ID   B2RTL6_MOUSE            Unreviewed;       963 AA.
AC   B2RTL6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   02-SEP-2026, entry version 143.
DE   RecName: Full=Thrombospondin-4 {ECO:0000256|ARBA:ARBA00072402};
GN   Name=Thbs4 {ECO:0000313|EMBL:AAI39415.1, ECO:0000313|MGI:MGI:1101779};
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 {ECO:0000313|EMBL:AAI39415.1};
RN   [1] {ECO:0000313|EMBL:AAI39415.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI39415.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 and is involved in various processes including
CC       cellular proliferation, migration, adhesion and attachment,
CC       inflammatory response to CNS injury, regulation of vascular
CC       inflammation and adaptive responses of the heart to pressure overload
CC       and in myocardial function and remodeling. Binds to structural
CC       extracellular matrix (ECM) proteins and modulates the ECM in response
CC       to tissue damage, contributing to cardioprotective and adaptive ECM
CC       remodeling. Plays a role in ER stress response, via its interaction
CC       with the activating transcription factor 6 alpha (ATF6) which produces
CC       adaptive ER stress response factors and protects myocardium from
CC       pressure overload. May contribute to spinal presynaptic
CC       hypersensitivity and neuropathic pain states after peripheral nerve
CC       injury. May play a role in regulating protective astrogenesis from the
CC       subventricular zone (SVZ) niche after injury in a NOTCH1-dependent
CC       manner. {ECO:0000256|ARBA:ARBA00054748}.
CC   -!- SUBUNIT: Homopentamer; disulfide-linked. Interacts with PTBP3.
CC       Interacts (via EGF-like 3; calcium-binding domain) with ATF6 and
CC       facilitates its processing, activation and nuclear translocation.
CC       Interacts with NOTCH1. {ECO:0000256|ARBA:ARBA00063266}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Sarcoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004369}. Secreted, extracellular space,
CC       extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
CC   -!- SIMILARITY: Belongs to the thrombospondin family.
CC       {ECO:0000256|ARBA:ARBA00009456}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; BC139414; AAI39415.1; -; mRNA.
DR   RefSeq; NP_035712.1; NM_011582.3.
DR   AlphaFoldDB; B2RTL6; -.
DR   SMR; B2RTL6; -.
DR   PeptideAtlas; B2RTL6; -.
DR   Antibodypedia; 3891; 173 antibodies from 27 providers.
DR   DNASU; 21828; -.
DR   GeneID; 21828; -.
DR   KEGG; mmu:21828; -.
DR   AGR; MGI:1101779; -.
DR   CTD; 7060; -.
DR   MGI; MGI:1101779; Thbs4.
DR   VEuPathDB; HostDB:ENSMUSG00000021702; -.
DR   HOGENOM; CLU_009257_1_1_1; -.
DR   OMA; ECQNGAC; -.
DR   OrthoDB; 14563at2759; -.
DR   PhylomeDB; B2RTL6; -.
DR   BioGRID-ORCS; 21828; 8 hits in 79 CRISPR screens.
DR   ExpressionAtlas; B2RTL6; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR   GO; GO:0048266; P:behavioral response to pain; IEA:UniProtKB-ARBA.
DR   GO; GO:0071603; P:endothelial cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0051451; P:myoblast migration; IEA:Ensembl.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IEA:Ensembl.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd16080; TSP-4cc; 1.
DR   FunFam; 4.10.1080.10:FF:000004; Cartilage oligomeric matrix protein; 1.
DR   FunFam; 2.10.25.10:FF:000025; Thrombospondin 3; 1.
DR   FunFam; 2.10.25.10:FF:000027; Thrombospondin 3; 1.
DR   FunFam; 2.60.120.200:FF:000002; Thrombospondin 3; 1.
DR   FunFam; 4.10.1080.10:FF:000001; Thrombospondin 3; 1.
DR   FunFam; 2.10.25.10:FF:000262; Thrombospondin 4; 1.
DR   FunFam; 2.10.25.10:FF:000277; Thrombospondin 4; 1.
