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   27-MAR-2024, entry version 168.
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   GlyCosmos; Q62009; 1 site, No reported glycans.
DR   GlyGen; Q62009; 1 site.
DR   iPTMnet; Q62009; -.
DR   PhosphoSitePlus; Q62009; -.
DR   CPTAC; non-CPTAC-3739; -.
DR   MaxQB; Q62009; -.
DR   PaxDb; 10090-ENSMUSP00000072773; -.
DR   PeptideAtlas; 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   Pumba; Q62009; -.
DR   Antibodypedia; 2020; 775 antibodies from 47 providers.
DR   DNASU; 50706; -.
DR   Ensembl; ENSMUST00000073012.13; ENSMUSP00000072773.7; ENSMUSG00000027750.17. [Q62009-2]
DR   Ensembl; ENSMUST00000081564.13; ENSMUSP00000080276.7; ENSMUSG00000027750.17. [Q62009-1]
DR   Ensembl; ENSMUST00000107985.10; ENSMUSP00000103619.4; ENSMUSG00000027750.17. [Q62009-3]
DR   Ensembl; ENSMUST00000117373.8; ENSMUSP00000112735.2; ENSMUSG00000027750.17. [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   AGR; MGI:1926321; -.
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; LHQVDRP; -.
DR   OrthoDB; 523796at2759; -.
DR   PhylomeDB; Q62009; -.
DR   TreeFam; TF316269; -.
DR   BioGRID-ORCS; 50706; 1 hit in 78 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 262 other cell types or tissues.
DR   ExpressionAtlas; Q62009; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
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: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; 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: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; IMP:MGI.
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; Q62009; MM.
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
//