GenomeNet

Database: UniProt
Entry: P35441
LinkDB: P35441
Original site: P35441 
ID   TSP1_MOUSE              Reviewed;        1170 AA.
AC   P35441;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   13-FEB-2019, entry version 166.
DE   RecName: Full=Thrombospondin-1;
DE   AltName: Full=Glycoprotein G {ECO:0000250|UniProtKB:P07996};
DE   Flags: Precursor;
GN   Name=Thbs1; Synonyms=Tsp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1774063; DOI=10.1016/0888-7543(91)90066-N;
RA   Lawler J., Duquette M., Ferro P., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A.;
RT   "Characterization of the murine thrombospondin gene.";
RL   Genomics 11:587-600(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1371115;
RA   Laherty C.D., O'Rourke K., Wolf F.W., Katz R., Seldin M.F.,
RA   Dixit V.M.;
RT   "Characterization of mouse thrombospondin 2 sequence and expression
RT   during cell growth and development.";
RL   J. Biol. Chem. 267:3274-3281(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-490.
RX   PubMed=2398070;
RA   Bornstein P., Alfi D., Devarayalu S., Framson P., Li P.;
RT   "Characterization of the mouse thrombospondin gene and evaluation of
RT   the role of the first intron in human gene expression.";
RL   J. Biol. Chem. 265:16691-16698(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 19-37.
RX   PubMed=8654563; DOI=10.1016/0014-5793(96)00460-7;
RA   Chen H., Aeschlimann D., Nowlen J., Mosher D.F.;
RT   "Expression and initial characterization of recombinant mouse
RT   thrombospondin 1 and thrombospondin 3.";
RL   FEBS Lett. 387:36-41(1996).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND 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
RT   response.";
RL   Cell 149:1257-1268(2012).
CC   -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and
CC       cell-to-matrix interactions. Binds heparin. May play a role in
CC       dentinogenesis and/or maintenance of dentin and dental pulp.
CC       Ligand for CD36 mediating antiangiogenic properties (By
CC       similarity). Plays a role in ER stress response, via its
CC       interaction with the activating transcription factor 6 alpha
CC       (ATF6) which produces adaptive ER stress response factors.
CC       {ECO:0000250, ECO:0000269|PubMed:22682248}.
CC   -!- SUBUNIT: Homotrimer; disulfide-linked (By similarity). Can bind to
CC       fibrinogen, fibronectin, laminin, type V collagen and integrins
CC       alpha-V/beta-1, alpha-V/beta-3 and alpha-IIb/beta-3. Binds
CC       heparin. Interacts (via the TSP type I repeats) with CD36; the
CC       interaction conveys an antiangiogenic effect. Interacts (via the
CC       TSP type I repeats) with HRG; the interaction blocks the
CC       antiangiogenic effect of THBS1 with CD36 (By similarity).
CC       Interacts with ATF6 (via lumenal domain). {ECO:0000250,
CC       ECO:0000269|PubMed:22682248}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07996}.
CC       Cell surface {ECO:0000250|UniProtKB:P07996}. Secreted,
CC       extracellular space, extracellular matrix
CC       {ECO:0000250|UniProtKB:P07996}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:22682248}. Sarcoplasmic reticulum
CC       {ECO:0000269|PubMed:22682248}. Note=Secreted by thrombin-activated
CC       platelets and binds to the cell surface in the presence of
CC       extracellular Ca(2+) (By similarity). Incorporated into the
CC       extracellular matrix of fibroblasts (By similarity). Also detected
CC       in the endoplasmic reticulum and sarcoplasmic reticulum where it
CC       plays a role in the ER stress response (PubMed:22682248).
CC       {ECO:0000250|UniProtKB:P07996, ECO:0000269|PubMed:22682248}.
CC   -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
DR   EMBL; M62470; AAA50611.1; -; Genomic_DNA.
