SIAL_CHICK
ID SIAL_CHICK Reviewed; 276 AA.
AC P79780; Q90619; Q91405;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Bone;
RX PubMed=7610935; DOI=10.1002/jbmr.5650100417;
RA Yang R., Gotoh Y., Moore M.A., Rafidi K., Gerstenfeld L.C.;
RT "Characterization of an avian bone sialoprotein (BSP) cDNA: comparisons to
RT mammalian BSP and identification of conserved structural domains.";
RL J. Bone Miner. Res. 10:632-640(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9015757;
RX DOI=10.1002/(sici)1097-4644(199701)64:1<77::aid-jcb11>3.0.co;2-h;
RA Yang R., Gerstenfeld L.C.;
RT "Structural analysis and characterization of tissue and hormonal responsive
RT expression of the avian bone sialoprotein (BSP) gene.";
RL J. Cell. Biochem. 64:77-93(1997).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 48-55, AND PHOSPHORYLATION.
RC TISSUE=Bone {ECO:0000269|PubMed:1701638};
RX PubMed=1701638; DOI=10.1016/s0006-291x(05)81082-4;
RA Gotoh Y., Pierschbacher M.D., Grzesiak J.J., Gerstenfeld L., Glimcher M.J.;
RT "Comparison of two phosphoproteins in chicken bone and their similarities
RT to the mammalian bone proteins, osteopontin and bone sialoprotein II.";
RL Biochem. Biophys. Res. Commun. 173:471-479(1990).
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: Phosphorylated on serine and threonine residues.
CC {ECO:0000269|PubMed:1701638}.
CC -!- PTM: Sulfated on either Tyr-272 or Tyr-273. {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; U10577; AAB38374.1; -; mRNA.
DR EMBL; U67889; AAB36520.1; -; Genomic_DNA.
DR RefSeq; NP_990493.1; NM_205162.1.
DR AlphaFoldDB; P79780; -.
DR STRING; 9031.ENSGALP00000037334; -.
DR GeneID; 396071; -.
DR KEGG; gga:396071; -.
DR CTD; 3381; -.
DR VEuPathDB; HostDB:geneid_396071; -.
DR eggNOG; KOG1181; Eukaryota.
DR InParanoid; P79780; -.
DR OrthoDB; 1565775at2759; -.
DR PRO; PR:P79780; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030282; P:bone mineralization; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR008412; BSP_II.
DR PANTHER; PTHR10345; PTHR10345; 1.
DR Pfam; PF05432; BSP_II; 2.
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|UniProtKB:Q28862"
FT CHAIN 17..276
FT /note="Bone sialoprotein 2"
FT /id="PRO_0000020333"
FT REGION 54..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 116..118
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 228..230
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 246..248
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 121..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..189
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 273
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="S -> T (in Ref. 1; AAB38374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 276 AA; 30302 MW; B91D6093B43AC89A CRC64;
MRSALLLACL LATASAFSVR SWLRRARAGD SEENAVLKSR HRYYLYRYAY PPLHRYKGSD
SSEEEGDGSE EEEEGGAPSH AGTQAAGEGL TLGDVGPGGD AASAHQDCKG GQKGTRGDSG
DEDSDEEEEE EEEEEEEEEV EEQDVSVNGT STNTTAETPH GNNTVAAEEE EDDDEEEEEE
EEEEEEAEAT TAAATTAQDE VTTLGDEQRS EVTTAGEQWE YEVTVGARGD EGPTESSYGD
QEEPARGDSY RAYEDEYGYY KGHGYDMYGQ DYYYNQ
