TSP3_HUMAN
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 03-AUG-2022, entry version 196.
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; 91.
DR ComplexPortal; CPX-1789; Thrombospondin 3 complex.
DR IntAct; P49746; 43.
DR MINT; P49746; -.
DR STRING; 9606.ENSP00000357362; -.
DR GlyConnect; 1806; 18 N-Linked glycans (2 sites).
DR GlyGen; P49746; 4 sites, 18 N-linked glycans (2 sites).
DR iPTMnet; P49746; -.
DR PhosphoSitePlus; P49746; -.
DR BioMuta; THBS3; -.
DR DMDM; 1717814; -.
DR EPD; P49746; -.
DR jPOST; P49746; -.
DR MassIVE; P49746; -.
DR PaxDb; P49746; -.
DR PeptideAtlas; P49746; -.
DR PRIDE; P49746; -.
DR ProteomicsDB; 4837; -.
DR ProteomicsDB; 56059; -. [P49746-1]
DR Antibodypedia; 34176; 210 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 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; 120983at2759; -.
DR PhylomeDB; P49746; -.
DR TreeFam; TF324917; -.
DR PathwayCommons; P49746; -.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR SignaLink; P49746; -.
DR BioGRID-ORCS; 7059; 20 hits in 1079 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 150 other tissues.
DR ExpressionAtlas; P49746; baseline and differential.
DR Genevisible; P49746; HS.
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 Gene3D; 4.10.1080.10; -; 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; IPR001791; Laminin_G.
DR InterPro; IPR024665; Thbs/COMP_coiled-coil.
DR InterPro; IPR028507; Thrombospondin-3.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR10199:SF89; PTHR10199:SF89; 1.
DR Pfam; PF11598; COMP; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 6.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF103647; SSF103647; 3.
DR SUPFAM; SSF49899; SSF49899; 2.
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; 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
