ID POSTN_HUMAN Reviewed; 836 AA. AC Q15063; B1ALD8; B1ALD9; C0IMJ1; C0IMJ2; C0IMJ4; D2KRH7; F5H628; Q15064; AC Q29XZ0; Q3KPJ5; Q5VSY5; Q8IZF9; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 27-MAR-2024, entry version 197. DE RecName: Full=Periostin; DE Short=PN; DE AltName: Full=Osteoblast-specific factor 2; DE Short=OSF-2; DE Flags: Precursor; GN Name=POSTN; Synonyms=OSF2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Osteosarcoma {ECO:0000269|PubMed:8363580}, and Placenta RC {ECO:0000269|PubMed:8363580}; RX PubMed=8363580; DOI=10.1042/bj2940271; RA Takeshita S., Kikuno R., Tezuka K., Amann E.; RT "Osteoblast-specific factor 2: cloning of a putative bone adhesion protein RT with homology with the insect protein fasciclin I."; RL Biochem. J. 294:271-278(1993). RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=12235007; RA Gillan L., Matei D., Fishman D.A., Gerbin C.S., Karlan B.Y., Chang D.D.; RT "Periostin secreted by epithelial ovarian carcinoma is a ligand for RT alpha(V)beta(3) and alpha(V)beta(5) integrins and promotes cell motility."; RL Cancer Res. 62:5358-5364(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5; 6; 7), ALTERNATIVE SPLICING, AND RP TISSUE SPECIFICITY. RX PubMed=23946676; DOI=10.4137/jcm.s5899; RA Bai Y., Nakamura M., Zhou G., Li Y., Liu Z., Ozaki T., Mori I., Kakudo K.; RT "Novel isoforms of periostin expressed in the human thyroid."; RL Jpn. Clin. Med. 1:13-20(2010). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RC TISSUE=Periodontal ligament; RA Yamada S., Maeda K., Matsubara K., Murakami S.; RT "Identification and characterization of a novel periodontal ligament- RT specific periostin isoform."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-798 (ISOFORM 5). RA Habtemichael N., Schweitzer A., Knauer S., Stauber R.H.; RT "OSF-2 expression in head and neck squamous cell carcinomas."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 629-836 (ISOFORMS 6; 7; 8 AND 9), TISSUE RP SPECIFICITY, AND ALTERNATIVE SPLICING. RX PubMed=21763681; DOI=10.1016/j.ajpath.2011.05.035; RA Morra L., Rechsteiner M., Casagrande S., Duc Luu V., Santimaria R., RA Diener P.A., Sulser T., Kristiansen G., Schraml P., Moch H., Soltermann A.; RT "Relevance of periostin splice variants in renal cell carcinoma."; RL Am. J. Pathol. 179:1513-1521(2011). RN [10] {ECO:0000305} RP TISSUE SPECIFICITY. RX PubMed=11550156; RX DOI=10.1002/1097-0142(20010815)92:4<843::aid-cncr1391>3.0.co;2-p; RA Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y., RA Fujii Y., Chen L.B.; RT "Serum level of the periostin, a homologue of an insect cell adhesion RT molecule, as a prognostic marker in nonsmall cell lung carcinomas."; RL Cancer 92:843-848(2001). RN [11] RP ERRATUM OF PUBMED:11550156. RA Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y., RA Fujii Y., Chen L.B.; RL Cancer 95:2580-2580(2002). RN [12] RP TISSUE SPECIFICITY. RX PubMed=15082792; DOI=10.1128/mcb.24.9.3992-4003.2004; RA Shao R., Bao S., Bai X., Blanchette C., Anderson R.M., Dang T., RA Gishizky M.L., Marks J.R., Wang X.-F.; RT "Acquired expression of periostin by human breast cancers promotes tumor RT angiogenesis through up-regulation of vascular endothelial growth factor RT receptor 2 expression."; RL Mol. Cell. Biol. 24:3992-4003(2004). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [14] RP SUBCELLULAR LOCATION, AND GAMMA-CARBOXYGLUTAMATION. RX PubMed=18450759; DOI=10.1074/jbc.m708029200; RA Coutu D.L., Wu J.H., Monette A., Rivard G.