POSTN_MOUSE
ID POSTN_MOUSE Reviewed; 838 AA.
AC Q62009; Q8BMJ6; Q8K1K0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:8363580};
RC TISSUE=Calvaria {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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH31449.1};
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 [4] {ECO:0000305}
RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 3 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10404027; DOI=10.1359/jbmr.1999.14.7.1239;
RA Horiuchi K., Amizuka N., Takeshita S., Takamatsu H., Katsuura M., Ozawa H.,
RA Toyama Y., Bonewald L.F., Kudo A.;
RT "Identification and characterization of a novel protein, periostin, with
RT restricted expression to periosteum and periodontal ligament and increased
RT expression by transforming growth factor beta.";
RL J. Bone Miner. Res. 14:1239-1249(1999).
RN [5] {ECO:0000305}
RP HEPARIN-BINDING ACTIVITY, AND GLYCOSYLATION.
RX PubMed=7663166; DOI=10.1006/prep.1995.1040;
RA Sugiura T., Takamatsu H., Kudo A., Amann E.;
RT "Expression and characterization of murine osteoblast-specific factor 2
RT (OSF-2) in a baculovirus expression system.";
RL Protein Expr. Purif. 6:305-311(1995).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11335131; DOI=10.1016/s0925-4773(01)00356-2;
RA Kruzynska-Frejtag A., Machnicki M., Rogers R., Markwald R.R., Conway S.J.;
RT "Periostin (an osteoblast-specific factor) is expressed within the
RT embryonic mouse heart during valve formation.";
RL Mech. Dev. 103:183-188(2001).
RN [7]
RP GAMMA-CARBOXYGLUTAMATION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, INTERACTION WITH BMP1 AND FIBRONECTIN, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20181949; DOI=10.1074/jbc.m109.088864;
RA Maruhashi T., Kii I., Saito M., Kudo A.;
RT "Interaction between periostin and BMP-1 promotes proteolytic activation of
RT lysyl oxidase.";
RL J. Biol. Chem. 285:13294-13303(2010).
CC -!- FUNCTION: Induces cell attachment and spreading and plays a role in
CC cell adhesion (PubMed:10404027). Enhances incorporation of BMP1 in the
CC fibronectin matrix of connective tissues, and subsequent proteolytic
CC activation of lysyl oxidase LOX (PubMed:20181949).
CC {ECO:0000269|PubMed:10404027, ECO:0000269|PubMed:20181949}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with BMP1 and fibronectin
CC (PubMed:20181949). {ECO:0000250|UniProtKB:Q15063,
CC ECO:0000269|PubMed:20181949}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:20181949}.
CC Secreted {ECO:0000269|PubMed:10404027, ECO:0000269|PubMed:18450759}.
CC Secreted, extracellular space, extracellular matrix
CC {ECO:0000269|PubMed:10404027}. Note=Colocalizes with BMP1 in the Golgi
CC (PubMed:20181949). {ECO:0000269|PubMed:20181949}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1 {ECO:0000269|PubMed:10404027};
CC IsoId=Q62009-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10404027};
CC IsoId=Q62009-2; Sequence=VSP_050666;
CC Name=3 {ECO:0000269|PubMed:10404027};
CC IsoId=Q62009-3; Sequence=VSP_050668;
CC Name=4 {ECO:0000269|PubMed:10404027};
CC IsoId=Q62009-4; Sequence=VSP_050667;
CC Name=5 {ECO:0000305};
CC IsoId=Q62009-5; Sequence=VSP_050666, VSP_050668;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in periosteum and
CC periodontal ligament (PubMed:10404027). Also expressed in the
CC developing and adult heart (PubMed:11335131).
CC {ECO:0000269|PubMed:10404027, ECO:0000269|PubMed:11335131}.
CC -!- DEVELOPMENTAL STAGE: In the heart, expressed from embryonic day 10.5.
CC Continues to be strongly expressed throughout cardiac development and
CC into adulthood (PubMed:11335131). {ECO:0000269|PubMed:11335131}.
CC -!- INDUCTION: By TGF-beta (PubMed:11335131).
CC {ECO:0000269|PubMed:11335131}.
