ID   TSP2_MOUSE              Reviewed;        1172 AA.
AC   Q03350; Q8CG21;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Thrombospondin-2;
DE   Flags: Precursor;
GN   Name=Thbs2; Synonyms=Tsp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1371115; DOI=10.1016/s0021-9258(19)50727-x;
RA   Laherty C.D., O'Rourke K., Wolf F.W., Katz R., Seldin M.F., Dixit V.M.;
RT   "Characterization of mouse thrombospondin 2 sequence and expression during
RT   cell growth and development.";
RL   J. Biol. Chem. 267:3274-3281(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129S6/SvEvTac;
RA   Brathwaite M., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA   Nagaraja R.;
RT   "Genomic sequence analysis in the mouse t-complex region.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-873.
RX   PubMed=1712771; DOI=10.1016/s0021-9258(18)98764-8;
RA   Bornstein P., O'Rourke K., Wikstrom K., Wolf F.W., Katz R., Li P.,
RA   Dixit V.M.;
RT   "A second, expressed thrombospondin gene (Thbs2) exists in the mouse
RT   genome.";
RL   J. Biol. Chem. 266:12821-12824(1991).
RN   [5]
RP   INTERACTION WITH CD36 AND HRG, AND FUNCTION.
RX   PubMed=15748999; DOI=10.1016/j.matbio.2004.11.005;
RA   Simantov R., Febbraio M., Silverstein R.L.;
RT   "The antiangiogenic effect of thrombospondin-2 is mediated by CD36 and
RT   modulated by histidine-rich glycoprotein.";
RL   Matrix Biol. 24:27-34(2005).
CC   -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC       matrix interactions. Ligand for CD36 mediating antiangiogenic
CC       properties. {ECO:0000269|PubMed:15748999}.
CC   -!- SUBUNIT: Homotrimer; disulfide-linked. Can bind to fibrinogen,
CC       fibronectin, laminin and type V collagen (By similarity). Interacts
CC       (via the TSP type I repeats) with CD36; the interaction conveys an
CC       antiangiogenic effect. Interacts (via the TSP type I repeats) with HRG;
CC       the interaction blocks the antiangiogenic effect of THBS2 with CD36.
CC       Can bind to fibrinogen, fibronectin, laminin. {ECO:0000250,
CC       ECO:0000269|PubMed:15748999}.
CC   -!- INTERACTION:
CC       Q03350; Q63722: Jag1; Xeno; NbExp=2; IntAct=EBI-4567830, EBI-4567800;
CC       Q03350; Q07954: LRP1; Xeno; NbExp=2; IntAct=EBI-4567830, EBI-1046087;
CC   -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
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DR   EMBL; L07803; AAA53064.1; -; mRNA.
DR   EMBL; AF549256; AAO16244.1; -; Genomic_DNA.
DR   EMBL; CH466630; EDL20481.1; -; Genomic_DNA.
DR   EMBL; M64866; AAA40432.1; -; mRNA.
DR   CCDS; CCDS49958.1; -.
DR   PIR; A42587; A42587.
DR   RefSeq; NP_035711.2; NM_011581.3.
DR   AlphaFoldDB; Q03350; -.
DR   SMR; Q03350; -.
DR   BioGRID; 204176; 5.
DR   ComplexPortal; CPX-3023; Thrombospondin 2 complex.
DR   IntAct; Q03350; 2.
DR   STRING; 10090.ENSMUSP00000128308; -.
DR   GlyConnect; 2765; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q03350; 7 sites, 1 glycan.
DR   GlyGen; Q03350; 7 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q03350; -.
DR   PhosphoSitePlus; Q03350; -.
DR   jPOST; Q03350; -.
DR   MaxQB; Q03350; -.
DR   PaxDb; 10090-ENSMUSP00000128308; -.
DR   PeptideAtlas; Q03350; -.
DR   ProteomicsDB; 297997; -.
DR   Pumba; Q03350; -.
DR   Antibodypedia; 33564; 286 antibodies from 26 providers.
DR   DNASU; 21826; -.
DR   Ensembl; ENSMUST00000170872.3; ENSMUSP00000128308.2; ENSMUSG00000023885.10.
