TSP1_HUMAN
ID TSP1_HUMAN Reviewed; 1170 AA.
AC P07996; A8K6H4; B4E3J7; B9EGH6; Q15667; Q59E99;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 251.
DE RecName: Full=Thrombospondin-1;
DE AltName: Full=Glycoprotein G {ECO:0000303|PubMed:6777381};
DE Flags: Precursor;
GN Name=THBS1; Synonyms=TSP, TSP1;
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=Endothelial cell;
RX PubMed=2430973; DOI=10.1083/jcb.103.5.1635;
RA Lawler J., Hynes R.O.;
RT "The structure of human thrombospondin, an adhesive glycoprotein with
RT multiple calcium-binding sites and homologies with several different
RT proteins.";
RL J. Cell Biol. 103:1635-1648(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-523.
RX PubMed=2918029; DOI=10.1083/jcb.108.2.729;
RA Hennessy S.W., Frazier B.A., Kim D.D., Deckwerth T.L., Baumgartel D.M.,
RA Rotwein P., Frazier W.A.;
RT "Complete thrombospondin mRNA sequence includes potential regulatory sites
RT in the 3' untranslated region.";
RL J. Cell Biol. 108:729-736(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-523.
RC TISSUE=Placenta, and Uterus;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-700.
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-397 (ISOFORM 1).
RX PubMed=3030396; DOI=10.1021/bi00374a014;
RA Kobayashi S., Eden-Mccutchan F., Framson P., Bornstein P.;
RT "Partial amino acid sequence of human thrombospondin as determined by
RT analysis of cDNA clones: homology to malarial circumsporozoite proteins.";
RL Biochemistry 25:8418-8425(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-374 (ISOFORM 1).
RX PubMed=3461443; DOI=10.1073/pnas.83.15.5449;
RA Dixit V.M., Hennessy S.W., Grant G.A., Rotwein P., Frazier W.A.;
RT "Characterization of a cDNA encoding the heparin and collagen binding
RT domains of human thrombospondin.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5449-5453(1986).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-166.
RX PubMed=2544587; DOI=10.1016/s0021-9258(18)60452-1;
RA Laherty C.D., Gierman T.M., Dixit V.M.;
RT "Characterization of the promoter region of the human thrombospondin gene.
RT DNA sequences within the first intron increase transcription.";
RL J. Biol. Chem. 264:11222-11227(1989).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1028-1170 (ISOFORM 1).
RA la Fleur M., Jobin C., Gauthier J., Kreis C.G.;
RT "Expression of thrombospondin in chronic inflammation: neutrophils from
RT synovial fluids synthesize a novel 3.9 kb TSP mRNA.";
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=6777381; DOI=10.1016/s0021-9258(19)70174-4;
RA Phillips D.R., Jennings L.K., Prasanna H.R.;
RT "Ca2+-mediated association of glycoprotein G (thrombin-sensitive protein,
RT thrombospondin) with human platelets.";
RL J. Biol. Chem. 255:11629-11632(1980).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=6341993; DOI=10.1073/pnas.80.4.998;
RA Jaffe E.A., Ruggiero J.T., Leung L.K., Doyle M.J., McKeown-Longo P.J.,
RA Mosher D.F.;
RT "Cultured human fibroblasts synthesize and secrete thrombospondin and
RT incorporate it into extracellular matrix.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:998-1002(1983).
RN [13]
RP INTERACTION WITH CD36.
RX PubMed=1371676; DOI=10.1016/0006-291x(92)91860-s;
RA Asch A.S., Silbiger S., Heimer E., Nachman R.L.;
RT "Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding.";
RL Biochem. Biophys. Res. Commun. 182:1208-1217(1992).
RN [14]
RP GLYCOSYLATION AT TRP-385; SER-394; TRP-438; TRP-441; THR-450; TRP-498 AND
RP THR-507.
RC TISSUE=Platelet;
RX PubMed=11067851; DOI=10.1074/jbc.m008073200;
RA Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J., Mosher D.F.,
RA Peter-Katalinic J.;
RT "C-mannosylation and O-fucosylation of the thrombospondin type 1 module.";
RL J. Biol. Chem. 276:6485-6498(2001).
