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P35441 (TSP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thrombospondin-1
Gene names
Name:Thbs1
Synonyms:Tsp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1170 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors. Ref.6

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. Interacts with ATF6 (via lumenal domain). Ref.6

Subcellular location

Endoplasmic reticulum. Sarcoplasmic reticulum Ref.6.

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 processCell adhesion
Unfolded protein response
   Cellular componentEndoplasmic reticulum
Sarcoplasmic reticulum
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Heparin-binding
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to pain

Inferred from mutant phenotype PubMed 22745497. Source: UniProtKB

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

response to endoplasmic reticulum stress

Inferred from mutant phenotype Ref.6. Source: UniProtKB

response to unfolded protein

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.6. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 12498716. Source: MGI

sarcoplasmic reticulum

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functioncalcium 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.4
Chain19 – 11701152Thrombospondin-1
PRO_0000035843

Regions

Domain56 – 270215Laminin G-like
Domain316 – 37358VWFC
Domain379 – 42951TSP type-1 1
Domain435 – 49056TSP type-1 2
Domain492 – 54756TSP type-1 3
Domain547 – 58741EGF-like 1
Domain646 – 69045EGF-like 2
Repeat691 – 72636TSP type-3 1
Repeat727 – 76236TSP type-3 2
Repeat763 – 78523TSP type-3 3
Repeat786 – 82136TSP type-3 4
Repeat822 – 84423TSP type-3 5
Repeat845 – 88238TSP type-3 6
Repeat883 – 91836TSP type-3 7
Repeat919 – 95436TSP type-3 8
Domain958 – 1170213TSP C-terminal
Region47 – 9549Heparin-binding By similarity
Motif926 – 9283Cell attachment site Potential

Amino acid modifications

Glycosylation2481N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Potential
Glycosylation7081N-linked (GlcNAc...) Potential
Glycosylation10671N-linked (GlcNAc...) Ref.5
Disulfide bond171 ↔ 232 By similarity
Disulfide bond270Interchain Probable
Disulfide bond274Interchain Probable
Disulfide bond391 ↔ 423 By similarity
Disulfide bond395 ↔ 428 By similarity
Disulfide bond406 ↔ 413 By similarity
Disulfide bond447 ↔ 484 By similarity
Disulfide bond451 ↔ 489 By similarity
Disulfide bond462 ↔ 474 By similarity
Disulfide bond504 ↔ 541 By similarity
Disulfide bond508 ↔ 546 By similarity
Disulfide bond519 ↔ 531 By similarity
Disulfide bond551 ↔ 562 By similarity
Disulfide bond556 ↔ 572 By similarity
Disulfide bond575 ↔ 586 By similarity
Disulfide bond592 ↔ 608 By similarity
Disulfide bond599 ↔ 617 By similarity
Disulfide bond620 ↔ 644 By similarity
Disulfide bond650 ↔ 663 By similarity
Disulfide bond657 ↔ 676 By similarity
Disulfide bond678 ↔ 689 By similarity
Disulfide bond705 ↔ 713 By similarity
Disulfide bond718 ↔ 738 By similarity
Disulfide bond754 ↔ 774 By similarity
Disulfide bond777 ↔ 797 By similarity
Disulfide bond813 ↔ 833 By similarity
Disulfide bond836 ↔ 856 By similarity
Disulfide bond874 ↔ 894 By similarity
Disulfide bond910 ↔ 930 By similarity
Disulfide bond946 ↔ 1167 By similarity

Experimental info

Sequence conflict10251F → L in AAA53063. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35441 [UniParc].

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

FASTA1,170129,647
        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' 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.
Tissue: Myoblast.
[6]"A thrombospondin-dependent pathway for a protective ER stress response."
Lynch J.M., Maillet M., Vanhoutte D., Schloemer A., Sargent M.A., Blair N.S., Lynch K.A., Okada T., Aronow B.J., Osinska H., Prywes R., Lorenz J.N., Mori K., Lawler J., Robbins J., Molkentin J.D.
Cell 149:1257-1268(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATF6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62470 expand/collapse EMBL AC list , M62450, M62451, M62452, M62453, M62454, M62455, M62456, M62457, M62458, M62459, M62460, M62461, M62462, M62463, M62464, M62465, M62466, M62467, M62468, M62469 Genomic DNA. Translation: AAA50611.1.
M87276 mRNA. Translation: AAA53063.1.
J05606, J05605 Genomic DNA. Translation: AAA40431.1.
PIRA40558.
UniGeneMm.4159.

3D structure databases

ProteinModelPortalP35441.
SMRP35441. Positions 30-233, 549-1169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP35441. 2 interactions.
MINTMINT-4138704.

PTM databases

PhosphoSiteP35441.

Proteomic databases

PaxDbP35441.
PRIDEP35441.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:98737. Thbs1.

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG018006.
InParanoidP35441.

Gene expression databases

CleanExMM_THBS1.
GenevestigatorP35441.

Family and domain databases

Gene3D2.60.120.200. 3 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR001791. Laminin_G.
IPR028499. Thrombospondin-1.
IPR000884. Thrombospondin_1_rpt.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR001007. VWF_C.
[Graphical view]
PANTHERPTHR10199:SF53. PTHR10199:SF53. 1 hit.
PfamPF07645. 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]
SMARTSM00181. EGF. 3 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 2 hits.
SSF82895. SSF82895. 3 hits.
PROSITEPS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
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]
ProtoNetSearch...

Other

ChiTaRSTHBS1. mouse.
PROP35441.
SOURCESearch...

Entry information

Entry nameTSP1_MOUSE
AccessionPrimary (citable) accession number: P35441
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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