TSP4_HUMAN
ID TSP4_HUMAN Reviewed; 961 AA.
AC P35443; B2R909; Q86TG2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Thrombospondin-4;
DE Flags: Precursor;
GN Name=THBS4; Synonyms=TSP4;
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], AND VARIANT VAL-420.
RC TISSUE=Heart;
RX PubMed=8350346; DOI=10.1007/bf00556355;
RA Lawler J., Duquette M., Urry L., McHenry K., Smith T.F.;
RT "The evolution of the thrombospondin gene family.";
RL J. Mol. Evol. 36:509-516(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-420, AND SUBUNIT.
RX PubMed=7852353; DOI=10.1074/jbc.270.6.2809;
RA Lawler J., McHenry K., Duquette M., Derick L.;
RT "Characterization of human thrombospondin-4.";
RL J. Biol. Chem. 270:2809-2814(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-387.
RC TISSUE=Synovium;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-55; PRO-387; VAL-420
RP AND ILE-646.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PNS;
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 [6]
RP FUNCTION IN CELL PROLIFERATION, AND INTERACTION WITH PTBP3.
RX PubMed=19441079; DOI=10.1002/jcp.21817;
RA Sadvakassova G., Dobocan M.C., Difalco M.R., Congote L.F.;
RT "Regulator of differentiation 1 (ROD1) binds to the amphipathic C-terminal
RT peptide of thrombospondin-4 and is involved in its mitogenic activity.";
RL J. Cell. Physiol. 220:672-679(2009).
RN [7]
RP INTERACTION WITH ATF6.
RX PubMed=22682248; DOI=10.1016/j.cell.2012.03.050;
RA Lynch J.M., Maillet M., Vanhoutte D., Schloemer A., Sargent M.A.,
RA Blair N.S., Lynch K.A., Okada T., Aronow B.J., Osinska H., Prywes R.,
RA Lorenz J.N., Mori K., Lawler J., Robbins J., Molkentin J.D.;
RT "A thrombospondin-dependent pathway for a protective ER stress response.";
RL Cell 149:1257-1268(2012).
RN [8]
RP REVIEW.
RX PubMed=23287452; DOI=10.1161/circresaha.112.280560;
RA Doroudgar S., Glembotski C.C.;
RT "ATF6 [corrected] and thrombospondin 4: the dynamic duo of the adaptive
RT endoplasmic reticulum stress response.";
RL Circ. Res. 112:9-12(2013).
RN [9]
RP ERRATUM OF PUBMED:23287452.
RX DOI=10.1161/RES.0b013e318286c21f;
RA Doroudgar S., Glembotski C.C.;
RL Circ. Res. 112:E31-E31(2013).
RN [10]
RP REVIEW.
RX PubMed=23892609; DOI=10.1097/mol.0b013e3283642912;
RA Stenina-Adognravi O.;
RT "Thrombospondins: old players, new games.";
RL Curr. Opin. Lipidol. 24:401-409(2013).
RN [11]
RP VARIANT PRO-387.
RX PubMed=22011848; DOI=10.1160/th11-03-0206;
RA Corsetti J.P., Ryan D., Moss A.J., McCarthy J., Goldenberg I., Zareba W.,
RA Sparks C.E.;
RT "Thrombospondin-4 polymorphism (A387P) predicts cardiovascular risk in
RT postinfarction patients with high HDL cholesterol and C-reactive protein
RT levels.";
RL Thromb. Haemost. 106:1170-1178(2011).
CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions and is involved in various processes including
CC cellular proliferation, migration, adhesion and attachment,
CC inflammatory response to CNS injury, regulation of vascular
CC inflammation and adaptive responses of the heart to pressure overload
CC and in myocardial function and remodeling. Binds to structural
CC extracellular matrix (ECM) proteins and modulates the ECM in response
CC to tissue damage, contributing to cardioprotective and adaptive ECM
CC remodeling. Plays a role in ER stress response, via its interaction
CC with the activating transcription factor 6 alpha (ATF6) which produces
CC adaptive ER stress response factors and protects myocardium from
CC pressure overload. May contribute to spinal presynaptic
CC hypersensitivity and neuropathic pain states after peripheral nerve
CC injury. May play a role in regulating protective astrogenesis from the
CC subventricular zone (SVZ) niche after injury in a NOTCH1-dependent
CC manner (By similarity). {ECO:0000250, ECO:0000269|PubMed:19441079}.
CC -!- SUBUNIT: Homopentamer; disulfide-linked. Interacts with PTBP3.