RN [15]
RP INTERACTION WITH HRG, AND FUNCTION.
RX PubMed=11134179; DOI=10.1172/jci9061;
RA Simantov R., Febbraio M., Crombie R., Asch A.S., Nachman R.L.,
RA Silverstein R.L.;
RT "Histidine-rich glycoprotein inhibits the antiangiogenic effect of
RT thrombospondin-1.";
RL J. Clin. Invest. 107:45-52(2001).
RN [16]
RP DISULFIDE BONDS IN THROMBOSPONDIN DOMAIN.
RX PubMed=12450399; DOI=10.1021/bi026463u;
RA Huwiler K.G., Vestling M.M., Annis D.S., Mosher D.F.;
RT "Biophysical characterization, including disulfide bond assignments, of the
RT anti-angiogenic type 1 domains of human thrombospondin-1.";
RL Biochemistry 41:14329-14339(2002).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-248 AND ASN-1067.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-248.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [20]
RP INTERACTION WITH FN1.
RX PubMed=18042364; DOI=10.1016/j.matbio.2007.10.003;
RA Kuznetsova S.A., Mahoney D.J., Martin-Manso G., Ali T., Nentwich H.A.,
RA Sipes J.M., Zeng B., Vogel T., Day A.J., Roberts D.D.;
RT "TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin
RT and increases fibronectin matrix assembly.";
RL Matrix Biol. 27:201-210(2008).
RN [21]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
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 [24]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 434-546, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT THR-450 AND THR-507.
RX PubMed=12391027; DOI=10.1083/jcb.200206062;
RA Tan K., Duquette M., Liu J.-H., Dong Y., Zhang R., Joachimiak A.,
RA Lawler J., Wang J.-H.;
RT "Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and
RT its biological implication.";
RL J. Cell Biol. 159:373-382(2002).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 834-1170 IN COMPLEX WITH CALCIUM
RP IONS, DISULFIDE BONDS, MUTAGENESIS OF ASN-1067, GLYCOSYLATION AT ASN-1067,
RP CELL ATTACHMENT SITE, AND FUNCTION.
RX PubMed=15014436; DOI=10.1038/sj.emboj.7600166;
RA Kvansakul M., Adams J.C., Hohenester E.;
RT "Structure of a thrombospondin C-terminal fragment reveals a novel calcium
RT core in the type 3 repeats.";
RL EMBO J. 23:1223-1233(2004).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 19-233 IN COMPLEX WITH SYNTHETIC
RP PENTAMERIC HEPARIN, AND DISULFIDE BOND.
RX PubMed=16407063; DOI=10.1016/j.str.2005.09.017;
RA Tan K., Duquette M., Liu J.-H., Zhang R., Joachimiak A., Wang J.-H.,
RA Lawler J.;
RT "The structures of the thrombospondin-1 N-terminal domain and its complex
RT with a synthetic pentameric heparin.";
RL Structure 14:33-42(2006).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-257 IN COMPLEXES WITH HEPARIN,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND GLYCOSYLATION AT ASN-248.
RX PubMed=18065761; DOI=10.1074/jbc.m705203200;
RA Tan K., Duquette M., Liu J.-H., Shanmugasundaram K., Joachimiak A.,
RA Gallagher J.T., Rigby A.C., Wang J.-H., Lawler J.;
RT "Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1
RT N-terminal domain.";
RL J. Biol. Chem. 283:3932-3941(2008).
CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions. Binds heparin. May play a role in dentinogenesis
CC and/or maintenance of dentin and dental pulp (By similarity). Ligand
CC for CD36 mediating antiangiogenic properties. Plays a role in ER stress
CC response, via its interaction with the activating transcription factor
CC 6 alpha (ATF6) which produces adaptive ER stress response factors (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:11134179,
CC ECO:0000269|PubMed:15014436}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Interacts (via the TSP type I
CC repeats) with HRG; the interaction blocks the antiangiogenic effect of
CC THBS1 with CD36 (By similarity). Can bind to fibrinogen, fibronectin,
CC laminin, type V collagen and integrins alpha-V/beta-1, alpha-V/beta-3
CC and alpha-IIb/beta-3. Interacts (via the TSP type I repeats) with CD36;
CC the interaction conveys an antiangiogenic effect. Interacts with ATF6
CC (via lumenal domain) (By similarity). Interacts with FN1; this
CC interaction is enhanced by TNFAIP6, which may act as a bridging
CC molecule between FN1 and THBS1. {ECO:0000250,
CC ECO:0000269|PubMed:18042364}.
