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Q03350 (TSP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thrombospondin-2
Gene names
Name:Thbs2
Synonyms:Tsp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1172 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. Ligand for CD36 mediating antiangiogenic properties. Ref.5

Subunit structure

Homotrimer; disulfide-linked. Can bind to fibrinogen, fibronectin, laminin and type V collagen By similarity. 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 THBS2 with CD36. Can bind to fibrinogen, fibronectin, laminin. Ref.5

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Jag1Q637222EBI-4567830,EBI-4567800From a different organism.
LRP1Q079542EBI-4567830,EBI-1046087From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 11721154Thrombospondin-2
PRO_0000035847

Regions

Domain19 – 215197Laminin G-like
Domain318 – 37558VWFC
Domain381 – 43151TSP type-1 1
Domain437 – 49256TSP type-1 2
Domain494 – 54956TSP type-1 3
Domain549 – 58941EGF-like 1
Domain648 – 69245EGF-like 2
Repeat693 – 72836TSP type-3 1
Repeat729 – 76436TSP type-3 2
Repeat765 – 78723TSP type-3 3
Repeat788 – 82336TSP type-3 4
Repeat824 – 84623TSP type-3 5
Repeat847 – 88438TSP type-3 6
Repeat885 – 92036TSP type-3 7
Repeat921 – 95636TSP type-3 8
Domain960 – 1172213TSP C-terminal
Region19 – 232214Heparin-binding Potential
Motif928 – 9303Cell attachment site Potential

Amino acid modifications

Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Glycosylation5841N-linked (GlcNAc...) Potential
Glycosylation7101N-linked (GlcNAc...) Potential
Glycosylation10691N-linked (GlcNAc...) Potential
Disulfide bond266Interchain Probable
Disulfide bond270Interchain Probable
Disulfide bond393 ↔ 425 By similarity
Disulfide bond397 ↔ 430 By similarity
Disulfide bond408 ↔ 415 By similarity
Disulfide bond449 ↔ 486 By similarity
Disulfide bond453 ↔ 491 By similarity
Disulfide bond464 ↔ 476 By similarity
Disulfide bond506 ↔ 543 By similarity
Disulfide bond510 ↔ 548 By similarity
Disulfide bond521 ↔ 533 By similarity
Disulfide bond553 ↔ 564 By similarity
Disulfide bond558 ↔ 574 By similarity
Disulfide bond577 ↔ 588 By similarity
Disulfide bond594 ↔ 610 By similarity
Disulfide bond601 ↔ 619 By similarity
Disulfide bond622 ↔ 646 By similarity
Disulfide bond652 ↔ 665 By similarity
Disulfide bond659 ↔ 678 By similarity
Disulfide bond680 ↔ 691 By similarity
Disulfide bond707 ↔ 715 By similarity
Disulfide bond720 ↔ 740 By similarity
Disulfide bond756 ↔ 776 By similarity
Disulfide bond779 ↔ 799 By similarity
Disulfide bond815 ↔ 835 By similarity
Disulfide bond838 ↔ 858 By similarity
Disulfide bond876 ↔ 896 By similarity
Disulfide bond912 ↔ 932 By similarity
Disulfide bond948 ↔ 1169 By similarity

Experimental info

Sequence conflict2251G → S in AAA53064. Ref.1
Sequence conflict2251G → S in AAA40432. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q03350 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 020ACD7EB5137B25

FASTA1,172129,882
        10         20         30         40         50         60 
MLWALALLAL GIGPRASAGD HVKDTSFDLF SISNINRKTI GAKQFRGPDP GVPAYRFVRF 

        70         80         90        100        110        120 
DYIPPVNTDD LNRIVKLARR KEGFFLTAQL KQDRKSRGTL LVLEGPGTSQ RQFEIVSNGP 

       130        140        150        160        170        180 
GDTLDLNYWV EGNQHTNFLE DVGLADSQWK NVTVQVASDT YSLYVGCDLI DSVTLEEPFY 

       190        200        210        220        230        240 
EQLEVDRSRM YVAKGASRES HFRGLLQNVH LVFADSVEDI LSKKGCQHSQ GAEVNTISEH 

       250        260        270        280        290        300 
TETLHLSPHI TTDLVVQGVE KAQEVCTHSC EELSNMMNEL SGLHVMVNQL SKNLERVSSD 

       310        320        330        340        350        360 
NQFLLELIGG PLKTRNMSAC VQEGRIFAEN ETWVVDSCTT CTCKKFKTVC HQITCSPATC 

       370        380        390        400        410        420 
ANPSFVEGEC CPSCSHSADS DEGWSPWAEW TECSVTCGSG TQQRGRSCDV TSNTCLGPSI 

       430        440        450        460        470        480 
QTRTCSLGKC DTRIRQNGGW SHWSPWSSCS VTCGVGNVTR IRLCNSPVPQ MGGKNCKGSG 