-E., Blostein M.D., Galipeau J.; RT "Periostin, a member of a novel family of vitamin K-dependent proteins, is RT expressed by mesenchymal stromal cells."; RL J. Biol. Chem. 283:17991-18001(2008). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [16] RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX PubMed=22079858; DOI=10.1016/j.lungcan.2011.10.013; RA Morra L., Rechsteiner M., Casagrande S., von Teichman A., Schraml P., RA Moch H., Soltermann A.; RT "Characterization of periostin isoform pattern in non-small cell lung RT cancer."; RL Lung Cancer 76:183-190(2012). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP SUBCELLULAR LOCATION, AND LACK OF GAMMA-CARBOXYGLUTAMATION. RX PubMed=26273833; DOI=10.1371/journal.pone.0135374; RA Annis D.S., Ma H., Balas D.M., Kumfer K.T., Sandbo N., Potts G.K., RA Coon J.J., Mosher D.F.; RT "Absence of vitamin K-dependent gamma-carboxylation in human periostin RT extracted from fibrotic lung or secreted from a cell line engineered to RT optimize gamma-carboxylation."; RL PLoS ONE 10:E0135374-E0135374(2015). RN [19] {ECO:0007744|PDB:5WT7} RP STRUCTURE BY NMR OF 496-632. RX PubMed=29086898; DOI=10.1007/s12104-017-9786-z; RA Yun H., Kim E.H., Lee C.W.; RT "1H, 13C, and 15N resonance assignments of FAS1-IV domain of human RT periostin, a component of extracellular matrix proteins."; RL Biomol. NMR. Assign. 12:95-98(2018). RN [20] {ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 22-631, SUBUNIT, DISULFIDE BONDS, RP CYSTEINYLATION AT CYS-60, AND MUTAGENESIS OF CYS-60 AND 463-ARG--ALA-465. RX PubMed=29754429; DOI=10.1002/1873-3468.13091; RA Liu J., Zhang J., Xu F., Lin Z., Li Z., Liu H.; RT "Structural characterizations of human periostin dimerization and RT cysteinylation."; RL FEBS Lett. 592:1789-1803(2018). CC -!- FUNCTION: Induces cell attachment and spreading and plays a role in CC cell adhesion (PubMed:12235007). Enhances incorporation of BMP1 in the CC fibronectin matrix of connective tissues, and subsequent proteolytic CC activation of lysyl oxidase LOX (By similarity). CC {ECO:0000250|UniProtKB:Q62009, ECO:0000269|PubMed:12235007}. CC -!- SUBUNIT: Homodimer (PubMed:29754429). Interacts with BMP1 and CC fibronectin. {ECO:0000250|UniProtKB:Q62009, CC ECO:0000269|PubMed:29754429}. CC -!- INTERACTION: CC Q15063; Q15582: TGFBI; NbExp=7; IntAct=EBI-7067070, EBI-10236573; CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q62009}. CC Secreted {ECO:0000269|PubMed:18450759, ECO:0000269|PubMed:26273833}. CC Secreted, extracellular space, extracellular matrix CC {ECO:0000269|PubMed:12235007, ECO:0000269|PubMed:18450759}. CC Note=Colocalizes with BMP1 in the Golgi. CC {ECO:0000250|UniProtKB:Q62009}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=10; CC Name=1 {ECO:0000269|PubMed:8363580}; Synonyms=OSF-2OS CC {ECO:0000303|PubMed:8363580}; CC IsoId=Q15063-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:8363580}; Synonyms=OSF-2p1; CC IsoId=Q15063-2; Sequence=VSP_050005; CC Name=3 {ECO:0000269|PubMed:12235007}; CC IsoId=Q15063-3; Sequence=VSP_050669, VSP_050670; CC Name=4; CC IsoId=Q15063-4; Sequence=VSP_050005, VSP_050670; CC Name=5; CC IsoId=Q15063-5; Sequence=VSP_050669; CC Name=6; CC IsoId=Q15063-6; Sequence=VSP_055183; CC Name=7; CC IsoId=Q15063-7; Sequence=VSP_055183, VSP_050670; CC Name=8; CC IsoId=Q15063-8; Sequence=VSP_050670; CC Name=9; CC IsoId=Q15063-9; Sequence=VSP_062248; CC Name=10; CC IsoId=Q15063-10; Sequence=VSP_062248, VSP_050670; CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in aorta, CC stomach, lower gastrointestinal tract, placenta, uterus, thyroid tissue CC and breast. Expressed in the kidney (PubMed:21763681). Expressed in the CC lung (PubMed:22079858). Up-regulated in epithelial ovarian tumors. Not CC expressed in normal ovaries. Also highly expressed at the tumor CC periphery of lung carcinoma tissue but not within the tumor. CC Overexpressed in breast cancers. {ECO:0000269|PubMed:11550156, CC ECO:0000269|PubMed:12235007, ECO:0000269|PubMed:15082792, CC ECO:0000269|PubMed:21763681, ECO:0000269|PubMed:22079858, CC ECO:0000269|PubMed:23946676}. CC -!- PTM: Gamma-carboxylation is controversial. Gamma-carboxyglutamated; CC gamma-carboxyglutamate residues are formed by vitamin K dependent CC carboxylation; this may be required for calcium binding CC (PubMed:18450759). According to a more recent report, does not contain CC vitamin K-dependent gamma-carboxyglutamate residues (PubMed:26273833). CC {ECO:0000269|PubMed:18450759, ECO:0000269|PubMed:26273833}. 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; D13665; BAA02836.1; -; mRNA. DR EMBL; D13666; BAA02837.1; -; mRNA. DR EMBL; AY140646; AAN17733.1; -; mRNA. DR EMBL; EU262883; ABY86630.1; -; mRNA. DR EMBL; EU262884; ABY86631.1; -; mRNA. DR EMBL; EU262886; ABY86633.1; -; mRNA. DR EMBL; AY918092; AAY15840.1; -; mRNA. DR EMBL; AL138679; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL646087; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08590.1; -; Genomic_DNA. DR EMBL; BC106709; AAI06710.1; -; mRNA. DR EMBL; BC106710; AAI06711.1; -; mRNA. DR EMBL; GU354210; ADA79517.1; -; mRNA. DR EMBL; JG969042; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; JG969043; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; JG969044; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; JG969045; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS45034.1; -. [Q15063-2] DR CCDS; CCDS53864.1; -. [Q15063-3] DR CCDS; CCDS66530.1; -. [Q15063-6] DR CCDS; CCDS66531.1; -. [Q15063-5] DR CCDS; CCDS9364.1; -. [Q15063-1] DR PIR; S36110; S36110. DR PIR; S36111; S36111. DR RefSeq; NP_001129406.1; NM_001135934.1. [Q15063-2] DR RefSeq; NP_001129407.1; NM_001135935.1. [Q15063-3] DR RefSeq; NP_001129408.1; NM_001135936.1. [Q15063-4] DR RefSeq; NP_001273594.1; NM_001286665.1. [Q15063-5] DR RefSeq; NP_001273595.1; NM_001286666.1. [Q15063-6] DR RefSeq; NP_001273596.1; NM_001286667.1. [Q15063-7] DR RefSeq; NP_001317446.1; NM_001330517.1. DR RefSeq; NP_006466.2; NM_006475.2. [Q15063-1] DR PDB; 5WT7; NMR; -; A=496-632. DR PDB; 5YJG; X-ray; 2.40 A; A=22-631. DR PDB; 5YJH; X-ray; 2.96 A; A=17-631. DR PDBsum; 5WT7; -. DR PDBsum; 5YJG; -. DR PDBsum; 5YJH; -. DR AlphaFoldDB; Q15063; -. DR SMR; Q15063; -. DR BioGRID; 115875; 7. DR IntAct; Q15063; 5. DR MINT; Q15063; -. DR STRING; 9606.ENSP00000369071; -. DR GlyConnect; 1599; 66 N-Linked glycans (1 site). DR GlyCosmos; Q15063; 2 sites, 63 glycans. DR GlyGen; Q15063; 3 sites, 62 N-linked glycans (1 site), 2 O-linked glycans (2 sites). DR iPTMnet; Q15063; -. DR PhosphoSitePlus; Q15063; -. DR SwissPalm; Q15063; -. DR BioMuta; POSTN; -. DR DMDM; 93138709; -. DR EPD; Q15063; -. DR jPOST; Q15063; -. DR MassIVE; Q15063; -. DR MaxQB; Q15063; -. DR PaxDb; 9606-ENSP00000369071; -. DR PeptideAtlas; Q15063; -. DR ProteomicsDB; 27060; -. DR ProteomicsDB; 3153; -. DR ProteomicsDB; 60417; -. [Q15063-1] DR ProteomicsDB; 60418; -. [Q15063-2] DR ProteomicsDB; 60419; -. [Q15063-3] DR ProteomicsDB; 60420; -. [Q15063-4] DR ABCD; Q15063; 4 sequenced antibodies. DR Antibodypedia; 2020; 775 antibodies from 47 providers. DR DNASU; 10631; -. DR Ensembl; ENST00000379742.4; ENSP00000369066.4; ENSG00000133110.15. [Q15063-2] DR Ensembl; ENST00000379743.8; ENSP00000369067.4; ENSG00000133110.15. [Q15063-5] DR Ensembl; ENST00000379747.9; ENSP00000369071.4; ENSG00000133110.15. [Q15063-1] DR Ensembl; ENST00000541179.5; ENSP00000437959.1; ENSG00000133110.15. [Q15063-3] DR Ensembl; ENST00000541481.5; ENSP00000437953.1; ENSG00000133110.15. [Q15063-6] DR GeneID; 10631; -. DR KEGG; hsa:10631; -. DR MANE-Select; ENST00000379747.9; ENSP00000369071.4; NM_006475.3; NP_006466.2. DR UCSC; uc001uwo.5; human. [Q15063-1] DR AGR; HGNC:16953; -. DR CTD; 10631; -. DR DisGeNET; 10631; -. DR GeneCards; POSTN; -. DR HGNC; HGNC:16953; POSTN. DR HPA; ENSG00000133110; Tissue enhanced (skin, stomach). DR MIM; 608777; gene. DR neXtProt; NX_Q15063; -. DR OpenTargets; ENSG00000133110; -. DR PharmGKB; PA134900304; -. DR VEuPathDB; HostDB:ENSG00000133110; -. DR eggNOG; KOG1437; Eukaryota. DR GeneTree; ENSGT00530000063860; -. DR HOGENOM; CLU_017611_0_0_1; -. DR InParanoid; Q15063; -. DR OMA; LHQVDRP; -. DR OrthoDB; 523796at2759; -. DR PhylomeDB; Q15063; -. DR TreeFam; TF316269; -. DR PathwayCommons; Q15063; -. DR SignaLink; Q15063; -. DR SIGNOR; Q15063; -. DR BioGRID-ORCS; 10631; 14 hits in 1153 CRISPR screens. DR ChiTaRS; POSTN; human. DR GeneWiki; Periostin; -. DR GeneWiki; POSTN; -. DR GenomeRNAi; 10631; -. DR Pharos; Q15063; Tbio. DR PRO; PR:Q15063; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q15063; Protein. DR Bgee; ENSG00000133110; Expressed in periodontal ligament and 177 other cell types or tissues. DR ExpressionAtlas; Q15063; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl. DR GO; GO:0005802; C:trans-Golgi network; IDA:BHF-UCL. DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central. DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB. DR GO; GO:1990523; P:bone regeneration; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0071307; P:cellular response to vitamin K; IDA:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl. DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl. DR GO; GO:1990138; P:neuron projection extension; IEA:Ensembl. DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IEA:Ensembl. DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl. DR GO; GO:0008593; P:regulation of Notch signaling pathway; IEA:Ensembl. DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl. DR GO; GO:0009888; P:tissue development; IEA:Ensembl. DR Gene3D; 2.30.180.10; FAS1 domain; 4. DR InterPro; IPR011489; EMI_domain. DR InterPro; IPR036378; FAS1_dom_sf. DR InterPro; IPR000782; FAS1_domain. DR InterPro; IPR016666; TGFBI/POSTN. DR PANTHER; PTHR10900:SF77; FI19380P1; 1. DR PANTHER; PTHR10900; PERIOSTIN-RELATED; 1. DR Pfam; PF02469; Fasciclin; 4. DR PIRSF; PIRSF016553; BIGH3_OSF2; 1. DR SMART; SM00554; FAS1; 4. DR SUPFAM; SSF82153; FAS1 domain; 4. DR PROSITE; PS51041; EMI; 1. DR PROSITE; PS50213; FAS1; 4. DR Genevisible; Q15063; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Disulfide bond; KW Extracellular matrix; Gamma-carboxyglutamic acid; Glycoprotein; KW Golgi apparatus; Heparin-binding; Reference proteome; Repeat; Secreted; KW Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..836 FT /note="Periostin" FT /id="PRO_0000008789" FT DOMAIN 40..94 FT /note="EMI" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384" FT DOMAIN 97..230 FT /note="FAS1 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 234..365 FT /note="FAS1 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 368..492 FT /note="FAS1 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 496..628 FT /note="FAS1 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT MOD_RES 60 FT /note="S-cysteinyl cysteine" FT /evidence="ECO:0000269|PubMed:29754429" FT CARBOHYD 599 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT DISULFID 44..80 FT /evidence="ECO:0000269|PubMed:29754429, FT ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH" FT DISULFID 69..333 FT /evidence="ECO:0000269|PubMed:29754429, FT ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH" FT DISULFID 79..92 FT /evidence="ECO:0000269|PubMed:29754429, FT ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH" FT DISULFID 208..311 FT /evidence="ECO:0000269|PubMed:29754429, FT ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH" FT DISULFID 467..472 FT /evidence="ECO:0000269|PubMed:29754429, FT ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH" FT VAR_SEQ 670..757 FT /note="TTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPEFRLIKEGETIT FT EVIHGEPIIKKYTKIIDGVPVEITEKETREERIITG -> S (in isoform 6 and FT isoform 7)" FT /evidence="ECO:0000269|PubMed:21763681, FT ECO:0000303|PubMed:23946676" FT /id="VSP_055183" FT VAR_SEQ 670..727 FT /note="TTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPEFRLIKEGETIT FT EVIHGE -> K (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8363580, ECO:0000303|Ref.4" FT /id="VSP_050005" FT VAR_SEQ 670..697 FT /note="TTKIITKVVEPKIKVIEGSLQPIIKTEG -> R (in isoform 3 and FT isoform 5)" FT /evidence="ECO:0000303|PubMed:12235007, FT ECO:0000303|PubMed:23946676, ECO:0000303|Ref.8" FT /id="VSP_050669" FT VAR_SEQ 697..726 FT /note="Missing (in isoform 9 and isoform 10)" FT /evidence="ECO:0000269|PubMed:21763681, FT ECO:0000269|PubMed:22079858" FT /id="VSP_062248" FT VAR_SEQ 783..810 FT /note="Missing (in isoform 3, isoform 4, isoform 7, isoform FT 8 and isoform 10)" FT /evidence="ECO:0000269|PubMed:21763681, FT ECO:0000269|PubMed:22079858, ECO:0000303|PubMed:12235007, FT ECO:0000303|PubMed:23946676, ECO:0000303|Ref.4" FT /id="VSP_050670" FT VARIANT 339 FT /note="T -> I (in dbSNP:rs9594223)" FT /id="VAR_049115" FT VARIANT 814 FT /note="V -> M (in dbSNP:rs9547952)" FT /id="VAR_049116" FT MUTAGEN 60 FT /note="C->A: No effect on homodimerization." FT /evidence="ECO:0000269|PubMed:29754429" FT MUTAGEN 463..465 FT /note="RTA->NTS: Loss of homodimerization." FT /evidence="ECO:0000269|PubMed:29754429" FT CONFLICT 290 FT /note="I -> F (in Ref. 1; BAA02836/BAA02837, 3; FT ABY86630/ABY86631/ABY86633 and 4; AAY15840)" FT /evidence="ECO:0000305" FT CONFLICT 421 FT /note="D -> V (in Ref. 1; BAA02836/BAA02837, 3; FT ABY86630/ABY86631/ABY86633 and 4; AAY15840)" FT /evidence="ECO:0000305" FT STRAND 43..49 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 55..62 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 73..79 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 101..107 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 111..119 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 123..126 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 139..144 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 147..154 FT /evidence="ECO:0007829|PDB:5YJG" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 160..167 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 169..172 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 193..198 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 209..218 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 221..228 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 237..243 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 248..257 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 269..274 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 276..281 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 286..292 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 294..302 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 305..308 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 312..314 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 319..323 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 326..334 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 337..340 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 346..353 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 356..363 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 368..370 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 373..376 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 379..381 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 382..390 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 394..396 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 403..408 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 410..412 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 415..418 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 422..430 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 433..436 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 440..442 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 448..451 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 456..461 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 466..468 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 481..490 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 499..505 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 507..509 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 510..518 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 522..526 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 527..529 FT /evidence="ECO:0007829|PDB:5WT7" FT STRAND 531..536 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 538..542 FT /evidence="ECO:0007829|PDB:5YJG" FT TURN 543..546 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 547..553 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 558..564 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 567..570 FT /evidence="ECO:0007829|PDB:5YJG" FT HELIX 574..576 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 582..586 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 590..598 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 601..606 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 614..616 FT /evidence="ECO:0007829|PDB:5YJG" FT STRAND 619..626 FT /evidence="ECO:0007829|PDB:5YJG" SQ SEQUENCE 836 AA; 93314 MW; 55E7B82D094824FD CRC64; MIPFLPMFSL LLLLIVNPIN ANNHYDKILA HSRIRGRDQG PNVCALQQIL GTKKKYFSTC KNWYKKSICG QKTTVLYECC PGYMRMEGMK GCPAVLPIDH VYGTLGIVGA TTTQRYSDAS KLREEIEGKG SFTYFAPSNE AWDNLDSDIR RGLESNVNVE LLNALHSHMI NKRMLTKDLK NGMIIPSMYN NLGLFINHYP NGVVTVNCAR IIHGNQIATN GVVHVIDRVL TQIGTSIQDF IEAEDDLSSF RAAAITSDIL EALGRDGHFT LFAPTNEAFE KLPRGVLERI MGDKVASEAL MKYHILNTLQ CSESIMGGAV FETLEGNTIE IGCDGDSITV NGIKMVNKKD IVTNNGVIHL IDQVLIPDSA KQVIELAGKQ QTTFTDLVAQ LGLASALRPD GEYTLLAPVN NAFSDDTLSM DQRLLKLILQ NHILKVKVGL NELYNGQILE TIGGKQLRVF VYRTAVCIEN SCMEKGSKQG RNGAIHIFRE IIKPAEKSLH EKLKQDKRFS TFLSLLEAAD LKELLTQPGD WTLFVPTNDA FKGMTSEEKE ILIRDKNALQ NIILYHLTPG VFIGKGFEPG VTNILKTTQG SKIFLKEVND TLLVNELKSK ESDIMTTNGV IHVVDKLLYP ADTPVGNDQL LEILNKLIKY IQIKFVRGST FKEIPVTVYT TKIITKVVEP KIKVIEGSLQ PIIKTEGPTL TKVKIEGEPE FRLIKEGETI TEVIHGEPII KKYTKIIDGV PVEITEKETR EERIITGPEI KYTRISTGGG ETEETLKKLL QEEVTKVTKF IEGGDGHLFE DEEIKRLLQG DTPVRKLQAN KKVQGSRRRL REGRSQ //