CC -!- INTERACTION:
CC P07996; P02751: FN1; NbExp=2; IntAct=EBI-2530274, EBI-1220319;
CC P07996; Q15113: PCOLCE; NbExp=3; IntAct=EBI-2530274, EBI-8869614;
CC P07996; P01137: TGFB1; NbExp=2; IntAct=EBI-2530274, EBI-779636;
CC PRO_0000035842; P16671: CD36; NbExp=2; IntAct=EBI-13915509, EBI-2808214;
CC PRO_0000035842; Q92743: HTRA1; NbExp=2; IntAct=EBI-13915509, EBI-352256;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6777381}. Cell
CC surface {ECO:0000269|PubMed:6777381}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000269|PubMed:6341993}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:P35441}. Sarcoplasmic reticulum
CC {ECO:0000250|UniProtKB:P35441}. Note=Secreted by thrombin-activated
CC platelets and binds to the cell surface in the presence of
CC extracellular Ca(2+) (PubMed:6777381). Incorporated into the
CC extracellular matrix of fibroblasts (PubMed:6341993). Also detected in
CC the endoplasmic reticulum and sarcoplasmic reticulum where it plays a
CC role in the ER stress response (By similarity).
CC {ECO:0000250|UniProtKB:P35441, ECO:0000269|PubMed:6341993,
CC ECO:0000269|PubMed:6777381}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P07996-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07996-2; Sequence=VSP_055757;
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93149.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/THBS1ID42548ch15q15.html";
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DR EMBL; X04665; CAA28370.1; -; mRNA.
DR EMBL; X14787; CAA32889.1; -; mRNA.
DR EMBL; AK291639; BAF84328.1; -; mRNA.
DR EMBL; AK304754; BAG65509.1; -; mRNA.
DR EMBL; AB209912; BAD93149.1; ALT_INIT; mRNA.
DR EMBL; AC037198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136469; AAI36470.1; -; mRNA.
DR EMBL; BC136470; AAI36471.1; -; mRNA.
DR EMBL; M25631; AAA36741.1; -; mRNA.
DR EMBL; M14326; AAA61237.1; ALT_SEQ; mRNA.
DR EMBL; J04835; AAA61178.1; -; Genomic_DNA.
DR EMBL; M99425; AAB59366.1; -; mRNA.
DR CCDS; CCDS32194.1; -. [P07996-1]
DR PIR; A26155; TSHUP1.
DR RefSeq; NP_003237.2; NM_003246.3. [P07996-1]
DR PDB; 1LSL; X-ray; 1.90 A; A=434-546.
DR PDB; 1UX6; X-ray; 1.90 A; A=834-1170.
DR PDB; 1Z78; X-ray; 1.80 A; A=19-233.
DR PDB; 1ZA4; X-ray; 1.90 A; A=19-257.
DR PDB; 2ERF; X-ray; 1.45 A; A=25-233.
DR PDB; 2ES3; X-ray; 1.85 A; A/B=25-233.
DR PDB; 2OUH; X-ray; 2.40 A; A/B=19-257.
DR PDB; 2OUJ; X-ray; 1.90 A; A=19-257.
DR PDB; 3R6B; X-ray; 2.40 A; A=434-547.
DR PDB; 5FOE; X-ray; 1.98 A; A/B=378-429.
DR PDBsum; 1LSL; -.
DR PDBsum; 1UX6; -.
DR PDBsum; 1Z78; -.
DR PDBsum; 1ZA4; -.
DR PDBsum; 2ERF; -.
DR PDBsum; 2ES3; -.
DR PDBsum; 2OUH; -.
DR PDBsum; 2OUJ; -.
