ID L9L562_TUPCH Unreviewed; 279 AA.
AC L9L562;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=TREES_T100011614 {ECO:0000313|EMBL:ELW70201.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW70201.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB320503; ELW70201.1; -; Genomic_DNA.
DR AlphaFoldDB; L9L562; -.
DR STRING; 246437.L9L562; -.
DR eggNOG; KOG1181; Eukaryota.
DR InParanoid; L9L562; -.
DR Proteomes; UP000011518; 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; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT REGION 25..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..73
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 30955 MW; 05227653D0D26A48 CRC64;
MVHVFKYRPR YYLYKHAYFY PPLRRFPVQS SDSSEENGDG DSSEEEEEGE EASNEEENNE
DSNGNEDEDS EAENSTLSTT TLGYGEEITP GTGDTGLAAI QLPKEAGDKR NKATKQKESD
EEEEEEEEEN ENEENEAEVD ENEQGINGTS TNSTEVDNGN GSSGGDNGEE EGEEESVTGA
VAEGTTVTRG QDNGGSKTTT SSNGGLVPTT PPQIYGTTSV SYEEYEHTGT NHYDNEYEVY
ENENGEPRGD NYRAYEDEYS YYKGQGYGGY GDQDYYYHQ
//
