Search by BoMiProt ID - Bomi9818


Primary Information

BoMiProt ID Bomi9818
Protein Name Thrombospondin type-1 domain-containing protein 1
Organism Bos taurus
Uniprot IdQ5BIR3
Milk FractionWhey
Ref Sequence Id NP_001014967.1
Aminoacid Length 849
Molecular Weight 92050
Fasta Sequence https://www.uniprot.org/uniprot/Q5BIR3.fasta
Gene Name THSD1
Gene Id 541228
Protein Existence Status reviewed

Secondary Information

Protein Function THSD1 interacts with talin. Of note, talin inactivation in endothelial cells had been shown to cause severe hemorrhaging in mouse embryos.
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.
PTMs N-linked Glycosylation at Asn,Phosphorylation at Ser,Disulfide bond formation
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
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction 1TMH; (414-436)
Significance of PTMs With three conserved disulfide bridges and stacked tryptophan and arginine residues that stabilize the TSR structure.
Additional Comments THSD1 mutations perturb endothelial focal adhesions, cell morphology, and cell adhesion in ways that may contribute partially to IA(Intracranial aneurysm).
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.