DR PDBsum; 3R6B; -.
DR PDBsum; 5FOE; -.
DR AlphaFoldDB; P07996; -.
DR SMR; P07996; -.
DR BioGRID; 112915; 109.
DR ComplexPortal; CPX-1785; Thrombospondin 1 complex.
DR CORUM; P07996; -.
DR DIP; DIP-1037N; -.
DR IntAct; P07996; 29.
DR MINT; P07996; -.
DR STRING; 9606.ENSP00000260356; -.
DR BindingDB; P07996; -.
DR ChEMBL; CHEMBL4630810; -.
DR GlyConnect; 594; 88 N-Linked glycans (6 sites), 2 O-Linked glycans (3 sites).
DR GlyGen; P07996; 16 sites, 1 C-linked glycan (5 sites), 88 N-linked glycans (6 sites), 3 O-linked glycans (6 sites).
DR iPTMnet; P07996; -.
DR MetOSite; P07996; -.
DR PhosphoSitePlus; P07996; -.
DR SwissPalm; P07996; -.
DR BioMuta; THBS1; -.
DR DMDM; 117949802; -.
DR OGP; P07996; -.
DR CPTAC; non-CPTAC-1162; -.
DR EPD; P07996; -.
DR jPOST; P07996; -.
DR MassIVE; P07996; -.
DR MaxQB; P07996; -.
DR PaxDb; P07996; -.
DR PeptideAtlas; P07996; -.
DR PRIDE; P07996; -.
DR ProteomicsDB; 52058; -. [P07996-1]
DR ABCD; P07996; 6 sequenced antibodies.
DR Antibodypedia; 9950; 726 antibodies from 38 providers.
DR DNASU; 7057; -.
DR Ensembl; ENST00000260356.6; ENSP00000260356.5; ENSG00000137801.11. [P07996-1]
DR GeneID; 7057; -.
DR KEGG; hsa:7057; -.
DR MANE-Select; ENST00000260356.6; ENSP00000260356.5; NM_003246.4; NP_003237.2.
DR UCSC; uc001zkh.4; human. [P07996-1]
DR CTD; 7057; -.
DR DisGeNET; 7057; -.
DR GeneCards; THBS1; -.
DR HGNC; HGNC:11785; THBS1.
DR HPA; ENSG00000137801; Low tissue specificity.
DR MIM; 188060; gene.
DR neXtProt; NX_P07996; -.
DR OpenTargets; ENSG00000137801; -.
DR PharmGKB; PA36497; -.
DR VEuPathDB; HostDB:ENSG00000137801; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000155832; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR InParanoid; P07996; -.
DR OMA; RLCNDPE; -.
DR OrthoDB; 120983at2759; -.
DR PhylomeDB; P07996; -.
DR TreeFam; TF324917; -.
DR PathwayCommons; P07996; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR SignaLink; P07996; -.
DR SIGNOR; P07996; -.
DR BioGRID-ORCS; 7057; 10 hits in 1026 CRISPR screens.
DR ChiTaRS; THBS1; human.
DR EvolutionaryTrace; P07996; -.
DR GeneWiki; Thrombospondin_1; -.
DR GenomeRNAi; 7057; -.
DR Pharos; P07996; Tchem.
DR PRO; PR:P07996; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P07996; protein.
DR Bgee; ENSG00000137801; Expressed in stromal cell of endometrium and 188 other tissues.
DR ExpressionAtlas; P07996; baseline and differential.
DR Genevisible; P07996; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005577; C:fibrinogen complex; IDA:BHF-UCL.
DR GO; GO:0031091; C:platelet alpha granule; IDA:BHF-UCL.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; NAS:BHF-UCL.
DR GO; GO:0070052; F:collagen V binding; IDA:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR GO; GO:0070051; F:fibrinogen binding; IDA:BHF-UCL.
DR GO; GO:0017134; F:fibroblast growth factor binding; IDA:BHF-UCL.
DR GO; GO:0001968; F:fibronectin binding; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; NAS:BHF-UCL.
DR GO; GO:0005178; F:integrin binding; IMP:BHF-UCL.