DR   EMBL; M62450; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62451; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62452; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62453; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62454; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62455; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62456; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62457; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62458; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62459; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62460; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62461; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62462; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62463; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62464; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62465; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62466; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62467; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62468; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M62469; AAA50611.1; JOINED; Genomic_DNA.
DR   EMBL; M87276; AAA53063.1; -; mRNA.
DR   EMBL; J05606; AAA40431.1; -; Genomic_DNA.
DR   EMBL; J05605; AAA40431.1; JOINED; Genomic_DNA.
DR   PIR; A40558; A40558.
DR   UniGene; Mm.4159; -.
DR   ProteinModelPortal; P35441; -.
DR   SMR; P35441; -.
DR   ComplexPortal; CPX-3022; Thrombospondin 1 complex.
DR   CORUM; P35441; -.
DR   IntAct; P35441; 4.
DR   MINT; P35441; -.
DR   STRING; 10090.ENSMUSP00000044903; -.
DR   GlyConnect; 667; -.
DR   iPTMnet; P35441; -.
DR   PhosphoSitePlus; P35441; -.
DR   SwissPalm; P35441; -.
DR   jPOST; P35441; -.
DR   MaxQB; P35441; -.
DR   PaxDb; P35441; -.
DR   PeptideAtlas; P35441; -.
DR   PRIDE; P35441; -.
DR   MGI; MGI:98737; Thbs1.
DR   eggNOG; ENOG410IFQQ; Eukaryota.
DR   eggNOG; ENOG410XQKE; LUCA.
DR   HOVERGEN; HBG018006; -.
DR   InParanoid; P35441; -.
DR   ChiTaRS; Thbs1; mouse.
DR   PRO; PR:P35441; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005577; C:fibrinogen complex; ISO:MGI.
DR   GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0030141; C:secretory granule; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0070052; F:collagen V binding; ISO:MGI.
DR   GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0070051; F:fibrinogen binding; ISO:MGI.
DR   GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
DR   GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR   GO; GO:0008201; F:heparin binding; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; ISO:MGI.
DR   GO; GO:0043236; F:laminin binding; ISO:MGI.
DR   GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:MGI.
DR   GO; GO:0001786; F:phosphatidylserine binding; ISO:MGI.
DR   GO; GO:0050431; F:transforming growth factor beta binding; ISO:MGI.
DR   GO; GO:0000187; P:activation of MAPK activity; ISO:MGI.
DR   GO; GO:0048266; P:behavioral response to pain; IMP:UniProtKB.
DR   GO; GO:0048514; P:blood vessel morphogenesis; IGI:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007050; P:cell cycle arrest; ISO:MGI.
DR   GO; GO:0016477; P:cell migration; ISO:MGI.
DR   GO; GO:0071732; P:cellular response to nitric oxide; IMP:MGI.
DR   GO; GO:0003197; P:endocardial cushion development; IGI:MGI.
DR   GO; GO:0043652; P:engulfment of apoptotic cell; ISO:MGI.
DR   GO; GO:0003417; P:growth plate cartilage development; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IDA:MGI.
DR   GO; GO:0002581; P:negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; ISO:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI.
DR   GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:MGI.
DR   GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; ISO:MGI.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR   GO; GO:0002605; P:negative regulation of dendritic cell antigen processing and presentation; ISO:MGI.
DR   GO; GO:2001027; P:negative regulation of endothelial cell chemotaxis; ISO:MGI.
DR   GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:MGI.
DR   GO; GO:0051918; P:negative regulation of fibrinolysis; ISO:MGI.
DR   GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; ISO:MGI.
DR   GO; GO:0032695; P:negative regulation of interleukin-12 production; ISO:MGI.
DR   GO; GO:0010748; P:negative regulation of long-chain fatty acid import across plasma membrane; ISO:MGI.
DR   GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; ISO:MGI.
DR   GO; GO:0010757; P:negative regulation of plasminogen activation; ISO:MGI.
