Thrombospondin-1 precursor - Mus musculus (Mouse)

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P35441 (TSP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Thrombospondin-1

Gene names

Name:	Thbs1
Synonyms:	Tsp1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1170 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function

Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Binds heparin. May play a role in dentinogenesis and/or maintenance of dentin and dental pulp. Ligand for CD36 mediating antiangiogenic properties By similarity.

Subunit structure

Homotrimer; disulfide-linked By similarity. Can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1, alpha-V/beta-3 and alpha-IIb/beta-3. Binds heparin. Interacts (via the TSP type I repeats) with CD36; the interaction conveys an antiangiogenic effect. Interacts (via the TSP type I repeats) with HRG; the interaction blocks the antiangiogenic effect of THBS1 with CD36 By similarity.

Sequence similarities

Belongs to the thrombospondin family.

Contains 2 EGF-like domains.

Contains 1 laminin G-like domain.

Contains 1 TSP C-terminal (TSPC) domain.

Contains 3 TSP type-1 domains.

Contains 8 TSP type-3 repeats.

Contains 1 VWFC domain.

Ontologies

Keywords
Biological process	Cell adhesion
Domain	EGF-like domain Repeat Signal
Ligand	Calcium Heparin-binding
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood vessel morphogenesis Inferred from genetic interaction PubMed 20026598. Source: MGI cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW endocardial cushion development Inferred from genetic interaction PubMed 20026598. Source: MGI growth plate cartilage development Inferred from mutant phenotype PubMed 18467703. Source: MGI inflammatory response Inferred from mutant phenotype PubMed 15963261. Source: MGI negative regulation of angiogenesis Inferred from direct assay PubMed 12498716. Source: MGI outflow tract morphogenesis Inferred from genetic interaction PubMed 20026598. Source: MGI positive regulation of cell-substrate adhesion Inferred from direct assay PubMed 18757743. Source: MGI positive regulation of macrophage chemotaxis Inferred from mutant phenotype PubMed 18757424. Source: BHF-UCL positive regulation of transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype PubMed 9657149. Source: BHF-UCL
Cellular_component	extracellular space Inferred from direct assay PubMed 12498716. Source: MGI
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro extracellular matrix binding Inferred from direct assay PubMed 18757743. Source: MGI heparin binding Inferred from sequence orthology PubMed 8288588. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Ref.4

Chain

19 – 1170

1152

Thrombospondin-1

PRO_0000035843

Regions

Domain

56 – 270

215

Laminin G-like

Domain

316 – 373

VWFC

Domain

379 – 429

TSP type-1 1

Domain

435 – 490

TSP type-1 2

Domain

492 – 547

TSP type-1 3

Domain

547 – 587

EGF-like 1

Domain

646 – 690

EGF-like 2

Repeat

691 – 726

TSP type-3 1

Repeat

727 – 762

TSP type-3 2

Repeat

763 – 785

TSP type-3 3

Repeat

786 – 821

TSP type-3 4

Repeat

822 – 844

TSP type-3 5

Repeat

845 – 882

TSP type-3 6

Repeat

883 – 918

TSP type-3 7

Repeat

919 – 954

TSP type-3 8

Domain

958 – 1170

213

TSP C-terminal

Region

47 – 95

Heparin-binding By similarity

Motif

926 – 928

Cell attachment site Potential

Amino acid modifications

Glycosylation

248

N-linked (GlcNAc...) Potential

Glycosylation

360

N-linked (GlcNAc...) Potential

Glycosylation

708

N-linked (GlcNAc...) Potential

Glycosylation

1067

N-linked (GlcNAc...) Ref.5

Disulfide bond

171 ↔ 232

By similarity

Disulfide bond

270

Interchain Probable

Disulfide bond

274

Interchain Probable

Disulfide bond

391 ↔ 423

By similarity

Disulfide bond

395 ↔ 428

By similarity

Disulfide bond

406 ↔ 413

By similarity

Disulfide bond

447 ↔ 484

By similarity

Disulfide bond

451 ↔ 489

By similarity

Disulfide bond

462 ↔ 474

By similarity

Disulfide bond

504 ↔ 541

By similarity

Disulfide bond

508 ↔ 546

By similarity

Disulfide bond

519 ↔ 531

By similarity

Disulfide bond

551 ↔ 562

By similarity

Disulfide bond

556 ↔ 572

By similarity

Disulfide bond

575 ↔ 586

By similarity

Disulfide bond

592 ↔ 608

By similarity

Disulfide bond

599 ↔ 617

By similarity

Disulfide bond

620 ↔ 644

By similarity

Disulfide bond

650 ↔ 663

By similarity

Disulfide bond

657 ↔ 676

By similarity

Disulfide bond

678 ↔ 689

By similarity

Disulfide bond

705 ↔ 713

By similarity

Disulfide bond

718 ↔ 738

By similarity

Disulfide bond

754 ↔ 774

By similarity

Disulfide bond

777 ↔ 797

By similarity

Disulfide bond

813 ↔ 833

By similarity

Disulfide bond

836 ↔ 856

By similarity

Disulfide bond

874 ↔ 894

By similarity

Disulfide bond

910 ↔ 930

By similarity

Disulfide bond

946 ↔ 1167

By similarity

Experimental info

Sequence conflict

1025

F → L in AAA53063. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P35441 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 0443E493615E7F06
Show »

FASTA

1,170

129,647

        10         20         30         40         50         60 
MELLRGLGVL FLLHMCGSNR IPESGGDNGV FDIFELIGGA RRGPGRRLVK GQDLSSPAFR 

        70         80         90        100        110        120 
IENANLIPAV PDDKFQDLLD AVWADKGFIF LASLRQMKKT RGTLLAVERK DNTGQIFSVV 

       130        140        150        160        170        180 
SNGKAGTLDL SLSLPGKQQV VSVEEALLAT GQWKSITLFV QEDRAQLYID CDKMESAELD 

       190        200        210        220        230        240 
VPIQSIFTRD LASVARLRVA KGDVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTNVLL 

       250        260        270        280        290        300 
TLDNNVVNGS SPAIRTNYIG HKTKDLQAIC GLSCDELSSM VLELKGLRTI VTTLQDSIRK 

       310        320        330        340        350        360 
VTEENRELVS ELKRPPLCFH NGVQYKNNEE WTVDSCTECH CQNSVTICKK VSCPIMPCSN 

       370        380        390        400        410        420 
ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSATCGNGIQ QRGRSCDSLN NRCEGSSVQT 

       430        440        450        460        470        480 
RTCHIQECDK RFKQDGGWSH WSPWSSCSVT CGDGVITRIR LCNSPSPQMN GKPCEGEARE 

       490        500        510        520        530        540 
TKACKKDACP INGGWGPWSP WDICSVTCGG GVQRRSRLCN NPTPQFGGKD CVGDVTENQV 

       550        560        570        580        590        600 
CNKQDCPIDG CLSNPCFAGA KCTSYPDGSW KCGACPPGYS GNGIQCKDVD ECKEVPDACF 

       610        620        630        640        650        660 
NHNGEHRCKN TDPGYNCLPC PPRFTGSQPF GRGVEHAMAN KQVCKPRNPC TDGTHDCNKN 

       670        680        690        700        710        720 
AKCNYLGHYS DPMYRCECKP GYAGNGIICG EDTDLDGWPN ENLVCVANAT YHCKKDNCPN 

       730        740        750        760        770        780 
LPNSGQEDYD KDGIGDACDD DDDNDKIPDD RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN 

       790        800        810        820        830        840 
HNPDQADTDK NGEGDACAVD IDGDGILNER DNCQYVYNVD QRDTDMDGVG DQCDNCPLEH 

       850        860        870        880        890        900 
NPDQLDSDSD LIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN 

