TSP3_MOUSE
ID TSP3_MOUSE Reviewed; 956 AA.
AC Q05895; Q6LCE0; Q7TN15;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Thrombospondin-3;
DE Flags: Precursor;
GN Name=Thbs3; Synonyms=Tsp3;
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].
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX PubMed=8468055; DOI=10.1006/geno.1993.1114;
RA Bornstein P., Devarayalu S., Edelhoff S., Disteche C.M.;
RT "Isolation and characterization of the mouse thrombospondin 3 (Thbs3)
RT gene.";
RL Genomics 15:607-613(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8288588; DOI=10.1016/s0021-9258(17)42252-6;
RA Qabar A.N., Lin Z., Wolf F.W., O'Shea K.S., Lawler J., Dixit V.M.;
RT "Thrombospondin 3 is a developmentally regulated heparin binding protein.";
RL J. Biol. Chem. 269:1262-1269(1994).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 517-956.
RC STRAIN=BALB/cJ;
RX PubMed=1601886; DOI=10.1016/s0021-9258(19)49823-2;
RA Vos H.L., Devarayalu S., de Vries Y., Bornstein P.;
RT "Thrombospondin 3 (Thbs3), a new member of the thrombospondin gene
RT family.";
RL J. Biol. Chem. 267:12192-12196(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 834-956.
RC STRAIN=BALB/cJ;
RX PubMed=8597643; DOI=10.1007/bf00539013;
RA Vos H.L., Mockensturm-Wilson M., Rood P.M.L., Maas A.M., Duhig T.,
RA Gendler S.J., Bornstein P.;
RT "A tightly organized, conserved gene cluster on mouse chromosome 3 (E3-
RT F1).";
RL Mamm. Genome 6:820-822(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX PubMed=8871542; DOI=10.1093/nar/24.19.3661;
RA Collins M., Bornstein P.;
RT "SP1-binding elements, within the common metaxin-thrombospondin 3
RT intergenic region, participate in the regulation of the metaxin gene.";
RL Nucleic Acids Res. 24:3661-3669(1996).
RN [8]
RP PROTEIN SEQUENCE OF 22-32.
RX PubMed=8654563; DOI=10.1016/0014-5793(96)00460-7;
RA Chen H., Aeschlimann D., Nowlen J., Mosher D.F.;
RT "Expression and initial characterization of recombinant mouse
RT thrombospondin 1 and thrombospondin 3.";
RL FEBS Lett. 387:36-41(1996).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions. Can bind to fibrinogen, fibronectin, laminin and
CC type V collagen.
CC -!- SUBUNIT: Oligomer; disulfide-linked.
CC -!- TISSUE SPECIFICITY: Brain, lung and cartilage.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
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DR EMBL; L04302; AAA40497.1; -; mRNA.
DR EMBL; L24434; AAA40433.1; -; mRNA.
DR EMBL; CH466547; EDL15225.1; -; Genomic_DNA.
DR EMBL; BC053023; AAH53023.1; -; mRNA.
DR EMBL; M86620; AAA40430.1; -; Genomic_DNA.
DR EMBL; M86611; AAA40430.1; JOINED; Genomic_DNA.
DR EMBL; M86612; AAA40430.1; JOINED; Genomic_DNA.
DR EMBL; M86613; AAA40430.1; JOINED; Genomic_DNA.
DR EMBL; M86614; AAA40430.1; JOINED; Genomic_DNA.
DR EMBL; M86615; AAA40430.1; JOINED; Genomic_DNA.
DR EMBL; M86616; AAA40430.1; JOINED; Genomic_DNA.
DR EMBL; M86617; AAA40430.1; JOINED; Genomic_DNA.
DR EMBL; M86618; AAA40430.1; JOINED; Genomic_DNA.
DR EMBL; M86619; AAA40430.1; JOINED; Genomic_DNA.
DR EMBL; U16175; AAA98537.1; -; Genomic_DNA.
DR EMBL; U66257; AAC52819.1; -; Genomic_DNA.
DR CCDS; CCDS17495.1; -.
DR PIR; A46016; A46016.
DR RefSeq; NP_038719.2; NM_013691.2.
DR AlphaFoldDB; Q05895; -.
DR SMR; Q05895; -.
DR ComplexPortal; CPX-3024; Thrombospondin 3 complex.
DR STRING; 10090.ENSMUSP00000029682; -.
DR GlyGen; Q05895; 4 sites.
DR PhosphoSitePlus; Q05895; -.
DR MaxQB; Q05895; -.
DR PaxDb; Q05895; -.
DR PRIDE; Q05895; -.
DR ProteomicsDB; 297729; -.
DR Antibodypedia; 34176; 210 antibodies from 30 providers.
DR DNASU; 21827; -.
DR Ensembl; ENSMUST00000029682; ENSMUSP00000029682; ENSMUSG00000028047.
DR GeneID; 21827; -.
DR KEGG; mmu:21827; -.
DR UCSC; uc008pyg.2; mouse.
DR CTD; 7059; -.
