ID D2GX57_AILME Unreviewed; 321 AA.
AC D2GX57;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
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};
DE Flags: Fragment;
GN Name=IBSP {ECO:0000313|Ensembl:ENSAMEP00000003372.1};
GN ORFNames=PANDA_001447 {ECO:0000313|EMBL:EFB19866.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB19866.1};
RN [1] {ECO:0000313|EMBL:EFB19866.1, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000003372.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; GL192364; EFB19866.1; -; Genomic_DNA.
DR RefSeq; XP_002913629.1; XM_002913583.1.
DR STRING; 9646.ENSAMEP00000003372; -.
DR Ensembl; ENSAMET00000003507.2; ENSAMEP00000003372.1; ENSAMEG00000003185.2.
DR GeneID; 100476112; -.
DR KEGG; aml:100476112; -.
DR CTD; 3381; -.
DR eggNOG; KOG1181; Eukaryota.
DR GeneTree; ENSGT00390000002485; -.
DR HOGENOM; CLU_076119_0_0_1; -.
DR OMA; HAYFYPH; -.
DR OrthoDB; 4616590at2759; -.
DR TreeFam; TF338678; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0036094; F:small molecule binding; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..321
FT /note="Bone sialoprotein 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015088178"
FT REGION 58..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 321
FT /evidence="ECO:0000313|EMBL:EFB19866.1"
SQ SEQUENCE 321 AA; 35607 MW; 02CAF890824EFE2A CRC64;
MKTALILLSI LGMACAFSMK NLHRRAKLED SEENGVFKYR PRYSLYKHAY FYPPLKRFPV
QSSSDSSEED GNGDSSEEEE EEEETSNEEE NNEENANSDE NEDEESEAEN TTLTATPGYG
EETTPGTGYI GLAAIQLPKK SGDIGHKATK EEESDEEEEE DEENEENEAE VDENGQGING
TSSNSTEAEN GNGSSDGDNG EEGEEESVTE AHTEGTTVVG KQDNGGSKTT VSPDGGFERT
TPPPELYGTT TRPSGEATPT GYEGEYEQTG TNEYDNGYEV YENENGEPRG DNYRAYEDEY
SYYKGRSYDG YDGQDYYYRH Q
//