DR   FunFam; 2.60.120.200:FF:000123; Thrombospondin 4; 1.
DR   FunFam; 1.20.5.10:FF:000001; thrombospondin-3 isoform X2; 1.
DR   Gene3D; 1.20.5.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR   InterPro; IPR017897; Thrombospondin_3_rpt.
DR   InterPro; IPR008859; Thrombospondin_C.
DR   InterPro; IPR024665; TSP/COMP_CC.
DR   InterPro; IPR046970; TSP/COMP_CC_sf.
DR   InterPro; IPR028974; TSP_type-3_rpt.
DR   InterPro; IPR048287; TSPN-like_N.
DR   PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR   PANTHER; PTHR10199:SF92; THROMBOSPONDIN-4; 1.
DR   Pfam; PF11598; COMP; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF02412; TSP_3; 5.
DR   Pfam; PF05735; TSP_C; 1.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS51234; TSP3; 3.
DR   PROSITE; PS51236; TSP_CTER; 1.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU00634}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Growth factor {ECO:0000256|ARBA:ARBA00023030};
KW   Mitogen {ECO:0000256|ARBA:ARBA00023246};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Tissue remodeling {ECO:0000256|ARBA:ARBA00023148};
KW   Unfolded protein response {ECO:0000256|ARBA:ARBA00023230}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..963
FT                   /note="Thrombospondin-4"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014298384"
FT   DOMAIN          328..365
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          381..418
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          422..464
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          498..533
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          557..592
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          694..729
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   DOMAIN          733..947
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          579..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..673
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  106366 MW;  B8BA83B84F489FB1 CRC64;
     MPAPRAAAAA FLLLHLVLQP WQRTSAQATP QVFDLLPSSS QRLNPSALQP VLTDPTLHEV
     YLISTFKLQS KSSATIFGLY SSSDNSKYFE FTVMGRLNKA ILRYLKNDGK IHLVVFNNLQ
     LADGRRHRVL LRLSNLQRGD GSVELYLDCA QADSVRNLPR AFSGLTQNPE SIELRTFQRK
     PQDFLEELKL VVRGSLFQVA SLQDCFLQQS EPLAATSTGD FNRQFLGQMT QLNQLLGEVK
     DLLRQQVKET SFLRNTIAEC QACGPLSFQS PTPNTLVPIA PPAPPTRPTR HCDSSPCFRG
     VRCTDTRDGF QCGPCPDGYT GNGITCSDVD ECKYHPCYPG VRCVNLAPGF RCDACPVGFT
     GPMVQGVGIN FAKTNKQVCT DVDECQNGAC VLNSICINTL GSYRCGPCKP GYTGDQTRGC
     KTERSCRNPE QNPCSVHAQC IEERQGDVTC VCGVGWAGDG YVCGKDVDID SYPDEELPCS
     ARNCKKDNCK YVPNSGQEDA DRDGIGDACD EDADGDGILN EQDNCVLTHN IDQRNSDKDI
     FGDACDNCRM VLNNDQKDTD GDGRGDACDD DMDGDGIKNI LDNCPRVPNR DQQDRDGDDV
     GDACDSCPDV SNPNQSDVDN DLVGDSCDTN QDSDGDGHQD STDNCPTVIN SSQLDTDKDG
     IGDECDDDDD NDGIPDLVPP GPDNCRLVPN PAQEDSNNDG VGDICEADFD QDQVIDHIDV
     CPENAEITLT DFRAYQTVVL DPEGDAQIDP NWVVLNQGME IVQTMNSDPG LAVGYTAFNG
     VDFEGTFHVN TQTDDDYAGF IFGYQDSSSF YVVMWKQTEQ TYWQATPFRA VAEPGIQLKA
     VKSKTGPGEH LRNSLWHTGD TSDQVRLLWK DSRNVGWKDK VSYRWFLQHR PQVGYIRVRF
     YEGSELVADS GVTIDTTMRG GRLGVFCFSQ ENIIWSNLKY RCNDTIPEDF QEFQTQSFDR
     LDN
//