ID OSTP_HUMAN STANDARD; PRT; 314 AA. AC P10451; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 15-JUL-1999 (Rel. 38, 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; Mammalia; OC Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 89263749. 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. 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. RA 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. 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 OF 67-278 FROM N.A. RC TISSUE=KIDNEY; RX MEDLINE; 92246977. 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 AN INTEGRAL PART OF THE MINERALIZED MATRIX. PROBABLY IMPORTANT CC TO CELL-MATRIX INTERACTION. CC -!- ALTERNATIVE PRODUCTS: TWO FORMS OF OPN ARE PRODUCES BY ALTERNATIVE CC SPLICING OF THE SAME GENE. THEY DIFFER BY THE PRESENCE (OP1B) OR CC ABSENCE (OP1A) OF 14 AMINO ACIDS AT RESIDUE 58 OF THE MOLECULE. 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 -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; D14813; BAA03554.1; -. DR PIR; A35326; A35326. DR PIR; S09575; S09575. DR PIR; JQ1529; JQ1529. DR MIM; 166490; -. DR PFAM; PF00865; Osteopontin; 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 VARSPLIC 59 72 MISSING (IN OP1A). FT CARBOHYD 79 79 POTENTIAL. FT CARBOHYD 106 106 POTENTIAL. FT CONFLICT 275 278 SHEF -> GNSL (IN REF. 2). SQ SEQUENCE 314 AA; 35422 MW; B2A9B8C0 CRC32; 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 //