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UniProtKB/Swiss-Prot Q15063 (POSTN_HUMAN)
Last modified
November 25, 2008.
Version 71.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Periostin Short name=PN Alternative name(s): Osteoblast-specific factor 2 Short name=OSF-2 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 836 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Binds to heparin. Induces cell attachment and spreading and plays a role in cell adhesion. May play a role in extracellular matrix mineralization. |
| Subcellular location | |
| Tissue specificity | Widely expressed with highest levels in aorta, stomach, lower gastrointestinal tract, placenta, uterus and breast. Up-regulated in epithelial ovarian tumors. Not expressed in normal ovaries. Also highly expressed at the tumor periphery of lung carcinoma tissue but not within the tumor. Overexpressed in breast cancers. |
| Post-translational modification | Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium. |
| Sequence similarities | Contains 1 EMI domain. Contains 4 FAS1 domains. |
Ontologies
Keywords | |
|---|---|
| Biological process | Cell adhesion |
| Cellular component | Extracellular matrix Secreted |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat Signal |
| Ligand | Heparin-binding |
| PTM | Gamma-carboxyglutamic acid Glycoprotein |
Gene Ontology (GO) | |
| Biological process | cell adhesion Ref.2 Inferred from direct assay. Source: UniProtKB skeletal system development Ref.1Traceable author statement. Source: ProtInc |
| Cellular component | proteinaceous extracellular matrix Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | heparin binding Inferred from sequence or structural similarity. Source: UniProtKB protein bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q15063-1) Also known as: OSF-2OS; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q15063-2) Also known as: OSF-2p1; The sequence of this isoform differs from the canonical sequence as follows: 670-727: TTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPEFRLIKEGETITEVIHGE → K | ||||||
| Isoform 3 (identifier: Q15063-3) The sequence of this isoform differs from the canonical sequence as follows: 670-697: TTKIITKVVEPKIKVIEGSLQPIIKTEG → R 783-810: Missing. | ||||||
| Isoform 4 (identifier: Q15063-4) The sequence of this isoform differs from the canonical sequence as follows: 670-727: TTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPEFRLIKEGETITEVIHGE → K 783-810: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 21 | 21 | Potential | ||||||||
| Chain | 22 – 836 | 815 | Periostin | PRO_0000008789 | |||||||
Regions | |||||||||||
| Domain | 40 – 94 | 55 | EMI | ||||||||
| Domain | 97 – 230 | 134 | FAS1 1 | ||||||||
| Domain | 234 – 365 | 132 | FAS1 2 | ||||||||
| Domain | 368 – 492 | 125 | FAS1 3 | ||||||||
| Domain | 496 – 628 | 133 | FAS1 4 | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 124 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 125 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 127 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 140 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 154 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 160 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 242 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 244 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 261 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 277 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 280 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 288 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 298 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 313 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 322 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 325 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 496 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 501 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 517 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 523 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 547 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 548 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 550 | 1 | 4-carboxyglutamate Potential | ||||||||
| Modified residue | 578 | 1 | 4-carboxyglutamate Potential | ||||||||
| Glycosylation | 599 | 1 | N-linked (GlcNAc...) | ||||||||
| Disulfide bond | 44 ↔ 80 | By similarity | |||||||||
| Disulfide bond | 60 ↔ 69 | By similarity | |||||||||
| Disulfide bond | 79 ↔ 92 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 670 – 727 | 58 | TTKII…VIHGE → K in isoform 2 and isoform 4. | VSP_050005 | |||||||
| Alternative sequence | 670 – 697 | 28 | TTKII…IKTEG → R in isoform 3. | VSP_050669 | |||||||
| Alternative sequence | 783 – 810 | 28 | Missing in isoform 3 and isoform 4. | VSP_050670 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 290 | 1 | I → F in BAA02836 and BAA02837. Ref.1 | ||||||||
| Sequence conflict | 290 | 1 | I → F in AAY15840. Ref.3 | ||||||||
| Sequence conflict | 421 | 1 | D → V in BAA02836 and BAA02837. Ref.1 | ||||||||
| Sequence conflict | 421 | 1 | D → V in AAY15840. Ref.3 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Osteoblast-specific factor 2: cloning of a putative bone adhesion protein with homology with the insect protein fasciclin I." Takeshita S., Kikuno R., Tezuka K., Amann E. Biochem. J. 294:271-278(1993) [PubMed: 8363580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Osteosarcoma and Placenta. |
| [2] | "Periostin secreted by epithelial ovarian carcinoma is a ligand for alpha(V)beta(3) and alpha(V)beta(5) integrins and promotes cell motility." Gillan L., Matei D., Fishman D.A., Gerbin C.S., Karlan B.Y., Chang D.D. Cancer Res. 62:5358-5364(2002) [PubMed: 12235007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
| [3] | "Identification and characterization of a novel periodontal ligament-specific periostin isoform." Yamada S., Maeda K., Matsubara K., Murakami S. Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). Tissue: Periodontal ligament. |
| [4] | "The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. Ross M.T.Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). |
| [7] | "Serum level of the periostin, a homologue of an insect cell adhesion molecule, as a prognostic marker in nonsmall cell lung carcinomas." Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y., Fujii Y., Chen L.B. Cancer 92:843-848(2001) [PubMed: 11550156] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [8] | Erratum Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y., Fujii Y., Chen L.B. Cancer 95:2580-2580(2002) |
| [9] | "Acquired expression of periostin by human breast cancers promotes tumor angiogenesis through up-regulation of vascular endothelial growth factor receptor 2 expression." Shao R., Bao S., Bai X., Blanchette C., Anderson R.M., Dang T., Gishizky M.L., Marks J.R., Wang X.-F. Mol. Cell. Biol. 24:3992-4003(2004) [PubMed: 15082792] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [10] | "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599, MASS SPECTROMETRY. Tissue: Plasma. |
| [11] | "Periostin, a member of a novel family of vitamin K-dependent proteins, is expressed by mesenchymal stromal cells." Coutu D.L., Wu J.H., Monette A., Rivard G.-E., Blostein M.D., Galipeau J. J. Biol. Chem. 283:17991-18001(2008) [PubMed: 18450759] [Abstract] Cited for: FUNCTION, GAMMA-CARBOXYGLUTAMATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| D13665 mRNA. Translation: BAA02836.1. D13666 mRNA. Translation: BAA02837.1. AY140646 mRNA. Translation: AAN17733.1. AY918092 mRNA. Translation: AAY15840.1. AL138679, AL646087 Genomic DNA. Translation: CAH70107.1. AL646087, AL138679 Genomic DNA. Translation: CAH73568.1. AL138679, AL646087 Genomic DNA. Translation: CAH70104.1. AL646087, AL138679 Genomic DNA. Translation: CAH73569.1. CH471075 Genomic DNA. Translation: EAX08590.1. BC106709 mRNA. Translation: AAI06710.1. BC106710 mRNA. Translation: AAI06711.1. | |
| PIR | S36110. S36111. |
| RefSeq | NP_006466.1. |
| UniGene | Hs.136348 |

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