DR   GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:MGI.
DR   GO; GO:0003151; P:outflow tract morphogenesis; IGI:MGI.
DR   GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR   GO; GO:0030194; P:positive regulation of blood coagulation; ISO:MGI.
DR   GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR   GO; GO:0050921; P:positive regulation of chemotaxis; ISO:MGI.
DR   GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:MGI.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR   GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR   GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:MGI.
DR   GO; GO:0043032; P:positive regulation of macrophage activation; ISO:MGI.
DR   GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:BHF-UCL.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR   GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISO:MGI.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR   GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; ISO:MGI.
DR   GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
DR   GO; GO:0009749; P:response to glucose; ISO:MGI.
DR   GO; GO:0032026; P:response to magnesium ion; ISO:MGI.
DR   GO; GO:0009612; P:response to mechanical stimulus; ISO:MGI.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   GO; GO:0002040; P:sprouting angiogenesis; ISO:MGI.
DR   Gene3D; 2.20.100.10; -; 3.
DR   Gene3D; 4.10.1080.10; -; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR037349; Thrombospondin.
DR   InterPro; IPR028499; Thrombospondin-1.
DR   InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR   InterPro; IPR017897; Thrombospondin_3_rpt.
DR   InterPro; IPR008859; Thrombospondin_C.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   InterPro; IPR028974; TSP_type-3_rpt.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR10199; PTHR10199; 2.
DR   PANTHER; PTHR10199:SF78; PTHR10199:SF78; 2.
DR   Pfam; PF00090; TSP_1; 3.
DR   Pfam; PF02412; TSP_3; 7.
DR   Pfam; PF05735; TSP_C; 1.
DR   Pfam; PF00093; VWC; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00209; TSP1; 3.
DR   SMART; SM00210; TSPN; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF103647; SSF103647; 3.
DR   SUPFAM; SSF49899; SSF49899; 2.
DR   SUPFAM; SSF82895; SSF82895; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS50092; TSP1; 3.
DR   PROSITE; PS51234; TSP3; 8.
DR   PROSITE; PS51236; TSP_CTER; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Endoplasmic reticulum;
KW   Extracellular matrix; Glycoprotein; Heparin-binding;
KW   Reference proteome; Repeat; Sarcoplasmic reticulum; Secreted; Signal;
KW   Unfolded protein response.
FT   SIGNAL        1     18       {ECO:0000269|PubMed:8654563}.
FT   CHAIN        19   1170       Thrombospondin-1.
FT                                /FTId=PRO_0000035843.
FT   DOMAIN       56    270       Laminin G-like.
FT   DOMAIN      316    373       VWFC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN      379    429       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      435    490       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      492    547       TSP type-1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      547    587       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      646    690       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      691    726       TSP type-3 1.
FT   REPEAT      727    762       TSP type-3 2.
FT   REPEAT      763    785       TSP type-3 3.
FT   REPEAT      786    821       TSP type-3 4.
FT   REPEAT      822    844       TSP type-3 5.
FT   REPEAT      845    882       TSP type-3 6.
FT   REPEAT      883    918       TSP type-3 7.
FT   REPEAT      919    954       TSP type-3 8.
FT   DOMAIN      958   1170       TSP C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00635}.
FT   REGION       47     95       Heparin-binding. {ECO:0000250}.
FT   MOTIF       926    928       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    248    248       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    360    360       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    708    708       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1067   1067       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19656770}.
FT   DISULFID    171    232       {ECO:0000250}.
FT   DISULFID    270    270       Interchain. {ECO:0000305}.
FT   DISULFID    274    274       Interchain. {ECO:0000305}.
FT   DISULFID    391    423       {ECO:0000250}.
FT   DISULFID    395    428       {ECO:0000250}.
FT   DISULFID    406    413       {ECO:0000250}.
FT   DISULFID    447    484       {ECO:0000250}.
FT   DISULFID    451    489       {ECO:0000250}.
