ID   OSTP_HUMAN     STANDARD;      PRT;   314 AA.
AC   P10451; Q15681; Q15682; Q15683;
DT   01-MAR-1989 (Rel. 10, Created)
DT   01-MAR-1989 (Rel. 10, Last sequence update)
DT   20-AUG-2001 (Rel. 40, Last annotation update)
DE   Osteopontin precursor (Bone sialoprotein 1) (Urinary stone protein)
DE   (Secreted phosphoprotein 1) (SPP-1) (Nephropontin) (Uropontin).
GN   SPP1 OR OPN.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=89263749; PubMed=2726470;
RA   Kiefer M.C., Bauer D.M., Barr P.J.;
RT   "The cDNA and derived amino acid sequence for human osteopontin.";
RL   Nucleic Acids Res. 17:3306-3306(1989).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=90353945; PubMed=1974876;
RA   Young M.F., Kerr J.M., Termine J.D., Wewer U.M., Wang M.G.,
RA   McBride O.W., Fisher L.W.;
RT   "cDNA cloning, mRNA distribution and heterogeneity, chromosomal
RT   location, and RFLP analysis of human osteopontin (OPN).";
RL   Genomics 7:491-502(1990).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=92108068; PubMed=1729712;
RA   Shiraga H., Min W., VanDusen W.J., Clayman M.D., Miner D.,
RA   Terrell C.H., Sherbotie J.R., Foreman J.W., Przysiecki C.,
RA   Neilson E.G., Hoyer J.R.;
RT   "Inhibition of calcium oxalate crystal growth in vitro by uropontin:
RT   another member of the aspartic acid-rich protein superfamily.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:426-430(1992).
RN   [4]
RP   SEQUENCE FROM N.A.
RA   Crosby A.H., Edwards S., Murray J.C., Dixon M.J.;
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   SEQUENCE FROM N.A.
RC   TISSUE=Liver;
RX   MEDLINE=95031968; PubMed=7945249;
RA   Hijiya N., Setoguchi M., Matsuura K., Higuchi Y., Akizuki S.,
RA   Yamamoto S.;
RT   "Cloning and characterization of the human osteopontin gene and its
RT   promoter.";
RL   Biochem. J. 303:255-262(1994).
RN   [6]
RP   SEQUENCE FROM N.A.
RC   TISSUE=Brain;
RA   Yu W., Sarginson J., Gibbs R.A.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING.
RX   MEDLINE=95139605; PubMed=7837791;
RA   Saitoh Y., Kuratsu J., Takeshima H., Yamamoto S., Ushio Y.;
RT   "Expression of osteopontin in human glioma. Its correlation with the
RT   malignancy.";
RL   Lab. Invest. 72:55-63(1995).
RN   [8]
RP   SEQUENCE OF 67-278 FROM N.A.
RC   TISSUE=Kidney;
RX   MEDLINE=92246977; PubMed=1575754;
RA   Kohri K., Suzuki Y., Yoshida K., Yamamoto K., Amasaki N., Yamate T.,
RA   Umekawa T., Iguchi M., Sinohara H., Kurita T.;
RT   "Molecular cloning and sequencing of cDNA encoding urinary stone
RT   protein, which is identical to osteopontin.";
RL   Biochem. Biophys. Res. Commun. 184:859-864(1992).
CC   -!- FUNCTION: BINDS TIGHTLY TO HYDROXYAPATITE. APPEARS TO FORM AN
CC       INTEGRAL PART OF THE MINERALIZED MATRIX. PROBABLY IMPORTANT TO
CC       CELL-MATRIX INTERACTION.
CC   -!- SUBUNIT: LIGAND FOR INTEGRIN ALPHA-V/BETA-3.
CC   -!- ALTERNATIVE PRODUCTS: 3 ISOFORMS; A/OPN-A/OP1B, B/OPN-B/OP1A AND
CC       C/OPN-C; ARE PRODUCED BY ALTERNATIVE SPLICING.
CC   -!- PTM: EXTENSIVELY PHOSPHORYLATED ON SERINE RESIDUES.
CC   -!- PTM: N- AND O-GLYCOSYLATED.
CC   -!- DISEASE: THIS PROTEIN PLAYS A PRINCIPAL ROLE IN URINARY STONE
CC       FORMATION AS THE STONE MATRIX.
CC   -!- SIMILARITY: BELONGS TO THE OSTEOPONTIN FAMILY.
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DR   EMBL; X13694; CAA31984.1; -.
DR   EMBL; J04765; AAA59974.1; -.
DR   EMBL; M83248; AAA17675.1; -.
DR   EMBL; U20758; AAA86886.1; -.
DR   EMBL; AF052124; AAC28619.1; -.
DR   EMBL; D28759; BAA05949.1; -.
DR   EMBL; D28760; BAA05950.1; -.
DR   EMBL; D28761; BAA05951.1; -.
DR   EMBL; D14813; BAA03554.1; -.
DR   PIR; A35326; A35326.
DR   PIR; S09575; S09575.
DR   PIR; JQ1529; JQ1529.
DR   MIM; 166490; -.
DR   InterPro; IPR002038; Osteopontin.
DR   Pfam; PF00865; Osteopontin; 1.
DR   PRINTS; PR00216; OSTEOPONTIN.
DR   SMART; SM00017; OSTEO; 1.
DR   PROSITE; PS00884; OSTEOPONTIN; 1.
KW   Glycoprotein; Sialic acid; Bone; Cell adhesion; Phosphorylation;
KW   Signal; Alternative splicing.
FT   SIGNAL        1     16       POTENTIAL.
FT   CHAIN        17    314       OSTEOPONTIN.
FT   SITE        159    161       CELL ATTACHMENT SITE.
FT   CARBOHYD     79     79       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    106    106       N-LINKED (GLCNAC...) (POTENTIAL).
FT   VARSPLIC     31     57       MISSING (IN ISOFORM C).
FT   VARSPLIC     58     71       MISSING (IN ISOFORM B).
FT   CONFLICT    188    188       D -> H (IN REF. 7).
FT   CONFLICT    237    237       T -> A (IN REF. 7).
FT   CONFLICT    275    278       SHEF -> GNSL (IN REF. 2).
SQ   SEQUENCE   314 AA;  35422 MW;  4996429EC4752B86 CRC64;
     MRIAVICFCL LGITCAIPVK QADSGSSEEK QLYNKYPDAV ATWLNPDPSQ KQNLLAPQNA
     VSSEETNDFK QETLPSKSNE SHDHMDDMDD EDDDDHVDSQ DSIDSNDSDD VDDTDDSHQS
     DESHHSDESD ELVTDFPTDL PATEVFTPVV PTVDTYDGRG DSVVYGLRSK SKKFRRPDIQ
     YPDATDEDIT SHMESEELNG AYKAIPVAQD LNAPSDWDSR GKDSYETSQL DDQSAETHSH
     KQSRLYKRKA NDESNEHSDV IDSQELSKVS REFHSHEFHS HEDMLVVDPK SKEEDKHLKF
     RISHELDSAS SEVN
//