SIAL_RAT
ID SIAL_RAT Reviewed; 320 AA.
AC P13839; P97828;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 123.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-45 AND 151-175.
RX PubMed=3198635; DOI=10.1016/s0021-9258(19)77651-0;
RA Oldberg A., Franzen A., Heinegaard D.;
RT "The primary structure of a cell-binding bone sialoprotein.";
RL J. Biol. Chem. 263:19430-19432(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Bone marrow;
RA Yamamoto S., Uemura T.;
RT "The amino acid sequence of bone sialoprotein from rat bone marrow derived
RT osteoblastic cells.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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 -!- 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-316 or Tyr-317. {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; J04215; AAA41763.1; -; mRNA.
DR EMBL; AB001383; BAA19248.1; -; mRNA.
DR PIR; A30058; GERTS.
DR AlphaFoldDB; P13839; -.
DR SMR; P13839; -.
DR ELM; P13839; -.
DR STRING; 10116.ENSRNOP00000002938; -.
DR GlyGen; P13839; 3 sites.
DR iPTMnet; P13839; -.
DR PhosphoSitePlus; P13839; -.
DR PaxDb; P13839; -.
DR RGD; 2855; Ibsp.
DR eggNOG; KOG1181; Eukaryota.
DR InParanoid; P13839; -.
DR PhylomeDB; P13839; -.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR PRO; PR:P13839; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; TAS:RGD.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IMP:RGD.
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:0001503; P:ossification; TAS:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
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:0000250"
FT CHAIN 17..320
FT /note="Bone sialoprotein 2"
FT /id="PRO_0000020332"
FT REGION 60..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 289..291
FT /note="Cell attachment site"
FT COMPBIAS 71..104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..175
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 316
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 317
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 50
FT /note="Missing (in Ref. 2; BAA19248)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="E -> EEE (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="V -> A (in Ref. 2; BAA19248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35251 MW; E71C9B03F6027347 CRC64;
MKTALILLCI LGMASAFSMK NFHRRIKAED SEENGVFKYR PRYFLYKHAT YFYPPLKRFP
VQGGSDSSEE NGDGDSSEEE GEEEETSNEE ENNEDSEGNE DQEAEAENAT LSGVTASYGV
ETTADAGKLE LAALQLPKKA GDAEGKAPKM KESDEEEEEE EEEENENEEA EVDENEQVVN
GTSTNSTEVD GGNGPSGGDN GEEAEEASVT EAGAEGTTAG VRELTSYGTT TAVLLNGFQQ
TTPPPEAYGT TSPPARKSST VEYGEEYEQI GNEYNTAYET YDENNGEPRG DTYRAYEDEY
SYYKGHGYEG YEGQDYYYHQ