DR MGI; MGI:98739; Thbs3.
DR VEuPathDB; HostDB:ENSMUSG00000028047; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000159283; -.
DR InParanoid; Q05895; -.
DR OMA; NSMIHRT; -.
DR OrthoDB; 120983at2759; -.
DR PhylomeDB; Q05895; -.
DR TreeFam; TF324917; -.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR BioGRID-ORCS; 21827; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Thbs3; mouse.
DR PRO; PR:Q05895; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q05895; protein.
DR Bgee; ENSMUSG00000028047; Expressed in ventricular zone and 203 other tissues.
DR ExpressionAtlas; Q05895; baseline and differential.
DR Genevisible; Q05895; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0060346; P:bone trabecula formation; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0003417; P:growth plate cartilage development; IMP:MGI.
DR GO; GO:0043931; P:ossification involved in bone maturation; IMP:MGI.
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; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR024665; Thbs/COMP_coiled-coil.
DR InterPro; IPR028507; Thrombospondin-3.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR10199:SF89; PTHR10199:SF89; 1.
DR Pfam; PF11598; COMP; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 6.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF103647; SSF103647; 3.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51234; TSP3; 8.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:8654563"
FT CHAIN 22..956
FT /note="Thrombospondin-3"
FT /id="PRO_0000035850"
FT DOMAIN 22..193
FT /note="Laminin G-like"
FT DOMAIN 316..354
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 370..410
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 414..456
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 457..491
FT /note="TSP type-3 1"
FT REPEAT 492..527
FT /note="TSP type-3 2"
FT REPEAT 528..550
FT /note="TSP type-3 3"
FT REPEAT 551..586
FT /note="TSP type-3 4"
FT REPEAT 587..609
FT /note="TSP type-3 5"
FT REPEAT 610..647
FT /note="TSP type-3 6"
FT REPEAT 648..687
FT /note="TSP type-3 7"
FT REPEAT 688..723
FT /note="TSP type-3 8"
FT DOMAIN 727..941
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 518..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..667
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 266
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 269
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 278..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 283..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 303..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 320..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 326..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 344..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 374..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 382..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 400..412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 418..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 426..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 444..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 471..478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 483..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 519..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 542..562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 578..598
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 601..621
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 639..659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 679..699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 715..936
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 433
FT /note="L -> F (in Ref. 2; AAA40433)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="D -> N (in Ref. 1; AAA40497 and 5; AAA40430)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="E -> G (in Ref. 1; AAA40497 and 5; AAA40430)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="W -> L (in Ref. 1; AAA40497 and 5; AAA40430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 104119 MW; 4FAC268D11C83CAA CRC64;
MEKPELWGVL ALLLLCSYTC GSQDLQVIDL LTVGESRQMV AVAEKIRTAL LTAGDIYLLS
TFRLPPKQGG VLFGLYSRQD NTRWLEASVV GKINKVLVRY QREDGKVHAV NLQQAGLADG
RTHTALLRLR GPSRPSPGLQ LYVDCKLGDQ HAGLPALAPI PPAEVSGLEI RTGQKAYLRM
QGFVESMKII LGGSMARVGA LSECPFQGDD SIHNAVTSAL QSILGEQTKA LVTQLTLFNQ
ILVELRDDIR DQVKEMSLIR NTIMECQVCG FHEQRSHCSP SPCFRGVDCM EVYEYPGYRC
GPCPPGLQGN GTHCDDINEC AHADPCFPGS SCINTMPGFH CEACPPGYKG TRVSGVGIDY
ARASKQVCND IDECNDGNNG GCDPNSICTN TVGSFKCGPC RLGFLGNQSQ GCVPARTCHS
PAHSPCHIHA HCLFERNGAV SCQCNVGWAG NGNVCGPDTD IDGYPDQALP CMDNNKHCKQ
DNCLLTPNSG QEDADNDGVG DQCDDDADGD GIKNVEDNCR LFPNKDQQNS DTDSFGDACD
NCPNVPNNDQ KDTDGNGEGD ACDNDVDGDG IPNGLDNCPK VPNPLQTDRD EDGVGDACDS
CPEMSNPTQT DADSDLVGDV CDTNEDSDGD GHQDTKDNCP QLPNSSQLDS DNDGLGDECD
GDDDNDGVPD YIPPGPDNCR LVPNPNQKDS DGNGVGDVCE DDFDNDAVVD PLDVCPESAE
VTLTDFRAYQ TVILDPEGDA QIDPNWVVLN QGMEIVQTMN SDPGLAVGYT AFNGVDFEGT
FHVNTVTDDD YAGFLFSYQD SGRFYVVMWK QTEQTYWQAT PFRAVAQPGL QLKAVTSISG
PGEHLRNALW HTGHTPDQVR LLWTDPRNVG WRDKTSYRWR LLHRPQVGYI RVKLYEGPQL
VADSGVIIDT SMRGGRLGVF CFSQENIIWS NLQYRCNDTV PEDFEPFRRQ LLQGRV
