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Q62009 (POSTN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Periostin

Short name=PN
Alternative name(s):
Osteoblast-specific factor 2
Short name=OSF-2
Gene names
Name:Postn
Synonyms:Osf2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length838 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Induces cell attachment and spreading and plays a role in cell adhesion. May play a role in extracellular matrix mineralization. Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX. Ref.4 Ref.8

Subunit structure

Interacts with BMP1 and fibronectin. Ref.8

Subcellular location

Golgi apparatus. Secretedextracellular spaceextracellular matrix. Note: Colocalizes with BMP1 in the Golgi. Ref.4 Ref.8

Tissue specificity

Preferentially expressed in periosteum and periodontal ligament. Also expressed in the developing and adult heart. Ref.4 Ref.6

Developmental stage

In the heart, expressed from embryonic day 10.5. Continues to be strongly expressed throughout cardiac development and into adulthood. Ref.6

Induction

By TGF-beta. Ref.4

Post-translational modification

Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium.

Disruption phenotype

Reduced amount of collagen cross-linking in femur and periosteum. Ref.8

Sequence similarities

Contains 1 EMI domain.

Contains 4 FAS1 domains.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.4 (identifier: Q62009-1)

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 Ref.4 (identifier: Q62009-2)

The sequence of this isoform differs from the canonical sequence as follows:
     672-699: TTKIITKVVEPKIKVIQGSLQPIIKTEG → R
Isoform 3 Ref.4 (identifier: Q62009-3)

The sequence of this isoform differs from the canonical sequence as follows:
     785-812: Missing.
Isoform 4 Ref.4 (identifier: Q62009-4)

The sequence of this isoform differs from the canonical sequence as follows:
     759-812: Missing.
Isoform 5 (identifier: Q62009-5)

The sequence of this isoform differs from the canonical sequence as follows:
     672-699: TTKIITKVVEPKIKVIQGSLQPIIKTEG → R
     785-812: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 838815Periostin
PRO_0000008790

Regions

Domain42 – 9655EMI
Domain99 – 232134FAS1 1
Domain236 – 367132FAS1 2
Domain370 – 494125FAS1 3
Domain498 – 630133FAS1 4

Amino acid modifications

Modified residue12614-carboxyglutamate Potential
Modified residue12714-carboxyglutamate Potential
Modified residue12914-carboxyglutamate Potential
Modified residue14214-carboxyglutamate Potential
Modified residue15614-carboxyglutamate Potential
Modified residue16214-carboxyglutamate Potential
Modified residue24414-carboxyglutamate Potential
Modified residue24614-carboxyglutamate Potential
Modified residue26314-carboxyglutamate Potential
Modified residue27914-carboxyglutamate Potential
Modified residue28214-carboxyglutamate Potential
Modified residue29014-carboxyglutamate Potential
Modified residue30014-carboxyglutamate Potential
Modified residue31514-carboxyglutamate Potential
Modified residue32414-carboxyglutamate Potential
Modified residue32714-carboxyglutamate Potential
Modified residue49814-carboxyglutamate Potential
Modified residue51914-carboxyglutamate Potential
Modified residue54914-carboxyglutamate Potential
Modified residue55014-carboxyglutamate Potential
Modified residue55214-carboxyglutamate Potential
Modified residue58014-carboxyglutamate Potential
Glycosylation6011N-linked (GlcNAc...) Probable Ref.5
Disulfide bond46 ↔ 82 By similarity
Disulfide bond62 ↔ 71 By similarity
Disulfide bond81 ↔ 94 By similarity

Natural variations

Alternative sequence672 – 69928TTKII…IKTEG → R in isoform 2 and isoform 5. Ref.4
VSP_050666
Alternative sequence759 – 81254Missing in isoform 4. Ref.4
VSP_050667
Alternative sequence785 – 81228Missing in isoform 3 and isoform 5. Ref.4
VSP_050668

