ID L5M3T3_MYODS Unreviewed; 217 AA.
AC L5M3T3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Bone sialoprotein 2 {ECO:0000256|ARBA:ARBA00017177};
DE AltName: Full=Bone sialoprotein II {ECO:0000256|ARBA:ARBA00033169};
DE AltName: Full=Cell-binding sialoprotein {ECO:0000256|ARBA:ARBA00032072};
DE AltName: Full=Integrin-binding sialoprotein {ECO:0000256|ARBA:ARBA00030309};
GN ORFNames=MDA_GLEAN10007999 {ECO:0000313|EMBL:ELK33016.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK33016.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- FUNCTION: Binds tightly to hydroxyapatite. Appears to form an integral
CC part of the mineralized matrix. Probably important to cell-matrix
CC interaction. Promotes Arg-Gly-Asp-dependent cell attachment.
CC {ECO:0000256|ARBA:ARBA00025685}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; KB104739; ELK33016.1; -; Genomic_DNA.
DR AlphaFoldDB; L5M3T3; -.
DR eggNOG; KOG1181; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0001503; P:ossification; IEA:InterPro.
DR InterPro; IPR008412; BSP_II.
DR PANTHER; PTHR10345; BONE SIALOPROTEIN 2; 1.
DR PANTHER; PTHR10345:SF0; BONE SIALOPROTEIN 2; 1.
DR Pfam; PF05432; BSP_II; 2.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..80
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 217 AA; 24683 MW; 4A8598B1AFD1419D CRC64;
MKNFHRRAKL EDSEENAVFK YRPRYYLYKH AYFYPPLKRF AVQAGDVGKK ATKKEESEEE
EEEEEEEEEN ENEENEAEVD ENGQGVNGTS TNSTDAENGN GSSGGDNGEE GEEEGEEENA
EGTTVAGEQD NGGSEPTTPP QEAYGTTPPP QGGTTTTEYE EEYEQTGTNE YDNGYEVYEN
ENAEPRGDNY RAYEDEYSYY KGRGYDSYDG QNYYYHQ
//