DR GO; GO:0043236; F:laminin binding; IDA:BHF-UCL.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:BHF-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0043394; F:proteoglycan binding; TAS:BHF-UCL.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISS:BHF-UCL.
DR GO; GO:0048266; P:behavioral response to pain; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:BHF-UCL.
DR GO; GO:0016477; P:cell migration; IDA:BHF-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0034605; P:cellular response to heat; NAS:BHF-UCL.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0002544; P:chronic inflammatory response; IEP:BHF-UCL.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IDA:BHF-UCL.
DR GO; GO:0006955; P:immune response; IEP:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IDA:CACAO.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0002581; P:negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IDA:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IDA:BHF-UCL.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IDA:BHF-UCL.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0002605; P:negative regulation of dendritic cell antigen processing and presentation; IDA:BHF-UCL.
DR GO; GO:2001027; P:negative regulation of endothelial cell chemotaxis; IDA:MGI.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:BHF-UCL.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; TAS:BHF-UCL.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:BHF-UCL.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; TAS:BHF-UCL.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:BHF-UCL.
DR GO; GO:0010748; P:negative regulation of long-chain fatty acid import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; IDA:BHF-UCL.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; IDA:BHF-UCL.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; IGI:BHF-UCL.
DR GO; GO:0018149; P:peptide cross-linking; IDA:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IDA:BHF-UCL.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:BHF-UCL.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IDA:BHF-UCL.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISS:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:BHF-UCL.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:BHF-UCL.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; ISS:BHF-UCL.
DR GO; GO:0045727; P:positive regulation of translation; IDA:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IDA:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; NAS:BHF-UCL.
DR GO; GO:0032026; P:response to magnesium ion; IDA:BHF-UCL.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; TAS:BHF-UCL.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:BHF-UCL.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
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:SF78; PTHR10199:SF78; 1.
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 3D-structure; Alternative splicing; Calcium; Cell adhesion; Disulfide bond;
KW EGF-like domain; Endoplasmic reticulum; Extracellular matrix; Glycoprotein;
KW Heparin-binding; Reference proteome; Repeat; Sarcoplasmic reticulum;
KW Secreted; Signal; Unfolded protein response.
FT SIGNAL 1..18
FT CHAIN 19..1170
FT /note="Thrombospondin-1"
FT /id="PRO_0000035842"
FT DOMAIN 65..270
FT /note="Laminin G-like"
FT DOMAIN 316..373
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 379..429
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 435..490
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 492..547
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 547..587
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 646..690
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 691..726
FT /note="TSP type-3 1"
FT REPEAT 727..762
FT /note="TSP type-3 2"
FT REPEAT 763..785
FT /note="TSP type-3 3"
FT REPEAT 786..821
FT /note="TSP type-3 4"
