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 10-OCT-2003 (Rel. 42, 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 FROM N.A. (ISOFORM A). RC TISSUE=Kidney; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [9] 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 -!- FUNCTION: Acts as a cytokine involved in enhancing production of CC interferon-gamma and interleukin-12 and reducing production of CC interleukin-10 and is essential in the pathway that leads to type CC I immunity (By similarity). CC -!- SUBUNIT: LIGAND FOR INTEGRIN ALPHA-V/BETA-3. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; Synonyms=OPN-A, OP1B; CC IsoId=P10451-1; Sequence=Displayed; CC Name=B; Synonyms=OPN-B, OP1A; CC IsoId=P10451-2; Sequence=VSP_003778; CC Name=C; Synonyms=OPN-C; CC IsoId=P10451-3; Sequence=VSP_003777; 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. 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; D28759; BAA05949.1; -. DR EMBL; D28760; BAA05950.1; -. DR EMBL; D28761; BAA05951.1; -. DR EMBL; D14813; BAA03554.1; -. DR EMBL; BC017387; AAH17387.1; -. DR PIR; S50028; S09575. DR GlycoSuiteDB; P10451; -. DR Genew; HGNC:11255; SPP1. DR MIM; 166490; -. DR GO; GO:0005578; C:extracellular matrix; TAS. DR GO; GO:0008189; F:apoptosis inhibitor activity; ISS. DR GO; GO:0042056; F:chemoattractant activity; TAS. DR GO; GO:0005125; F:cytokine activity; ISS. DR GO; GO:0003793; F:defense/immunity protein activity; TAS. DR GO; GO:0008083; F:growth factor activity; TAS. DR GO; GO:0005178; F:integrin binding; NAS. DR GO; GO:0006916; P:anti-apoptosis; ISS. DR GO; GO:0007267; P:cell-cell signaling; TAS. DR GO; GO:0007160; P:cell-matrix adhesion; NAS. DR GO; GO:0030595; P:immune cell chemotaxis; TAS. DR GO; GO:0006954; P:inflammatory response; TAS. DR GO; GO:0030502; P:negative regulation of bone mineralization; NAS. DR GO; GO:0001503; P:ossification; TAS. DR GO; GO:0042102; P:positive regulation of T-cell proliferation; TAS. DR GO; GO:0045637; P:regulation of myeloid blood cell differenti...; TAS. DR GO; GO:0042088; P:T-helper 1 type immune response; TAS. DR InterPro; IPR002038; Osteopontin. DR Pfam; PF00865; Osteopontin; 1. DR PRINTS; PR00216; OSTEOPONTIN. DR SMART; SM00017; OSTEO; 1. DR PROSITE; PS00884; OSTEOPONTIN; 1. KW Cytokine; Glycoprotein; Sialic acid; Biomineralization; Cell adhesion; KW Phosphorylation; Signal; Alternative splicing; Polymorphism. 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 /FTId=VSP_003777. FT VARSPLIC 58 71 Missing (in isoform B). FT /FTId=VSP_003778. FT VARIANT 301 301 R -> H (in dbSNP:4660). FT /FTId=VAR_014717. 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 //