SIAL_PIG
ID SIAL_PIG Reviewed; 300 AA.
AC P31936;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 104.
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;
GN Name=IBSP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE OF 1-20.
RC TISSUE=Bone;
RX PubMed=2332443; DOI=10.1016/s0021-9258(19)39154-9;
RA Zhang Q., Domenicucci C., Goldberg H.A., Wrana J.L., Sodek J.;
RT "Characterization of fetal porcine bone sialoproteins, secreted
RT phosphoprotein I (SPPI, osteopontin), bone sialoprotein, and a 23-kDa
RT glycoprotein. Demonstration that the 23-kDa glycoprotein is derived from
RT the carboxyl terminus of SPPI.";
RL J. Biol. Chem. 265:7583-7589(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-300.
RX PubMed=8309422; DOI=10.1016/s0934-8832(11)80109-5;
RA Shapiro H.S., Chen J., Wrana J.L., Zhang Q., Blum M., Sodek J.;
RT "Characterization of porcine bone sialoprotein: primary structure and
RT cellular expression.";
RL Matrix 13:431-440(1993).
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-299 or Tyr-300. {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; L10363; AAA19822.1; -; mRNA.
DR PIR; B35204; B35204.
DR PIR; S40032; S35103.
DR AlphaFoldDB; P31936; -.
DR STRING; 9823.ENSSSCP00000029623; -.
DR PaxDb; P31936; -.
DR PRIDE; P31936; -.
DR eggNOG; KOG1181; Eukaryota.
DR InParanoid; P31936; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P31936; SS.
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; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Cell adhesion; Direct protein sequencing; Glycoprotein;
KW Phosphoprotein; Reference proteome; Secreted; Sialic acid; Sulfation.
FT CHAIN 1..300
FT /note="Bone sialoprotein 2"
FT /id="PRO_0000160609"
FT REGION 41..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 272..274
FT /note="Cell attachment site"
FT COMPBIAS 55..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..158
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 299
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 300
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 300 AA; 33026 MW; C853E8EBDE156BE6 CRC64;
FSMKNFHRRA KLEDPEENGV FKYRPRYYLY KHAYFYPPLK RFPVQSSSDS SEENGNGDSS
EEEEEEEENS NEEENNEENE DSDGNEDEDS EAENITLSTT TLGYGGDVTP GTASIGLAAL
QLPKKAGDIG KKSAKEEESD EDEEEEEENE ENEAEVDDNE QGTNGTSTNS TEVDSGNGHS
GGDNGEEGDQ ESVTEAQGTT VAGEQDNGGA KTTTSPNGGL EPTPPPQDIS GTTLPPSGKT
TTPEYEGEYE QTGAHEYDNG YEIYESENGE PRGDSYRAYE DEYSYYKGRS YNSYGGHDYY