FT REPEAT 822..844
FT /note="TSP type-3 5"
FT REPEAT 845..882
FT /note="TSP type-3 6"
FT REPEAT 883..918
FT /note="TSP type-3 7"
FT REPEAT 919..954
FT /note="TSP type-3 8"
FT DOMAIN 958..1170
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 47..95
FT /note="Heparin-binding"
FT REGION 839..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 926..928
FT /note="Cell attachment site"
FT /evidence="ECO:0000305"
FT COMPBIAS 841..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:16263699,
FT ECO:0000305|PubMed:16335952, ECO:0000305|PubMed:18065761"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:11067851"
FT /id="CAR_000205"
FT CARBOHYD 394
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:11067851"
FT /id="CAR_000206"
FT CARBOHYD 438
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:11067851"
FT /id="CAR_000207"
FT CARBOHYD 441
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:11067851"
FT /id="CAR_000208"
FT CARBOHYD 450
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:11067851,
FT ECO:0000269|PubMed:12391027"
FT /id="CAR_000209"
FT CARBOHYD 498
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:11067851"
FT /id="CAR_000210"
FT CARBOHYD 507
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:11067851,
FT ECO:0000269|PubMed:12391027"
FT /id="CAR_000211"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1067
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15014436,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:19159218"
FT DISULFID 171..232
FT /evidence="ECO:0000269|PubMed:16407063,
FT ECO:0000269|PubMed:18065761, ECO:0007744|PDB:1Z78,
FT ECO:0007744|PDB:2ERF, ECO:0007744|PDB:2ES3,
FT ECO:0007744|PDB:2OUH, ECO:0007744|PDB:2OUJ"
FT DISULFID 270
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 274
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 391..423
FT DISULFID 395..428
FT DISULFID 406..413
FT DISULFID 447..484
FT /evidence="ECO:0000269|PubMed:12391027,
FT ECO:0007744|PDB:1LSL"
FT DISULFID 451..489
FT /evidence="ECO:0000269|PubMed:12391027,
FT ECO:0007744|PDB:1LSL"
FT DISULFID 462..474
FT /evidence="ECO:0000269|PubMed:12391027,
FT ECO:0007744|PDB:1LSL"
FT DISULFID 504..541
FT /evidence="ECO:0000269|PubMed:12391027,
FT ECO:0007744|PDB:1LSL"
FT DISULFID 508..546
FT /evidence="ECO:0000269|PubMed:12391027,
FT ECO:0007744|PDB:1LSL"
FT DISULFID 519..531
FT /evidence="ECO:0000269|PubMed:12391027,
FT ECO:0007744|PDB:1LSL"
FT DISULFID 551..562
FT /evidence="ECO:0000250"
FT DISULFID 556..572
FT /evidence="ECO:0000250"
FT DISULFID 575..586
FT /evidence="ECO:0000250"
FT DISULFID 592..608
FT /evidence="ECO:0000250"
FT DISULFID 599..617
FT /evidence="ECO:0000250"
FT DISULFID 620..644
FT /evidence="ECO:0000250"
FT DISULFID 650..663
FT /evidence="ECO:0000250"
FT DISULFID 657..676
FT /evidence="ECO:0000250"
FT DISULFID 678..689
FT /evidence="ECO:0000250"
FT DISULFID 705..713
FT /evidence="ECO:0000250"
FT DISULFID 718..738
FT /evidence="ECO:0000250"
FT DISULFID 754..774
FT /evidence="ECO:0000250"
FT DISULFID 777..797
FT /evidence="ECO:0000250"
FT DISULFID 813..833
FT /evidence="ECO:0000250"
FT DISULFID 836..856
FT /evidence="ECO:0000269|PubMed:15014436,
FT ECO:0007744|PDB:1UX6"
FT DISULFID 874..894
FT /evidence="ECO:0000269|PubMed:15014436,
FT ECO:0007744|PDB:1UX6"
FT DISULFID 910..930
FT /evidence="ECO:0000269|PubMed:15014436,
FT ECO:0007744|PDB:1UX6"
FT DISULFID 946..1167
FT /evidence="ECO:0000269|PubMed:15014436,
FT ECO:0007744|PDB:1UX6"
FT VAR_SEQ 17..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055757"
FT VARIANT 24
FT /note="S -> A (in dbSNP:rs41515347)"
FT /id="VAR_052657"
FT VARIANT 523
FT /note="T -> A (in dbSNP:rs2292305)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:2918029"
FT /id="VAR_028938"
FT VARIANT 700
FT /note="N -> S (in dbSNP:rs2228262)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_028939"
FT MUTAGEN 1067
FT /note="N->K: Loss of N-glycosylation site."