CC -!- PTM: Gamma-carboxylation is controversial. Gamma-carboxyglutamated;
CC gamma-carboxyglutamate residues are formed by vitamin K dependent
CC carboxylation; these residues may be required for binding to calcium
CC (PubMed:18450759). According to a more recent report in human, does not
CC contain vitamin K-dependent gamma-carboxyglutamate residues (By
CC similarity). {ECO:0000250|UniProtKB:Q15063,
CC ECO:0000269|PubMed:18450759}.
CC -!- DISRUPTION PHENOTYPE: Reduced amount of collagen cross-linking in femur
CC and periosteum (PubMed:20181949). {ECO:0000269|PubMed:20181949}.
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DR EMBL; D13664; BAA02835.1; -; mRNA.
DR EMBL; AK030756; BAC27122.1; -; mRNA.
DR EMBL; BC031449; AAH31449.1; -; mRNA.
DR CCDS; CCDS17351.1; -. [Q62009-2]
DR CCDS; CCDS57211.1; -. [Q62009-3]
DR CCDS; CCDS57212.1; -. [Q62009-5]
DR CCDS; CCDS89624.1; -. [Q62009-1]
DR PIR; S36109; S36109.
DR RefSeq; NP_001185694.1; NM_001198765.1. [Q62009-3]
DR RefSeq; NP_001185695.1; NM_001198766.1. [Q62009-5]
DR RefSeq; NP_056599.1; NM_015784.3. [Q62009-2]
DR RefSeq; XP_006501716.1; XM_006501653.2.
DR AlphaFoldDB; Q62009; -.
DR SMR; Q62009; -.
DR BioGRID; 206060; 6.
DR IntAct; Q62009; 1.
DR MINT; Q62009; -.
DR STRING; 10090.ENSMUSP00000072773; -.
DR GlyGen; Q62009; 1 site.
DR iPTMnet; Q62009; -.
DR PhosphoSitePlus; Q62009; -.
DR CPTAC; non-CPTAC-3739; -.
DR MaxQB; Q62009; -.
DR PaxDb; Q62009; -.
DR PeptideAtlas; Q62009; -.
DR PRIDE; Q62009; -.
DR ProteomicsDB; 289364; -. [Q62009-1]
DR ProteomicsDB; 289365; -. [Q62009-2]
DR ProteomicsDB; 289366; -. [Q62009-3]
DR ProteomicsDB; 289367; -. [Q62009-4]
DR ProteomicsDB; 289368; -. [Q62009-5]
DR Antibodypedia; 2020; 669 antibodies from 47 providers.
DR DNASU; 50706; -.
DR Ensembl; ENSMUST00000073012; ENSMUSP00000072773; ENSMUSG00000027750. [Q62009-2]
DR Ensembl; ENSMUST00000081564; ENSMUSP00000080276; ENSMUSG00000027750. [Q62009-1]
DR Ensembl; ENSMUST00000107985; ENSMUSP00000103619; ENSMUSG00000027750. [Q62009-3]
DR Ensembl; ENSMUST00000117373; ENSMUSP00000112735; ENSMUSG00000027750. [Q62009-5]
DR GeneID; 50706; -.
DR KEGG; mmu:50706; -.
DR UCSC; uc008pfh.2; mouse. [Q62009-2]
DR UCSC; uc008pfi.2; mouse. [Q62009-3]
DR UCSC; uc008pfj.2; mouse. [Q62009-5]
DR CTD; 10631; -.
DR MGI; MGI:1926321; Postn.
DR VEuPathDB; HostDB:ENSMUSG00000027750; -.
DR eggNOG; KOG1437; Eukaryota.
DR GeneTree; ENSGT00530000063860; -.
DR HOGENOM; CLU_017611_0_0_1; -.
DR InParanoid; Q62009; -.
DR OMA; VFVYRTX; -.
DR OrthoDB; 1437416at2759; -.
DR PhylomeDB; Q62009; -.
DR TreeFam; TF316269; -.
DR BioGRID-ORCS; 50706; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Postn; mouse.
DR PRO; PR:Q62009; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q62009; protein.
DR Bgee; ENSMUSG00000027750; Expressed in secondary palatal shelf and 260 other tissues.
DR ExpressionAtlas; Q62009; baseline and differential.