       910        920        930        940        950        960 
DGIPDDRDNC RLVPNPDQKD SDGDGRGDAC KDDFDHDNVP DIDDICPENF DISETDFRRF 

       970        980        990       1000       1010       1020 
QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY DEFNAVDFSG TFFINTERDD 

      1030       1040       1050       1060       1070       1080 
DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL 

      1090       1100       1110       1120       1130       1140 
WHTGNTPGQV RTLWHDPRHI GWKDFTAYRW RLSHRPKTGY IRVVMYEGKK IMADSGPIYD 

      1150       1160       1170 
KTYAGGRLGL FVFSQEMVFF SDMKYECRDS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the murine thrombospondin gene." Lawler J., Duquette M., Ferro P., Copeland N.G., Gilbert D.J., Jenkins N.A. Genomics 11:587-600(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Characterization of mouse thrombospondin 2 sequence and expression during cell growth and development." Laherty C.D., O'Rourke K., Wolf F.W., Katz R., Seldin M.F., Dixit V.M. J. Biol. Chem. 267:3274-3281(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Characterization of the mouse thrombospondin gene and evaluation of the role of the first intron in human gene expression." Bornstein P., Alfi D., Devarayalu S., Framson P., Li P. J. Biol. Chem. 265:16691-16698(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-490.
[4]	"Expression and initial characterization of recombinant mouse thrombospondin 1 and thrombospondin 3." Chen H., Aeschlimann D., Nowlen J., Mosher D.F. FEBS Lett. 387:36-41(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-37.
[5]	"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067, MASS SPECTROMETRY. Tissue: Myoblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M62470 M62469 Genomic DNA. Translation: AAA50611.1. M87276 mRNA. Translation: AAA53063.1. J05606, J05605 Genomic DNA. Translation: AAA40431.1.
IPI	IPI00118413.
PIR	A40558.
UniGene	Mm.4159.
3D structure databases
ProteinModelPortal	P35441.
SMR	P35441. Positions 30-233, 379-1169.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35441. 1 interaction.
PTM databases
PhosphoSite	P35441.
Proteomic databases
PaxDb	P35441.
PRIDE	P35441.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:98737. Thbs1.
Phylogenomic databases
eggNOG	NOG12793.
HOVERGEN	HBG018006.
InParanoid	P35441.
OrthoDB	EOG466VK5.
Gene expression databases
CleanEx	MM_THBS1.
Genevestigator	P35441.
GermOnline	ENSMUSG00000040152. Mus musculus.
Family and domain databases
Gene3D	2.60.120.200. 3 hits.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR001791. Laminin_G. IPR000884. Thrombospondin_1_rpt. IPR003367. Thrombospondin_3-like_rpt. IPR017897. Thrombospondin_3_rpt. IPR008859. Thrombospondin_C. IPR001007. VWF_C. [Graphical view]
Pfam	PF07645. EGF_CA. 1 hit. PF02210. Laminin_G_2. 1 hit. PF00090. TSP_1. 3 hits. PF02412. TSP_3. 7 hits. PF05735. TSP_C. 1 hit. PF00093. VWC. 1 hit. [Graphical view]
SMART	SM00181. EGF. 3 hits. SM00209. TSP1. 3 hits. SM00210. TSPN. 1 hit. SM00214. VWC. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 2 hits. SSF82895. TSP1. 3 hits.
PROSITE	PS00022. EGF_1. False negative. PS01186. EGF_2. 1 hit. PS50026. EGF_3. 2 hits. PS50025. LAM_G_DOMAIN. False negative. PS50092. TSP1. 3 hits. PS51234. TSP3. 8 hits. PS51236. TSP_CTER. 1 hit. PS01208. VWFC_1. 1 hit. PS50184. VWFC_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	THBS1. mouse.
SOURCE	Search...

Entry information

Entry name

TSP1_MOUSE

Accession

Primary (citable) accession number: P35441

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents