SIAL_BOVIN
ID SIAL_BOVIN Reviewed; 310 AA.
AC Q28862;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Bone sialoprotein 2;
DE AltName: Full=Bone sialoprotein II;
DE Short=BSP II;
DE AltName: Full=Cell-binding sialoprotein;
DE AltName: Full=Integrin-binding sialoprotein;
DE Flags: Precursor;
GN Name=IBSP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone;
RX PubMed=7514841; DOI=10.1002/jbmr.5650090318;
RA Chenu C., Ibaraki K., Gehron Robey P., Delmas P.D., Young M.F.;
RT "Cloning and sequence analysis of bovine bone sialoprotein cDNA:
RT conservation of acidic domains, tyrosine sulfation consensus repeats, and
RT RGD cell attachment domain.";
RL J. Bone Miner. Res. 9:417-421(1994).
RN [2]
RP PROTEIN SEQUENCE OF 17-27 AND 140-148, AND PHOSPHORYLATION.
RX PubMed=8663267; DOI=10.1074/jbc.271.28.16897;
RA Salih E., Zhou H.-Y., Glimcher M.J.;
RT "Phosphorylation of purified bovine bone sialoprotein and osteopontin by
RT protein kinases.";
RL J. Biol. Chem. 271:16897-16905(1996).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-31; SER-62; SER-67;
RP SER-75; SER-76; SER-98; SER-106; THR-144; SER-154; SER-273 AND SER-300, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15004024; DOI=10.1074/jbc.m310299200;
RA Salih E., Flueckiger R.;
RT "Complete topographical distribution of both the in vivo and in vitro
RT phosphorylation sites of bone sialprotein and their biological
RT implications.";
RL J. Biol. Chem. 279:19808-19815(2004).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: N-glycosylated; glycans consist of sialylated and core-fucosylated
CC bi-, tri- and tetraantennary chains. {ECO:0000250}.
CC -!- PTM: Sulfated on either Tyr-306 or Tyr-307. {ECO:0000250}.
CC -!- MISCELLANEOUS: It is possible that the segments of clustered carboxyl
CC groups mediate the strong binding to hydroxyapatite.
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DR EMBL; S73144; AAB30817.1; -; mRNA.
DR PIR; I46987; I46987.
DR RefSeq; NP_776509.1; NM_174084.3.
DR RefSeq; XP_010804306.1; XM_010806004.1.
DR AlphaFoldDB; Q28862; -.
DR SMR; Q28862; -.
DR STRING; 9913.ENSBTAP00000000595; -.
DR iPTMnet; Q28862; -.
DR PaxDb; Q28862; -.
DR PRIDE; Q28862; -.
DR Ensembl; ENSBTAT00000000595; ENSBTAP00000000595; ENSBTAG00000000470.
DR GeneID; 281233; -.
DR KEGG; bta:281233; -.
DR CTD; 3381; -.
DR VEuPathDB; HostDB:ENSBTAG00000000470; -.
DR VGNC; VGNC:30021; IBSP.
DR eggNOG; KOG1181; Eukaryota.
DR GeneTree; ENSGT00390000002485; -.
DR HOGENOM; CLU_076119_0_0_1; -.
DR InParanoid; Q28862; -.
DR OMA; QDYYYHQ; -.
DR OrthoDB; 1565775at2759; -.
DR TreeFam; TF338678; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000000470; Expressed in diaphragm and 19 other 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:0030282; P:bone mineralization; IEP:UniProtKB.
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; PTHR10345; 1.
DR Pfam; PF05432; BSP_II; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Cell adhesion; Direct protein sequencing; Glycoprotein;
KW Phosphoprotein; Reference proteome; Secreted; Sialic acid; Signal;
KW Sulfation.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:8663267"
FT CHAIN 17..310
FT /note="Bone sialoprotein 2"
FT /id="PRO_0000020329"
FT REGION 61..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 279..281
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 71..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 173..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15004024"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15004024"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15004024"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15004024"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15004024"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15004024"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15004024"
FT MOD_RES 144
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15004024"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15004024"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15004024"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15004024"
FT MOD_RES 306
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 307
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 310 AA; 34101 MW; B5BD8F61BAD88261 CRC64;
MKTVLILLSI LGMACALSMK NLNRRAKLED SEENGVFKYR PQYYVYKHGY FYPALKRFAV
QSSSDSSEEN GNGDSSEEEE EEEETSNEEG NNGGNEDSDE NEDEESEAEN TTLSTTTLGY
GEITPGTGDI GLAAIWLPRK AGATGKKATK EDESDEEEEE EEEEENEAEV DDNEQGINGT
SSNSTEVDNG HGSSGGDNGE EDGEEESVTE ANTEGITVAG ETTTSPNGGF KPTTPHQEVY
GTTPPPFGKI TTPGEYEQTG TNEYDNGYEI YESENGDPRG DNYRAYEDEY SYYKGRGYDS
YDGQDYYSHQ