FT   DISULFID    462    474       {ECO:0000250}.
FT   DISULFID    504    541       {ECO:0000250}.
FT   DISULFID    508    546       {ECO:0000250}.
FT   DISULFID    519    531       {ECO:0000250}.
FT   DISULFID    551    562       {ECO:0000250}.
FT   DISULFID    556    572       {ECO:0000250}.
FT   DISULFID    575    586       {ECO:0000250}.
FT   DISULFID    592    608       {ECO:0000250}.
FT   DISULFID    599    617       {ECO:0000250}.
FT   DISULFID    620    644       {ECO:0000250}.
FT   DISULFID    650    663       {ECO:0000250}.
FT   DISULFID    657    676       {ECO:0000250}.
FT   DISULFID    678    689       {ECO:0000250}.
FT   DISULFID    705    713       {ECO:0000250}.
FT   DISULFID    718    738       {ECO:0000250}.
FT   DISULFID    754    774       {ECO:0000250}.
FT   DISULFID    777    797       {ECO:0000250}.
FT   DISULFID    813    833       {ECO:0000250}.
FT   DISULFID    836    856       {ECO:0000250}.
FT   DISULFID    874    894       {ECO:0000250}.
FT   DISULFID    910    930       {ECO:0000250}.
FT   DISULFID    946   1167       {ECO:0000250}.
FT   CONFLICT   1025   1025       F -> L (in Ref. 2; AAA53063).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1170 AA;  129647 MW;  0443E493615E7F06 CRC64;
     MELLRGLGVL FLLHMCGSNR IPESGGDNGV FDIFELIGGA RRGPGRRLVK GQDLSSPAFR
     IENANLIPAV PDDKFQDLLD AVWADKGFIF LASLRQMKKT RGTLLAVERK DNTGQIFSVV
     SNGKAGTLDL SLSLPGKQQV VSVEEALLAT GQWKSITLFV QEDRAQLYID CDKMESAELD
     VPIQSIFTRD LASVARLRVA KGDVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTNVLL
     TLDNNVVNGS SPAIRTNYIG HKTKDLQAIC GLSCDELSSM VLELKGLRTI VTTLQDSIRK
     VTEENRELVS ELKRPPLCFH NGVQYKNNEE WTVDSCTECH CQNSVTICKK VSCPIMPCSN
     ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSATCGNGIQ QRGRSCDSLN NRCEGSSVQT
     RTCHIQECDK RFKQDGGWSH WSPWSSCSVT CGDGVITRIR LCNSPSPQMN GKPCEGEARE
     TKACKKDACP INGGWGPWSP WDICSVTCGG GVQRRSRLCN NPTPQFGGKD CVGDVTENQV
     CNKQDCPIDG CLSNPCFAGA KCTSYPDGSW KCGACPPGYS GNGIQCKDVD ECKEVPDACF
     NHNGEHRCKN TDPGYNCLPC PPRFTGSQPF GRGVEHAMAN KQVCKPRNPC TDGTHDCNKN
     AKCNYLGHYS DPMYRCECKP GYAGNGIICG EDTDLDGWPN ENLVCVANAT YHCKKDNCPN
     LPNSGQEDYD KDGIGDACDD DDDNDKIPDD RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN
     HNPDQADTDK NGEGDACAVD IDGDGILNER DNCQYVYNVD QRDTDMDGVG DQCDNCPLEH
     NPDQLDSDSD LIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN
     DGIPDDRDNC RLVPNPDQKD SDGDGRGDAC KDDFDHDNVP DIDDICPENF DISETDFRRF
     QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY DEFNAVDFSG TFFINTERDD
     DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL
     WHTGNTPGQV RTLWHDPRHI GWKDFTAYRW RLSHRPKTGY IRVVMYEGKK IMADSGPIYD
     KTYAGGRLGL FVFSQEMVFF SDMKYECRDS
//
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