       490        500        510        520        530        540 
RETKPCQRDP CPIDGRWSPW SPWSACTVTC AGGIRERSRV CNSPEPQYGG KDCVGDVTEH 

       550        560        570        580        590        600 
QMCNKRSCPI DGCLSNPCFP GAKCNSFPDG SWSCGSCPVG FLGNGTHCED LDECAVVTDI 

       610        620        630        640        650        660 
CFSTNKAPRC VNTNPGFHCL PCPPRYKGNQ PFGVGLEDAR TEKQVCEPEN PCKDKTHSCH 

       670        680        690        700        710        720 
KNAECIYLGH FSDPMYKCEC QIGYAGDGLI CGEDSDLDGW PNNNLVCATN ATYHCIKDNC 

       730        740        750        760        770        780 
PKLPNSGQED FDKDGIGDAC DEDDDNDGVS DEKDNCQLLF NPRQLDYDKD EVGDRCDNCP 

       790        800        810        820        830        840 
YVHNPAQIDT DNNGEGDACS VDIDGDDVFN ERDNCPYVYN TDQRDTDGDG VGDHCDNCPL 

       850        860        870        880        890        900 
MHNPDQIDQD NDLVGDQCDN NEDIDDDGHQ NNQDNCPYIS NSNQADHDND GKGDACDSDD 

       910        920        930        940        950        960 
DNDGVPDDRD NCRLVFNPDQ EDSDGDGRGD ICKDDFDNDN VPDIDDVCPE NNAITETDFR 

       970        980        990       1000       1010       1020 
NFQMVPLDPK GTTQIDPNWV IRHQGKELVQ TANSDPGIAV GFDEFGSVDF SGTFYVNTDR 

      1030       1040       1050       1060       1070       1080 
DDDYAGFVFG YQSSSRFYVV MWKQVTQTYW EDKPSRAYGY SGVSLKVVNS TTGTGEHLRN 

      1090       1100       1110       1120       1130       1140 
ALWHTGNTEG QVRTLWHDPK NIGWKDYTAY RWHLIHRPKT GYMRVLVHEG KQVMADSGPI 

      1150       1160       1170 
YDQTYAGGRL GLFVFSQEMV YFSDLKYECR DA 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"Genomic sequence analysis in the mouse t-complex region."
Brathwaite M., Waeltz P., Qian Y., Dudekula D., Schlessinger D., Nagaraja R.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129S6/SvEvTac.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"A second, expressed thrombospondin gene (Thbs2) exists in the mouse genome."
Bornstein P., O'Rourke K., Wikstrom K., Wolf F.W., Katz R., Li P., Dixit V.M.
J. Biol. Chem. 266:12821-12824(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-873.
[5]"The antiangiogenic effect of thrombospondin-2 is mediated by CD36 and modulated by histidine-rich glycoprotein."
Simantov R., Febbraio M., Silverstein R.L.
Matrix Biol. 24:27-34(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD36 AND HRG, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07803 mRNA. Translation: AAA53064.1.
AF549256 Genomic DNA. Translation: AAO16244.1.
CH466630 Genomic DNA. Translation: EDL20481.1.
M64866 mRNA. Translation: AAA40432.1.
PIRA42587.
RefSeqNP_035711.2. NM_011581.3.
UniGeneMm.26688.

3D structure databases

ProteinModelPortalQ03350.
SMRQ03350. Positions 27-226, 315-549, 551-1171.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204176. 2 interactions.
IntActQ03350. 3 interactions.
MINTMINT-4115682.

PTM databases

PhosphoSiteQ03350.

Proteomic databases

PaxDbQ03350.
PRIDEQ03350.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000170872; ENSMUSP00000128308; ENSMUSG00000023885.
GeneID21826.
KEGGmmu:21826.
UCSCuc008anb.2. mouse.

Organism-specific databases

CTD7058.
MGIMGI:98738. Thbs2.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00550000074507.
HOGENOMHOG000007542.
HOVERGENHBG018006.
InParanoidQ8CG21.
KOK04659.
OMATEKQVCE.
OrthoDBEOG76QFGD.
TreeFamTF324917.

Gene expression databases

ArrayExpressQ03350.
BgeeQ03350.
CleanExMM_THBS2.
GenevestigatorQ03350.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR024731. EGF_dom_MSP1-like.
IPR001791. Laminin_G.
IPR015455. Thrombospondin-2.
IPR000884. Thrombospondin_1_rpt.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR001007. VWF_C.
[Graphical view]
PANTHERPTHR10199:SF10. PTHR10199:SF10. 1 hit.
PfamPF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 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

ChiTaRSTHBS2. mouse.
NextBio301256.
PROQ03350.
SOURCESearch...

Entry information

Entry nameTSP2_MOUSE
AccessionPrimary (citable) accession number: Q03350
Secondary accession number(s): Q8CG21
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 126 of the entry and version 2 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