CC Interacts with NOTCH1 (By similarity). Interacts (via EGF-like 3;
CC calcium-binding domain) with ATF6 and facilitates its processing,
CC activation and nuclear translocation. {ECO:0000250,
CC ECO:0000269|PubMed:19441079, ECO:0000269|PubMed:22682248,
CC ECO:0000269|PubMed:7852353}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Z1T2}. Sarcoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted
CC {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted, extracellular space
CC {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000250|UniProtKB:Q9Z1T2}.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/thbs4/";
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DR EMBL; Z19585; CAA79635.1; -; mRNA.
DR EMBL; AK313587; BAG36356.1; -; mRNA.
DR EMBL; AY566253; AAS66982.1; -; Genomic_DNA.
DR EMBL; BC050456; AAH50456.1; -; mRNA.
DR CCDS; CCDS4049.1; -.
DR PIR; A55710; TSHUP4.
DR RefSeq; NP_001293141.1; NM_001306212.1.
DR RefSeq; NP_001293142.1; NM_001306213.1.
DR RefSeq; NP_001293143.1; NM_001306214.1.
DR RefSeq; NP_003239.2; NM_003248.5.
DR AlphaFoldDB; P35443; -.
DR SMR; P35443; -.
DR BioGRID; 112918; 4.
DR ComplexPortal; CPX-1790; Thrombospondin 4 complex.
DR IntAct; P35443; 2.
DR STRING; 9606.ENSP00000339730; -.
DR GlyGen; P35443; 5 sites, 3 O-linked glycans (3 sites).
DR iPTMnet; P35443; -.
DR PhosphoSitePlus; P35443; -.
DR BioMuta; THBS4; -.
DR DMDM; 55977790; -.
DR CPTAC; non-CPTAC-2703; -.
DR jPOST; P35443; -.
DR MassIVE; P35443; -.
DR MaxQB; P35443; -.
DR PaxDb; P35443; -.
DR PeptideAtlas; P35443; -.
DR PRIDE; P35443; -.
DR ProteomicsDB; 55063; -.
DR Antibodypedia; 3891; 175 antibodies from 26 providers.
DR DNASU; 7060; -.
DR Ensembl; ENST00000350881.6; ENSP00000339730.2; ENSG00000113296.14.
DR GeneID; 7060; -.
DR KEGG; hsa:7060; -.
DR MANE-Select; ENST00000350881.6; ENSP00000339730.2; NM_003248.6; NP_003239.2.
DR UCSC; uc021yaw.2; human.
DR CTD; 7060; -.
DR DisGeNET; 7060; -.
DR GeneCards; THBS4; -.
DR HGNC; HGNC:11788; THBS4.
DR HPA; ENSG00000113296; Tissue enhanced (adipose tissue, heart muscle, smooth muscle, tongue).
DR MIM; 600715; gene.
DR neXtProt; NX_P35443; -.
DR OpenTargets; ENSG00000113296; -.
DR PharmGKB; PA36500; -.
DR VEuPathDB; HostDB:ENSG00000113296; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000155227; -.
DR InParanoid; P35443; -.
DR OMA; PRVPNRD; -.
DR OrthoDB; 120983at2759; -.
DR PhylomeDB; P35443; -.
DR TreeFam; TF324917; -.
DR PathwayCommons; P35443; -.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR SignaLink; P35443; -.
DR BioGRID-ORCS; 7060; 10 hits in 1067 CRISPR screens.
DR ChiTaRS; THBS4; human.
DR GeneWiki; THBS4; -.
DR GenomeRNAi; 7060; -.
DR Pharos; P35443; Tbio.
DR PRO; PR:P35443; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P35443; protein.
DR Bgee; ENSG00000113296; Expressed in calcaneal tendon and 181 other tissues.
DR ExpressionAtlas; P35443; baseline and differential.
DR Genevisible; P35443; HS.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0048266; P:behavioral response to pain; ISS:UniProtKB.
DR GO; GO:0071603; P:endothelial cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0051451; P:myoblast migration; IDA:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEP:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0034103; P:regulation of tissue remodeling; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
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; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR028974; TSP_type-3_rpt.
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; 3.
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; 4.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51234; TSP3; 8.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
KW Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Growth factor;
KW Mitogen; Reference proteome; Repeat; Sarcoplasmic reticulum; Secreted;
KW Signal; Tissue remodeling; Unfolded protein response.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..961
FT /note="Thrombospondin-4"
FT /id="PRO_0000035852"
FT DOMAIN 27..192
FT /note="Laminin G-like"
FT DOMAIN 286..325
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 326..363
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 379..419
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 420..462
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 463..495
FT /note="TSP type-3 1"
FT REPEAT 496..531
FT /note="TSP type-3 2"
FT REPEAT 532..554
FT /note="TSP type-3 3"
FT REPEAT 555..590
FT /note="TSP type-3 4"
FT REPEAT 591..613
FT /note="TSP type-3 5"
FT REPEAT 614..651
FT /note="TSP type-3 6"
FT REPEAT 652..691
FT /note="TSP type-3 7"
FT REPEAT 692..727
FT /note="TSP type-3 8"
FT DOMAIN 731..945
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 579..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 562..564
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 585..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..672
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 258
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 261
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 290..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 295..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 313..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 330..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 335..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 353..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 383..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 388..403
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 406..418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 424..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 432..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 450..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 477..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 487..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 523..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 546..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 582..602
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 605..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 643..663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 683..703
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 719..940
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VARIANT 55
FT /note="L -> Q (in dbSNP:rs17881847)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019951"
FT VARIANT 387
FT /note="A -> P (associated with a pro-atherogenic phenotype;
FT dbSNP:rs1866389)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:22011848, ECO:0000269|Ref.4"
FT /id="VAR_019952"
FT VARIANT 420
FT /note="A -> V (in dbSNP:rs17882372)"
FT /evidence="ECO:0000269|PubMed:7852353,
FT ECO:0000269|PubMed:8350346, ECO:0000269|Ref.4"
FT /id="VAR_019953"
FT VARIANT 646
FT /note="V -> I (in dbSNP:rs2229396)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019954"
FT VARIANT 737
FT /note="V -> I (in dbSNP:rs2229398)"
FT /id="VAR_052659"
FT CONFLICT 96
FT /note="N -> S (in Ref. 1; no nucleotide entry and 2;
FT CAA79635)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="P -> A (in Ref. 1; no nucleotide entry and 2;
FT CAA79635)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="V -> G (in Ref. 1; no nucleotide entry and 2;
FT CAA79635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 961 AA; 105869 MW; 18F867AA5FFDA54B CRC64;
MLAPRGAAVL LLHLVLQRWL AAGAQATPQV FDLLPSSSQR LNPGALLPVL TDPALNDLYV
ISTFKLQTKS SATIFGLYSS TDNSKYFEFT VMGRLNKAIL RYLKNDGKVH LVVFNNLQLA
DGRRHRILLR LSNLQRGAGS LELYLDCIQV DSVHNLPRAF AGPSQKPETI ELRTFQRKPQ
DFLEELKLVV RGSLFQVASL QDCFLQQSEP LAATGTGDFN RQFLGQMTQL NQLLGEVKDL
LRQQVKETSF LRNTIAECQA CGPLKFQSPT PSTVVPPAPP APPTRPPRRC DSNPCFRGVQ
CTDSRDGFQC GPCPEGYTGN GITCIDVDEC KYHPCYPGVH CINLSPGFRC DACPVGFTGP
MVQGVGISFA KSNKQVCTDI DECRNGACVP NSICVNTLGS YRCGPCKPGY TGDQIRGCKA
ERNCRNPELN PCSVNAQCIE ERQGDVTCVC GVGWAGDGYI CGKDVDIDSY PDEELPCSAR
NCKKDNCKYV PNSGQEDADR DGIGDACDED ADGDGILNEQ DNCVLIHNVD QRNSDKDIFG
DACDNCLSVL NNDQKDTDGD GRGDACDDDM DGDGIKNILD NCPKFPNRDQ RDKDGDGVGD
ACDSCPDVSN PNQSDVDNDL VGDSCDTNQD SDGDGHQDST DNCPTVINSA QLDTDKDGIG
DECDDDDDND GIPDLVPPGP DNCRLVPNPA QEDSNSDGVG DICESDFDQD QVIDRIDVCP
ENAEVTLTDF RAYQTVVLDP EGDAQIDPNW VVLNQGMEIV QTMNSDPGLA VGYTAFNGVD
FEGTFHVNTQ TDDDYAGFIF GYQDSSSFYV VMWKQTEQTY WQATPFRAVA EPGIQLKAVK
SKTGPGEHLR NSLWHTGDTS DQVRLLWKDS RNVGWKDKVS YRWFLQHRPQ VGYIRVRFYE
GSELVADSGV TIDTTMRGGR LGVFCFSQEN IIWSNLKYRC NDTIPEDFQE FQTQNFDRFD
N