Experimental info

Sequence conflict3461K → R in BAC27122. Ref.2
Sequence conflict5411D → N in BAC27122. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 2, 2004. Version 2.
Checksum: 907FEB37942EADEC

FASTA83893,144
        10         20         30         40         50         60 
MVPLLPLYAL LLLFLCDINP ANANSYYDKV LAHSRIRGRD QGPNVCALQQ ILGTKKKYFS 

        70         80         90        100        110        120 
SCKNWYQGAI CGKKTTVLYE CCPGYMRMEG MKGCPAVMPI DHVYGTLGIV GATTTQHYSD 

       130        140        150        160        170        180 
VSKLREEIEG KGSYTYFAPS NEAWENLDSD IRRGLENNVN VELLNALHSH MVNKRMLTKD 

       190        200        210        220        230        240 
LKHGMVIPSM YNNLGLFINH YPNGVVTVNC ARVIHGNQIA TNGVVHVIDR VLTQIGTSIQ 

       250        260        270        280        290        300 
DFLEAEDDLS SFRAAAITSD LLESLGRDGH FTLFAPTNEA FEKLPRGVLE RIMGDKVASE 

       310        320        330        340        350        360 
ALMKYHILNT LQCSEAITGG AVFETMEGNT IEIGCEGDSI SINGIKMVNK KDIVTKNGVI 

       370        380        390        400        410        420 
HLIDEVLIPD SAKQVIELAG KQQTTFTDLV AQLGLASSLK PDGEYTLLAP VNNAFSDDTL 

       430        440        450        460        470        480 
SMDQRLLKLI LQNHILKVKV GLSDLYNGQI LETIGGKQLR VFVYRTAICI ENSCMVRGSK 

       490        500        510        520        530        540 
QGRNGAIHIF REIIQPAEKS LHDKLRQDKR FSIFLSLLEA ADLKDLLTQP GDWTLFAPTN 

       550        560        570        580        590        600 
DAFKGMTSEE RELLIGDKNA LQNIILYHLT PGVYIGKGFE PGVTNILKTT QGSKIYLKGV 

       610        620        630        640        650        660 
NETLLVNELK SKESDIMTTN GVIHVVDKLL YPADIPVGND QLLELLNKLI KYIQIKFVRG 

       670        680        690        700        710        720 
STFKEIPMTV YTTKIITKVV EPKIKVIQGS LQPIIKTEGP AMTKIQIEGD PDFRLIKEGE 

       730        740        750        760        770        780 
TVTEVIHGEP VIKKYTKIID GVPVEITEKQ TREERIITGP EIKYTRISTG GGETGETLQK 

       790        800        810        820        830 
FLQKEVSKVT KFIEGGDGHL FEDEEIKRLL QGDTPAKKIP ANKRVQGPRR RSREGRSQ 

« Hide

Isoform 2 [UniParc].

Checksum: DA5CE8F8B9380234
Show »

FASTA81190,255
Isoform 3 [UniParc].

Checksum: 7CF602BDD3BAB995
Show »

FASTA81089,987
Isoform 4 [UniParc].

Checksum: 915027B89E47A6C3
Show »

FASTA78487,166
Isoform 5 [UniParc].

Checksum: 24B93AB348C9A7FE
Show »