DR Genevisible; Q62009; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0071307; P:cellular response to vitamin K; IDA:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:1990138; P:neuron projection extension; ISO:MGI.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:MGI.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISO:MGI.
DR GO; GO:0009888; P:tissue development; IMP:MGI.
DR Gene3D; 2.30.180.10; -; 4.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR016666; TGFBI/POSTN.
DR Pfam; PF02469; Fasciclin; 4.
DR PIRSF; PIRSF016553; BIGH3_OSF2; 1.
DR SMART; SM00554; FAS1; 4.
DR SUPFAM; SSF82153; SSF82153; 4.
DR PROSITE; PS51041; EMI; 1.
DR PROSITE; PS50213; FAS1; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Disulfide bond; Extracellular matrix;
KW Gamma-carboxyglutamic acid; Glycoprotein; Golgi apparatus; Heparin-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..838
FT /note="Periostin"
FT /id="PRO_0000008790"
FT DOMAIN 42..96
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 99..232
FT /note="FAS1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 236..367
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 370..494
FT /note="FAS1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 498..630
FT /note="FAS1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT REGION 811..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="S-cysteinyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q15063"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000303|PubMed:7663166"
FT DISULFID 46..82
FT /evidence="ECO:0000250|UniProtKB:Q15063"
FT DISULFID 71..335
FT /evidence="ECO:0000250|UniProtKB:Q15063"
FT DISULFID 81..94
FT /evidence="ECO:0000250|UniProtKB:Q15063"
FT DISULFID 210..313
FT /evidence="ECO:0000250|UniProtKB:Q15063"
FT DISULFID 469..474
FT /evidence="ECO:0000250|UniProtKB:Q15063"
FT VAR_SEQ 672..699
FT /note="TTKIITKVVEPKIKVIQGSLQPIIKTEG -> R (in isoform 2 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:10404027,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8363580"
FT /id="VSP_050666"
FT VAR_SEQ 759..812
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10404027"
FT /id="VSP_050667"
FT VAR_SEQ 785..812
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10404027,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_050668"
FT CONFLICT 346
FT /note="K -> R (in Ref. 2; BAC27122)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="D -> N (in Ref. 2; BAC27122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 838 AA; 93144 MW; 907FEB37942EADEC CRC64;
MVPLLPLYAL LLLFLCDINP ANANSYYDKV LAHSRIRGRD QGPNVCALQQ ILGTKKKYFS
SCKNWYQGAI CGKKTTVLYE CCPGYMRMEG MKGCPAVMPI DHVYGTLGIV GATTTQHYSD
VSKLREEIEG KGSYTYFAPS NEAWENLDSD IRRGLENNVN VELLNALHSH MVNKRMLTKD
LKHGMVIPSM YNNLGLFINH YPNGVVTVNC ARVIHGNQIA TNGVVHVIDR VLTQIGTSIQ
DFLEAEDDLS SFRAAAITSD LLESLGRDGH FTLFAPTNEA FEKLPRGVLE RIMGDKVASE
ALMKYHILNT LQCSEAITGG AVFETMEGNT IEIGCEGDSI SINGIKMVNK KDIVTKNGVI
HLIDEVLIPD SAKQVIELAG KQQTTFTDLV AQLGLASSLK PDGEYTLLAP VNNAFSDDTL
SMDQRLLKLI LQNHILKVKV GLSDLYNGQI LETIGGKQLR VFVYRTAICI ENSCMVRGSK
QGRNGAIHIF REIIQPAEKS LHDKLRQDKR FSIFLSLLEA ADLKDLLTQP GDWTLFAPTN
DAFKGMTSEE RELLIGDKNA LQNIILYHLT PGVYIGKGFE PGVTNILKTT QGSKIYLKGV
NETLLVNELK SKESDIMTTN GVIHVVDKLL YPADIPVGND QLLELLNKLI KYIQIKFVRG
STFKEIPMTV YTTKIITKVV EPKIKVIQGS LQPIIKTEGP AMTKIQIEGD PDFRLIKEGE
TVTEVIHGEP VIKKYTKIID GVPVEITEKQ TREERIITGP EIKYTRISTG GGETGETLQK
FLQKEVSKVT KFIEGGDGHL FEDEEIKRLL QGDTPAKKIP ANKRVQGPRR RSREGRSQ
