GenomeNet

Database: UniProt
Entry: H2QPV2_PANTR
LinkDB: H2QPV2_PANTR
Original site: H2QPV2_PANTR 
ID   H2QPV2_PANTR            Unreviewed;       317 AA.
AC   H2QPV2; A0A2J8MA53;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
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:ENSPTRP00000027934.3,
GN   ECO:0000313|VGNC:VGNC:6424};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000027934.3, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000027934.3, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000027934.3}
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}.
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; AACZ04021331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_016807337.1; XM_016951848.1.
DR   AlphaFoldDB; H2QPV2; -.
DR   STRING; 9598.ENSPTRP00000027934; -.
DR   PaxDb; 9598-ENSPTRP00000027934; -.
DR   Ensembl; ENSPTRT00000030263.4; ENSPTRP00000027934.3; ENSPTRG00000016263.4.
DR   GeneID; 471249; -.
DR   KEGG; ptr:471249; -.
DR   CTD; 3381; -.
DR   VGNC; VGNC:6424; IBSP.
DR   eggNOG; KOG1181; Eukaryota.
DR   GeneTree; ENSGT00390000002485; -.
DR   HOGENOM; CLU_076119_0_0_1; -.
DR   InParanoid; H2QPV2; -.
DR   OMA; HAYFYPH; -.
DR   OrthoDB; 4616590at2759; -.
DR   TreeFam; TF338678; -.
DR   Proteomes; UP000002277; Chromosome 4.
DR   Bgee; ENSPTRG00000016263; Expressed in Brodmann (1909) area 10 and 2 other cell types or tissues.
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; IBA:GO_Central.
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:UP000002277};
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_5015092949"
FT   REGION          58..256
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        104..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..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;  35187 MW;  C105F24BB14C35F9 CRC64;
     MKTALILLSI LGMACAFSMK NLHRRVKIED SEENGVFKYR PRYYLYKHAY FYPHLKRFPV
     QGSSDSSEEN GDDSSEEEEE EEETSNEGEN NEESNEDEDS EAENTTLSAT TLGYGEDTTP
     GTGYTRLAAI HLPKKAGDIT NKATKEKESD EEEEEEEEEN ENEESEAEVD ENEQGINGTS
     TNSTEAENGN GSSGGDNGEE GEEESVTGAN AEGTTETGGQ GKGSSKTTTS PNGGFEPTTP
     PQVYRTTSPP FGKTTTVEYE GEYEYTGANE YDNGYEIYES ENGEPRGDNY RAYEDEYSYF
     KGQGYDGYDG QNYYHHQ
//
DBGET integrated database retrieval system