DR   GeneID; 21826; -.
DR   KEGG; mmu:21826; -.
DR   UCSC; uc008anb.2; mouse.
DR   AGR; MGI:98738; -.
DR   CTD; 7058; -.
DR   MGI; MGI:98738; Thbs2.
DR   VEuPathDB; HostDB:ENSMUSG00000023885; -.
DR   eggNOG; ENOG502QRK8; Eukaryota.
DR   GeneTree; ENSGT00940000157846; -.
DR   HOGENOM; CLU_009257_0_0_1; -.
DR   InParanoid; Q03350; -.
DR   OMA; MPGVMLQ; -.
DR   OrthoDB; 5345349at2759; -.
DR   PhylomeDB; Q03350; -.
DR   TreeFam; TF324917; -.
DR   Reactome; R-MMU-186797; Signaling by PDGF.
DR   Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR   BioGRID-ORCS; 21826; 0 hits in 80 CRISPR screens.
DR   ChiTaRS; Thbs2; mouse.
DR   PRO; PR:Q03350; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q03350; Protein.
DR   Bgee; ENSMUSG00000023885; Expressed in vault of skull and 193 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; ISO:MGI.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 6.20.200.20; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR   Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR   InterPro; IPR017897; Thrombospondin_3_rpt.
DR   InterPro; IPR008859; Thrombospondin_C.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   InterPro; IPR028974; TSP_type-3_rpt.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR   PANTHER; PTHR10199:SF10; THROMBOSPONDIN-2; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF00090; TSP_1; 3.
DR   Pfam; PF02412; TSP_3; 7.
DR   Pfam; PF05735; TSP_C; 1.
DR   Pfam; PF00093; VWC; 1.
DR   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00209; TSP1; 3.
DR   SMART; SM00210; TSPN; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS50092; TSP1; 3.
DR   PROSITE; PS51234; TSP3; 8.
DR   PROSITE; PS51236; TSP_CTER; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
DR   Genevisible; Q03350; MM.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Heparin-binding; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1172
FT                   /note="Thrombospondin-2"
FT                   /id="PRO_0000035847"
FT   DOMAIN          19..215
FT                   /note="Laminin G-like"
FT   DOMAIN          318..375
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          381..431
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          437..492
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          494..549
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          549..589
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          648..692
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REPEAT          693..728
FT                   /note="TSP type-3 1"
FT   REPEAT          729..764
FT                   /note="TSP type-3 2"
FT   REPEAT          765..787
FT                   /note="TSP type-3 3"
FT   REPEAT          788..823
FT                   /note="TSP type-3 4"
FT   REPEAT          824..846
FT                   /note="TSP type-3 5"
FT   REPEAT          847..884
FT                   /note="TSP type-3 6"
FT   REPEAT          885..920
FT                   /note="TSP type-3 7"
FT   REPEAT          921..956
FT                   /note="TSP type-3 8"
FT   DOMAIN          960..1172
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT   REGION          19..232
FT                   /note="Heparin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          727..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           928..930
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        735..750
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..886
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..938
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        584
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        710
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1069
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        266
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        270
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        393..425
FT                   /evidence="ECO:0000250"
FT   DISULFID        397..430
FT                   /evidence="ECO:0000250"
FT   DISULFID        408..415
FT                   /evidence="ECO:0000250"
FT   DISULFID        449..486
FT                   /evidence="ECO:0000250"
FT   DISULFID        453..491
FT                   /evidence="ECO:0000250"
FT   DISULFID        464..476
FT                   /evidence="ECO:0000250"
FT   DISULFID        506..543
FT                   /evidence="ECO:0000250"
FT   DISULFID        510..548
FT                   /evidence="ECO:0000250"
FT   DISULFID        521..533
FT                   /evidence="ECO:0000250"
FT   DISULFID        553..564
FT                   /evidence="ECO:0000250"
FT   DISULFID        558..574
FT                   /evidence="ECO:0000250"
FT   DISULFID        577..588
FT                   /evidence="ECO:0000250"
FT   DISULFID        594..610
FT                   /evidence="ECO:0000250"
FT   DISULFID        601..619
FT                   /evidence="ECO:0000250"
FT   DISULFID        622..646
FT                   /evidence="ECO:0000250"
FT   DISULFID        652..665
FT                   /evidence="ECO:0000250"
FT   DISULFID        659..678
FT                   /evidence="ECO:0000250"
FT   DISULFID        680..691
FT                   /evidence="ECO:0000250"
FT   DISULFID        707..715
FT                   /evidence="ECO:0000250"
FT   DISULFID        720..740
FT                   /evidence="ECO:0000250"
FT   DISULFID        756..776
FT                   /evidence="ECO:0000250"
FT   DISULFID        779..799
FT                   /evidence="ECO:0000250"
FT   DISULFID        815..835
FT                   /evidence="ECO:0000250"
FT   DISULFID        838..858
FT                   /evidence="ECO:0000250"
FT   DISULFID        876..896
FT                   /evidence="ECO:0000250"
FT   DISULFID        912..932
FT                   /evidence="ECO:0000250"
FT   DISULFID        948..1169
FT                   /evidence="ECO:0000250"
FT   CONFLICT        225
FT                   /note="G -> S (in Ref. 1; AAA53064 and 4; AAA40432)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1172 AA;  129882 MW;  020ACD7EB5137B25 CRC64;
     MLWALALLAL GIGPRASAGD HVKDTSFDLF SISNINRKTI GAKQFRGPDP GVPAYRFVRF
     DYIPPVNTDD LNRIVKLARR KEGFFLTAQL KQDRKSRGTL LVLEGPGTSQ RQFEIVSNGP
     GDTLDLNYWV EGNQHTNFLE DVGLADSQWK NVTVQVASDT YSLYVGCDLI DSVTLEEPFY
     EQLEVDRSRM YVAKGASRES HFRGLLQNVH LVFADSVEDI LSKKGCQHSQ GAEVNTISEH
     TETLHLSPHI TTDLVVQGVE KAQEVCTHSC EELSNMMNEL SGLHVMVNQL SKNLERVSSD
     NQFLLELIGG PLKTRNMSAC VQEGRIFAEN ETWVVDSCTT CTCKKFKTVC HQITCSPATC
     ANPSFVEGEC CPSCSHSADS DEGWSPWAEW TECSVTCGSG TQQRGRSCDV TSNTCLGPSI
     QTRTCSLGKC DTRIRQNGGW SHWSPWSSCS VTCGVGNVTR IRLCNSPVPQ MGGKNCKGSG
     RETKPCQRDP CPIDGRWSPW SPWSACTVTC AGGIRERSRV CNSPEPQYGG KDCVGDVTEH
     QMCNKRSCPI DGCLSNPCFP GAKCNSFPDG SWSCGSCPVG FLGNGTHCED LDECAVVTDI
     CFSTNKAPRC VNTNPGFHCL PCPPRYKGNQ PFGVGLEDAR TEKQVCEPEN PCKDKTHSCH
     KNAECIYLGH FSDPMYKCEC QIGYAGDGLI CGEDSDLDGW PNNNLVCATN ATYHCIKDNC
     PKLPNSGQED FDKDGIGDAC DEDDDNDGVS DEKDNCQLLF NPRQLDYDKD EVGDRCDNCP
     YVHNPAQIDT DNNGEGDACS VDIDGDDVFN ERDNCPYVYN TDQRDTDGDG VGDHCDNCPL
     MHNPDQIDQD NDLVGDQCDN NEDIDDDGHQ NNQDNCPYIS NSNQADHDND GKGDACDSDD
     DNDGVPDDRD NCRLVFNPDQ EDSDGDGRGD ICKDDFDNDN VPDIDDVCPE NNAITETDFR
     NFQMVPLDPK GTTQIDPNWV IRHQGKELVQ TANSDPGIAV GFDEFGSVDF SGTFYVNTDR
     DDDYAGFVFG YQSSSRFYVV MWKQVTQTYW EDKPSRAYGY SGVSLKVVNS TTGTGEHLRN
     ALWHTGNTEG QVRTLWHDPK NIGWKDYTAY RWHLIHRPKT GYMRVLVHEG KQVMADSGPI
     YDQTYAGGRL GLFVFSQEMV YFSDLKYECR DA
//