Primary Information |
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| BoMiProt ID | Bomi9818 |
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| Protein Name | Thrombospondin type-1 domain-containing protein 1 |
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| Organism | Bos taurus |
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| Uniprot ID | Q5BIR3 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001014967.1 |
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| Aminoacid Length | 849 |
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| Molecular Weight | 92050 |
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| FASTA Sequence |
Download |
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| Gene Name | THSD1 |
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| Gene ID | 541228 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | THSD1 interacts with talin. Of note, talin inactivation in endothelial cells had been shown to cause severe hemorrhaging in mouse embryos. |
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| Biochemical Properties | THSD1 shares some similarities to PKD1 and PKD2 which can form a complex that is involved in focal adhesion and cell–extracellular matrix interactions. |
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| PTMs | N-linked Glycosylation at Asn,Phosphorylation at Ser,Disulfide bond formation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q5BIR3|THSD1_BOVIN Thrombospondin type-1 domain-containing protein 1 OS=Bos taurus OX=9913 GN=THSD1 PE=2 SV=1
MKQTLKDFSNLLLVVLCDYVLGEAEHLVLGEPGHVALSN*39STVTVDFHGAN*50GTLRN*55VSVLL
VEASSN*66QTLTTKYLLTN*77QSQGTLEFECFYFKEAGDYWFVMTREATN*106SSLPVPPRERSAFL
KVEWPVFHVDLSRTSMAAEGTFQVGLFTSQPLCPFPGDKPDILLEVTFTNSLPEARAGQA
LPLEIRASKRVELAQGQWVEFDCPPVGPEAYVTVTVVLKLLGRDSVIMSTGPIDLAQKFG
YKLVMEPELTCEAGVEVTVLPPPCIFVQGVIAVFKEAPRLPGERTNRLAENSLALGERRT
GFN*303CTLFDMGRNKYCFDFGVSSQSQFSAKEKECMLIRRSIETWGLWQPWSQCSASCGDGV
RERRRVCLTSSPSRPGCPGMSSETSPCSLEDCAAFQPSSPSPLQPQAPVKSNNVVTVTGI
SLCLFIIVATVLITLWRKLGRAPKCSTPARHNSLHGPGCRKNS*463DEENICELSEPRGSFSD
AGDGPAGSPGDPGIPLTYRRSVPAPPDDEASGSESFQANAQKIIPPLFSYRLAQQQLKEM
KKKGLTETTKVYHVSQSPLTDTAIDAAATAAAAAAASPGGSESPEEAAAGKFRIKSPFLE
HPPTVGAGDRPPSRLDHPFSAASCAVSPSQTLLRKSQVRSHSRGSHFRRTASFHEARQAR
PFRERSLSTLTPRPTPAHGPRARTWDQAGERGRPPSRGTALFPEKRDHGPGAAGASGPLS
PLPKPHSLGPPPRKPDLGDRQAGFVGAGERPEPPRARRGPSPSHRSVSRKQPSPPAPKDG
YQRVSPLSPSQGRKDKCQSFPAHPEFAFYDNTSFGLTEAEQRMLDLPGYFGSNEEDETTS
TLSVEKLVI
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH; (414-436) |
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| Significance of PTMs | With three conserved disulfide bridges and stacked tryptophan and arginine residues that stabilize the TSR structure. |
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| Additional Comments | THSD1 mutations perturb endothelial focal adhesions, cell morphology, and cell adhesion in ways that may contribute partially to IA(Intracranial aneurysm). |
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| Bibliography | 1.. Drummond IA. Polycystins, focal adhesions and extracellular matrix interactions. Biochim Biophys Acta. 2011;1812:1322–1326. doi:10.1016/j.bbadis.2011.03.003. 2.Hassane S, Claij N, Lantinga-van Leeuwen IS, Van Munsteren JC,Van Lent N, Hanemaaijer R, et al. Pathogenic sequence for dissecting aneurysm formation in a hypomorphic polycystic kidney disease 1 mouse model. Arterioscler Thromb Vasc Biol. 2007;27:2177–2183. doi:10.1161/ATVBAHA.107.149252. 3.Monkley SJ, Kostourou V, Spence L, Petrich B, Coleman S, Ginsberg
MH, et al. Endothelial cell talin1 is essential for embryonic angiogenesis.
Dev Biol. 2011;349:494–502. doi: 10.1016/j.ydbio.2010.11.010. 4.Tan K, Duquette M, Liu JH, Dong Y, Zhang R, Joachimiak A, Lawler J and
Wang JH (2002) Crystal structure of the TSP-1 type 1 repeats: a novel
layered fold and its biological implication. The Journal of Cell Biology
159, 373–382. |
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