FT /evidence="ECO:0000269|PubMed:15014436"
FT CONFLICT 4
FT /note="A -> S (in Ref. 3; BAG65509)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="A -> T (in Ref. 1; CAA28370 and 9; AAA61178)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="R -> I (in Ref. 3; BAG65509)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="C -> R (in Ref. 3; BAG65509)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="C -> Y (in Ref. 3; BAF84328)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="N -> D (in Ref. 3; BAG65509)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="F -> S (in Ref. 3; BAF84328)"
FT /evidence="ECO:0000305"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2ERF"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:2ERF"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2ERF"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2ERF"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:2ERF"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 150..161
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2ERF"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:2ERF"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2ERF"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:2ERF"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2ERF"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:2ERF"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:2ERF"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2OUH"
FT STRAND 394..403
FT /evidence="ECO:0007829|PDB:5FOE"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:5FOE"
FT STRAND 450..459
FT /evidence="ECO:0007829|PDB:1LSL"
FT STRAND 478..485
FT /evidence="ECO:0007829|PDB:1LSL"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:1LSL"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:1LSL"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:1LSL"
FT TURN 838..840
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 849..852
FT /evidence="ECO:0007829|PDB:1UX6"
FT TURN 854..856
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 865..867
FT /evidence="ECO:0007829|PDB:1UX6"
FT HELIX 869..871
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:1UX6"
FT HELIX 892..894
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 901..903
FT /evidence="ECO:0007829|PDB:1UX6"
FT HELIX 905..907
FT /evidence="ECO:0007829|PDB:1UX6"
FT TURN 909..912
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 924..926
FT /evidence="ECO:0007829|PDB:1UX6"
FT HELIX 928..930
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 937..939
FT /evidence="ECO:0007829|PDB:1UX6"
FT TURN 941..943
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 961..965
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 986..988
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 995..1014
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 1022..1031
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 1034..1043
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 1051..1053
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 1059..1067
FT /evidence="ECO:0007829|PDB:1UX6"
FT HELIX 1074..1081
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 1082..1084
FT /evidence="ECO:0007829|PDB:1UX6"
FT TURN 1087..1089
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 1090..1095
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 1107..1115
FT /evidence="ECO:0007829|PDB:1UX6"
FT TURN 1116..1119
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 1120..1127
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 1130..1134
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 1146..1154
FT /evidence="ECO:0007829|PDB:1UX6"
FT STRAND 1156..1167
FT /evidence="ECO:0007829|PDB:1UX6"
SQ SEQUENCE 1170 AA; 129383 MW; 74749B2418E0943B CRC64;
MGLAWGLGVL FLMHVCGTNR IPESGGDNSV FDIFELTGAA RKGSGRRLVK GPDPSSPAFR
IEDANLIPPV PDDKFQDLVD AVRAEKGFLL LASLRQMKKT RGTLLALERK DHSGQVFSVV
SNGKAGTLDL SLTVQGKQHV VSVEEALLAT GQWKSITLFV QEDRAQLYID CEKMENAELD
VPIQSVFTRD LASIARLRIA KGGVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTSVLL
TLDNNVVNGS SPAIRTNYIG HKTKDLQAIC GISCDELSSM VLELRGLRTI VTTLQDSIRK
VTEENKELAN ELRRPPLCYH NGVQYRNNEE WTVDSCTECH CQNSVTICKK VSCPIMPCSN
ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSTSCGNGIQ QRGRSCDSLN NRCEGSSVQT
RTCHIQECDK RFKQDGGWSH WSPWSSCSVT CGDGVITRIR LCNSPSPQMN GKPCEGEARE
TKACKKDACP INGGWGPWSP WDICSVTCGG GVQKRSRLCN NPTPQFGGKD CVGDVTENQI
CNKQDCPIDG CLSNPCFAGV KCTSYPDGSW KCGACPPGYS GNGIQCTDVD ECKEVPDACF
NHNGEHRCEN TDPGYNCLPC PPRFTGSQPF GQGVEHATAN KQVCKPRNPC TDGTHDCNKN
AKCNYLGHYS DPMYRCECKP GYAGNGIICG EDTDLDGWPN ENLVCVANAT YHCKKDNCPN
LPNSGQEDYD KDGIGDACDD DDDNDKIPDD RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN
HNPDQADTDN NGEGDACAAD IDGDGILNER DNCQYVYNVD QRDTDMDGVG DQCDNCPLEH
NPDQLDSDSD RIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN
DGIPDDKDNC RLVPNPDQKD SDGDGRGDAC KDDFDHDSVP DIDDICPENV DISETDFRRF
QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY DEFNAVDFSG TFFINTERDD
DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL
WHTGNTPGQV RTLWHDPRHI GWKDFTAYRW RLSHRPKTGF IRVVMYEGKK IMADSGPIYD
KTYAGGRLGL FVFSQEMVFF SDLKYECRDP