FASTA78387,099

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: C57BL/6.
Tissue: Calvaria.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Strain: C57BL/6J.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Mammary gland.
[4]"Identification and characterization of a novel protein, periostin, with restricted expression to periosteum and periodontal ligament and increased expression by transforming growth factor beta."
Horiuchi K., Amizuka N., Takeshita S., Takamatsu H., Katsuura M., Ozawa H., Toyama Y., Bonewald L.F., Kudo A.
J. Bone Miner. Res. 14:1239-1249(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 3 AND 4), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[5]"Expression and characterization of murine osteoblast-specific factor 2 (OSF-2) in a baculovirus expression system."
Sugiura T., Takamatsu H., Kudo A., Amann E.
Protein Expr. Purif. 6:305-311(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: HEPARIN-BINDING ACTIVITY, GLYCOSYLATION.
[6]"Periostin (an osteoblast-specific factor) is expressed within the embryonic mouse heart during valve formation."
Kruzynska-Frejtag A., Machnicki M., Rogers R., Markwald R.R., Conway S.J.
Mech. Dev. 103:183-188(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"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] [Europe PMC] [Abstract]
Cited for: GAMMA-CARBOXYGLUTAMATION.
[8]"Interaction between periostin and BMP-1 promotes proteolytic activation of lysyl oxidase."
Maruhashi T., Kii I., Saito M., Kudo A.
J. Biol. Chem. 285:13294-13303(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BMP1 AND FIBRONECTIN, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13664 mRNA. Translation: BAA02835.1.
AK030756 mRNA. Translation: BAC27122.1.
BC031449 mRNA. Translation: AAH31449.1.
CCDSCCDS17351.1. [Q62009-2]
CCDS57211.1. [Q62009-3]
CCDS57212.1. [Q62009-5]
PIRS36109.
RefSeqNP_001185694.1. NM_001198765.1. [Q62009-3]
NP_001185695.1. NM_001198766.1. [Q62009-5]
NP_056599.1. NM_015784.3. [Q62009-2]
XP_006501716.1. XM_006501653.1. [Q62009-1]
XP_006501717.1. XM_006501654.1. [Q62009-4]
UniGeneMm.236067.

3D structure databases

ProteinModelPortalQ62009.
SMRQ62009. Positions 124-238, 241-369, 500-632.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ62009. 1 interaction.
MINTMINT-4108229.

PTM databases

PhosphoSiteQ62009.

Proteomic databases

MaxQBQ62009.
PaxDbQ62009.
PRIDEQ62009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000073012; ENSMUSP00000072773; ENSMUSG00000027750. [Q62009-2]
ENSMUST00000081564; ENSMUSP00000080276; ENSMUSG00000027750. [Q62009-1]
ENSMUST00000107985; ENSMUSP00000103619; ENSMUSG00000027750. [Q62009-3]
ENSMUST00000117373; ENSMUSP00000112735; ENSMUSG00000027750. [Q62009-5]
GeneID50706.
KEGGmmu:50706.
UCSCuc008pfh.2. mouse. [Q62009-2]
uc008pfi.2. mouse. [Q62009-3]
uc008pfj.2. mouse. [Q62009-5]

Organism-specific databases

CTD10631.
MGIMGI:1926321. Postn.

Phylogenomic databases

eggNOGCOG2335.
GeneTreeENSGT00530000063860.
HOGENOMHOG000220865.
HOVERGENHBG000715.
InParanoidQ62009.
OMAHGEPIIK.
OrthoDBEOG7N8ZV1.
PhylomeDBQ62009.
TreeFamTF316269.

Gene expression databases

BgeeQ62009.
CleanExMM_POSTN.
GenevestigatorQ62009.

Family and domain databases

Gene3D2.30.180.10. 4 hits.
InterProIPR011489. EMI_domain.
IPR000782. FAS1_domain.
IPR016666. TGFb-ind_bIGH3/osteoblast_fac2.
[Graphical view]
PfamPF02469. Fasciclin. 4 hits.
[Graphical view]
PIRSFPIRSF016553. BIGH3_OSF2. 1 hit.
SMARTSM00554. FAS1. 4 hits.
[Graphical view]
SUPFAMSSF82153. SSF82153. 4 hits.
PROSITEPS51041. EMI. 1 hit.
PS50213. FAS1. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio307557.
PROQ62009.
SOURCESearch...

Entry information

Entry namePOSTN_MOUSE
AccessionPrimary (citable) accession number: Q62009
Secondary accession number(s): Q8BMJ6, Q8K1K0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: February 2, 2004
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot