TSP2_MOUSE
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 03-AUG-2022, entry version 180.
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 GlyGen; Q03350; 7 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q03350; -.
DR PhosphoSitePlus; Q03350; -.
DR jPOST; Q03350; -.
DR MaxQB; Q03350; -.
DR PaxDb; Q03350; -.
DR PeptideAtlas; Q03350; -.
DR PRIDE; Q03350; -.
DR ProteomicsDB; 297997; -.
DR Antibodypedia; 33564; 254 antibodies from 26 providers.
DR DNASU; 21826; -.
DR Ensembl; ENSMUST00000170872; ENSMUSP00000128308; ENSMUSG00000023885.
DR GeneID; 21826; -.
DR KEGG; mmu:21826; -.
DR UCSC; uc008anb.2; mouse.
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; PPVTCAN; -.
DR OrthoDB; 120983at2759; -.
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 75 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 192 other tissues.
DR Genevisible; Q03350; MM.
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; 2.20.100.10; -; 3.
DR Gene3D; 4.10.1080.10; -; 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; IPR001791; Laminin_G.
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; IPR015455; TSP2.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR10199:SF10; PTHR10199:SF10; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 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 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; SSF103647; SSF103647; 3.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF82895; SSF82895; 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.
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
