ID   OSTP_HUMAN     STANDARD;      PRT;   314 AA.
AC   P10451; Q15681; Q15682; Q15683; Q8NBK2; Q96IZ1;
DT   01-MAR-1989 (Rel. 10, Created)
DT   01-MAR-1989 (Rel. 10, Last sequence update)
DT   25-JAN-2005 (Rel. 46, Last annotation update)
DE   Osteopontin precursor (Bone sialoprotein 1) (Secreted phosphoprotein
DE   1) (SPP-1) (Urinary stone protein) (Nephropontin) (Uropontin).
GN   Name=SPP1; Synonyms=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   NUCLEOTIDE SEQUENCE (ISOFORM 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   NUCLEOTIDE SEQUENCE (ISOFORM B).
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   NUCLEOTIDE SEQUENCE (ISOFORM 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   NUCLEOTIDE SEQUENCE (ISOFORM A).
RX   MEDLINE=95394452; PubMed=7665163;
RA   Crosby A.H., Edwards S.J., Murray J.C., Dixon M.J.;
RT   "Genomic organization of the human osteopontin gene: exclusion of the
RT   locus from a causative role in the pathogenesis of dentinogenesis
RT   imperfecta type II.";
RL   Genomics 27:155-160(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 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   NUCLEOTIDE SEQUENCE (ISOFORMS A; B AND C).
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   [7]
RP   NUCLEOTIDE SEQUENCE (ISOFORM B).
RC   TISSUE=Brain;
RA   Yu W., Sarginson J., Gibbs R.A.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE (ISOFORM D).
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J.-I., Saito K., Kawai Y., Isono Y., Nakamura Y.,
RA   Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M.,
RA   Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H.,
RA   Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E.,
RA   Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M.,
RA   Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K.,
RA   Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y.,
RA   Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T.,
RA   Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O.,
RA   Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M.,
RA   Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS A AND B).
RC   TISSUE=Brain, and Kidney;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
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 human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [10]
RP   NUCLEOTIDE SEQUENCE OF 67-278.
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).
RN   [11]
RP   PROTEIN SEQUENCE OF 17-23 AND 169-182.
RC   TISSUE=Milk;
RX   PubMed=2736258;
RA   Senger D.R., Perruzzi C.A., Papadopoulos A., Tenen D.G.;
RT   "Purification of a human milk protein closely similar to tumor-
RT   secreted phosphoproteins and osteopontin.";
RL   Biochim. Biophys. Acta 996:43-48(1989).
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=4;
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       Name=D;
CC         IsoId=P10451-4; Sequence=VSP_011639;
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; D14813; BAA03554.1; -.
DR   EMBL; D28759; BAA05949.1; -.
DR   EMBL; D28760; BAA05950.1; -.
DR   EMBL; D28761; BAA05951.1; -.
DR   EMBL; AF052124; AAC28619.1; -.
DR   EMBL; AK075463; BAC11635.1; -.
DR   EMBL; BC007016; AAH07016.1; -.
DR   EMBL; BC017387; AAH17387.1; -.
DR   EMBL; BC022844; AAH22844.1; -.
DR   PIR; S50028; S09575.
DR   GlycoSuiteDB; P10451; -.
DR   Ensembl; ENSG00000118785; Homo sapiens.
DR   Genew; HGNC:11255; SPP1.
DR   H-InvDB; HIX0004361; -.
DR   MIM; 166490; -.
DR   GO; GO:0005578; C:extracellular matrix (sensu Metazoa); TAS.
DR   GO; GO:0005125; F:cytokine activity; ISS.
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:0050930; P:induction of positive chemotaxis; 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   Alternative splicing; Biomineralization; Cell adhesion; Cytokine;
KW   Direct protein sequencing; Glycoprotein; Phosphorylation;
KW   Polymorphism; Sialic acid; Signal.
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   VARSPLIC     95    116       Missing (in isoform D).
FT                                /FTId=VSP_011639.
FT   VARIANT     301    301       R -> H (in dbSNP:4660).
FT                                /FTId=VAR_014717.
FT   CONFLICT    188    188       D -> H (in Ref. 6).
FT   CONFLICT    237    237       T -> A (in Ref. 6).
FT   CONFLICT    275    278       SHEF -> GNSL (in Ref. 2).
SQ   SEQUENCE   314 AA;  35423 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
//