ID   B2RTL6_MOUSE            Unreviewed;       963 AA.
AC   B2RTL6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   SubName: Full=Thrombospondin 4 {ECO:0000313|EMBL:AAI39415.1};
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   -!- 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   EPD; B2RTL6; -.
DR   PeptideAtlas; B2RTL6; -.
DR   Antibodypedia; 3891; 205 antibodies from 26 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; DSNPCFQ; -.
DR   OrthoDB; 5345349at2759; -.
DR   PhylomeDB; B2RTL6; -.
DR   BioGRID-ORCS; 21828; 8 hits in 79 CRISPR screens.
DR   ChiTaRS; Thbs4; mouse.
DR   ExpressionAtlas; B2RTL6; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; 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: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:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
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   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd16080; TSP-4cc; 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; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_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_coiled-coil.
DR   InterPro; IPR046970; TSP/COMP_coiled-coil_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}; 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   Unfolded protein response {ECO:0000256|ARBA:ARBA00023230}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..963
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        588..602
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..674
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
//