR GO; GO:0008201; F:heparin binding; IDA:MGI. DR GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl. DR GO; GO:0007160; P:cell-matrix adhesion; NAS:UniProtKB. DR GO; GO:0003417; P:growth plate cartilage development; IEA:Ensembl. DR GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl. DR CDD; cd00054; EGF_CA; 2. DR CDD; cd16079; TSP-3cc; 1. DR Gene3D; 1.20.5.10; -; 1. DR Gene3D; 2.60.120.200; -; 2. DR Gene3D; 2.10.25.10; Laminin; 4. DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 2. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR049883; NOTCH1_EGF-like. DR InterPro; IPR003367; Thrombospondin_3-like_rpt. DR InterPro; IPR017897; Thrombospondin_3_rpt. DR InterPro; IPR008859; Thrombospondin_C. DR InterPro; IPR024665; TSP/COMP_coiled-coil. DR InterPro; IPR046970; TSP/COMP_coiled-coil_sf. DR InterPro; IPR028507; TSP3_coiled-coil. DR InterPro; IPR028974; TSP_type-3_rpt. DR InterPro; IPR048287; TSPN-like_N. DR PANTHER; PTHR10199; THROMBOSPONDIN; 1. DR PANTHER; PTHR10199:SF89; THROMBOSPONDIN-3; 1. DR Pfam; PF11598; COMP; 1. DR Pfam; PF07645; EGF_CA; 2. DR Pfam; PF02412; TSP_3; 5. DR Pfam; PF05735; TSP_C; 1. DR SMART; SM00181; EGF; 4. DR SMART; SM00179; EGF_CA; 2. DR SMART; SM00210; TSPN; 1. DR SUPFAM; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF103647; TSP type-3 repeat; 3. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 3. DR PROSITE; PS01187; EGF_CA; 2. DR PROSITE; PS51234; TSP3; 8. DR PROSITE; PS51236; TSP_CTER; 1. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cell adhesion; Disulfide bond; KW EGF-like domain; Glycoprotein; Proteomics identification; KW Reference proteome; Repeat; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..956 FT /note="Thrombospondin-3" FT /id="PRO_0000035849" FT DOMAIN 23..193 FT /note="Laminin G-like" FT DOMAIN 316..354 FT /note="EGF-like 1; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 370..410 FT /note="EGF-like 2; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 414..456 FT /note="EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REPEAT 457..491 FT /note="TSP type-3 1" FT REPEAT 492..527 FT /note="TSP type-3 2" FT REPEAT 528..550 FT /note="TSP type-3 3" FT REPEAT 551..586 FT /note="TSP type-3 4" FT REPEAT 587..609 FT /note="TSP type-3 5" FT REPEAT 610..647 FT /note="TSP type-3 6" FT REPEAT 648..687 FT /note="TSP type-3 7" FT REPEAT 688..723 FT /note="TSP type-3 8" FT DOMAIN 727..941 FT /note="TSP C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635" FT REGION 518..537 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 546..702 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 521..537 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 637..652 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 653..667 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 310 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 407 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 644 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 937 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 266 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 269 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 278..289 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 283..300 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 303..314 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 320..332 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 326..341 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 344..368 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 374..388 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 382..397 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 400..412 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 418..432 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 426..442 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 444..455 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 471..478 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 483..503 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 519..539 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 542..562 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 578..598 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 601..621 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 639..659 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 679..699 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 715..936 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT VAR_SEQ 96..215 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045328" FT VARIANT 279 FT /note="S -> G (in dbSNP:rs35154152)" FT /id="VAR_052658" FT VARIANT 955 FT /note="R -> G (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035808" SQ SEQUENCE 956 AA; 104201 MW; AE9B136DF0FFE5B8 CRC64; METQELRGAL ALLLLCFFTS ASQDLQVIDL LTVGESRQMV AVAEKIRTAL LTAGDIYLLS TFRLPPKQGG VLFGLYSRQD NTRWLEASVV GKINKVLVRY QREDGKVHAV NLQQAGLADG RTHTVLLRLR GPSRPSPALH LYVDCKLGDQ HAGLPALAPI PPAEVDGLEI RTGQKAYLRM QGFVESMKII LGGSMARVGA LSECPFQGDE SIHSAVTNAL HSILGEQTKA LVTQLTLFNQ ILVELRDDIR DQVKEMSLIR NTIMECQVCG FHEQRSHCSP NPCFRGVDCM EVYEYPGYRC GPCPPGLQGN GTHCSDINEC AHADPCFPGS SCINTMPGFH CEACPRGYKG TQVSGVGIDY ARASKQVCND IDECNDGNNG GCDPNSICTN TVGSFKCGPC RLGFLGNQSQ GCLPARTCHS PAHSPCHIHA HCLFERNGAV SCQCNVGWAG NGNVCGTDTD IDGYPDQALP CMDNNKHCKQ DNCLLTPNSG QEDADNDGVG DQCDDDADGD GIKNVEDNCR LFPNKDQQNS DTDSFGDACD NCPNVPNNDQ KDTDGNGEGD ACDNDVDGDG IPNGLDNCPK VPNPLQTDRD EDGVGDACDS CPEMSNPTQT DADSDLVGDV CDTNEDSDGD GHQDTKDNCP QLPNSSQLDS DNDGLGDECD GDDDNDGIPD YVPPGPDNCR LVPNPNQKDS DGNGVGDVCE DDFDNDAVVD PLDVCPESAE VTLTDFRAYQ TVVLDPEGDA QIDPNWVVLN QGMEIVQTMN SDPGLAVGYT AFNGVDFEGT FHVNTVTDDD YAGFLFSYQD SGRFYVVMWK QTEQTYWQAT PFRAVAQPGL QLKAVTSVSG PGEHLRNALW HTGHTPDQVR LLWTDPRNVG WRDKTSYRWQ LLHRPQVGYI RVKLYEGPQL VADSGVIIDT SMRGGRLGVF CFSQENIIWS NLQYRCNDTV PEDFEPFRRQ LLQGRV //