ID H2PDV2_PONAB Unreviewed; 317 AA.
AC H2PDV2; A0A2J8V5E3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 52.
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 Name=IBSP {ECO:0000313|Ensembl:ENSPPYP00000016657.2};
GN ORFNames=CR201_G0022454 {ECO:0000313|EMBL:PNJ52689.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000016657.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000016657.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ52689.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ52689.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000016657.2}
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; NDHI03003433; PNJ52689.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000016657; -.
DR Ensembl; ENSPPYT00000017336.2; ENSPPYP00000016657.2; ENSPPYG00000014918.2.
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; UP000001595; Chromosome 4.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; ISS:UniProtKB.
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:UP000001595};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..317
FT /note="Bone sialoprotein 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041117710"
FT REGION 58..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..103
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 34960 MW; 7C18685B4641ACF0 CRC64;
MKTALILLSI LGMACAFSMK NLHRRVKIED SEENGVFKYR PRYYLYKHAY FYPHLKRFPV
QGSSDSSEEN GDDSSEEEEE EEETSNEGEN NEESNEDEDS EAENTTLSAT TLGYGEDATL
ATGYPGLAAI QLPKKAGDIT SKATKEEESD EEEEEEEEEN ENEESEAEVD ENEQGINGTS
TNSTEAENGN GSSGGDNGEE GEEESVTGAN AEGTTAAGGQ GKGSSKTTTS PNGGFEPTTP
PQVYRTTSPP FGKTTTVEYE GEYEYTGANE YDNGYEIYES ENGEPRGDNY RAYEDEYSYF
KGQGYDGYDG QNYYHHQ
//
