ID FSTL3_HUMAN Reviewed; 263 AA. AC O95633; A8K7E3; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-FEB-2019, entry version 161. DE RecName: Full=Follistatin-related protein 3; DE AltName: Full=Follistatin-like protein 3; DE AltName: Full=Follistatin-related gene protein; DE Flags: Precursor; GN Name=FSTL3; Synonyms=FLRG; ORFNames=UNQ674/PRO1308; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHROMOSOMAL TRANSLOCATION. RC TISSUE=Placenta; RX PubMed=9671416; DOI=10.1038/sj.onc.1201807; RA Hayette S., Gadoux M., Martel S., Bertrand S., Tigaud I., RA Magaud J.-P., Rimokh R.; RT "FLRG (follistatin-related gene), a new target of chromosomal RT rearrangement in malignant blood disorders."; RL Oncogene 16:2949-2954(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 27-41. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [7] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=11459787; DOI=10.1210/endo.142.8.8319; RA Tortoriello D.V., Sidis Y., Holtzman D.A., Holmes W.E., Schneyer A.L.; RT "Human follistatin-related protein: a structural homologue of RT follistatin with nuclear localization."; RL Endocrinology 142:3426-3434(2001). RN [8] RP FUNCTION. RX PubMed=11948405; DOI=10.1038/sj.onc.1205294; RA Bartholin L., Maguer-Satta V., Hayette S., Martel S., Gadoux M., RA Corbo L., Magaud J.P., Rimokh R.; RT "Transcription activation of FLRG and follistatin by activin A, RT through Smad proteins, participates in a negative feedback loop to RT modulate activin A function."; RL Oncogene 21:2227-2235(2002). RN [9] RP INTERACTION WITH INHBA AND INHBB. RX PubMed=12697670; DOI=10.1210/en.2002-0203; RA Schneyer A., Schoen A., Quigg A., Sidis Y.; RT "Differential binding and neutralization of activins A and B by RT follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG)."; RL Endocrinology 144:1671-1674(2003). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=12970321; DOI=10.1210/jc.2002-021758; RA Wang H.Q., Takebayashi K., Tsuchida K., Nishimura M., Noda Y.; RT "Follistatin-related gene (FLRG) expression in human endometrium: sex RT steroid hormones regulate the expression of FLRG in cultured human RT endometrial stromal cells."; RL J. Clin. Endocrinol. Metab. 88:4432-4439(2003). RN [11] RP FUNCTION IN HEMATOPOIESIS. RX PubMed=15451575; DOI=10.1016/j.mce.2004.07.009; RA Maguer-Satta V., Rimokh R.; RT "FLRG, member of the follistatin family, a new player in RT hematopoiesis."; RL Mol. Cell. Endocrinol. 225:109-118(2004). RN [12] RP FUNCTION IN OSTEOCLAST DIFFERENTIATION, AND INTERACTION WITH ADAM8 AND RP ADAM12. RX PubMed=15574124; DOI=10.1042/BC20040506; RA Bartholin L., Destaing O., Forissier S., Martel S., Maguer-Satta V., RA Jurdic P., Rimokh R.; RT "FLRG, a new ADAM12-associated protein, modulates osteoclast RT differentiation."; RL Biol. Cell 97:577-588(2005). RN [13] RP SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, AND MUTAGENESIS OF RP MET-27. RX PubMed=16150905; DOI=10.1210/en.2005-0833; RA Saito S., Sidis Y., Mukherjee A., Xia Y., Schneyer A.; RT "Differential biosynthesis and intracellular transport of follistatin RT isoforms and follistatin-like-3."; RL Endocrinology 146:5052-5062(2005). RN [14] RP FUNCTION IN HEMATOPOIESIS, AND INTERACTION WITH FN1. RX PubMed=16336961; DOI=10.1016/j.yexcr.2005.11.006; RA Maguer-Satta V., Forissier S., Bartholin L., Martel S., Jeanpierre S., RA Bachelard E., Rimokh R.; RT "A novel role for fibronectin type I domain in the regulation of human RT hematopoietic cell adhesiveness through binding to follistatin domains RT of FLRG and follistatin."; RL Exp. Cell Res. 312:434-442(2006). RN [15] RP FUNCTION IN TRANSCRIPTION REGULATION, AND INTERACTION WITH MLLT10. RX PubMed=17868029; DOI=10.1042/BC20060131; RA Forissier S., Razanajaona D., Ay A.S., Martel S., Bartholin L., RA Rimokh R.; RT "AF10-dependent transcription is enhanced by its interaction with RT FLRG."; RL Biol. Cell 99:563-571(2007). RN [16] RP FUNCTION, AND INTERACTION WITH MSTN. RX PubMed=17878677; DOI=10.2152/jmi.54.276; RA Takehara-Kasamatsu Y., Tsuchida K., Nakatani M., Murakami T., RA Kurisaki A., Hashimoto O., Ohuchi H., Kurose H., Mori K., Kagami S., RA Noji S., Sugino H.; RT "Characterization of follistatin-related gene as a negative regulatory RT factor for activin family members during mouse heart development."; RL J. Med. Invest. 54:276-288(2007). RN [17] RP PHOSPHORYLATION AT SER-255. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted RT phosphoproteome."; RL Cell 161:1619-1632(2015). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 27-263 IN COMPLEX WITH RP INHBA, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-215. RX PubMed=18768470; DOI=10.1074/jbc.M801266200; RA Stamler R., Keutmann H.T., Sidis Y., Kattamuri C., Schneyer A., RA Thompson T.B.; RT "The structure of FSTL3.activin A complex. Differential binding of N- RT terminal domains influences follistatin-type antagonist specificity."; RL J. Biol. Chem. 283:32831-32838(2008). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 36-244 IN COMPLEX WITH MOUSE RP GDF8, GLYCOSYLATION AT ASN-73, AND DISULFIDE BONDS. RX PubMed=22052913; DOI=10.1074/jbc.M111.270801; RA Cash J.N., Angerman E.B., Kattamuri C., Nolan K., Zhao H., Sidis Y., RA Keutmann H.T., Thompson T.B.; RT "Structure of myostatin.follistatin-like 3: N-terminal domains of RT follistatin-type molecules exhibit alternate modes of binding."; RL J. Biol. Chem. 287:1043-1053(2012). CC -!- FUNCTION: Isoform 1 or the secreted form is a binding and CC antagonizing protein for members of the TGF-beta family, such us CC activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and CC MSDT-induced cellular signaling; more effective on activin A than CC on activin B. Involved in bone formation; inhibits osteoclast CC differentiationc. Involved in hematopoiesis; involved in CC differentiation of hemopoietic progenitor cells, increases CC hematopoietic cell adhesion to fibronectin and seems to contribute CC to the adhesion of hematopoietic precursor cells to the bone CC marrow stroma. Isoform 2 or the nuclear form is probably involved CC in transcriptional regulation via interaction with MLLT10. CC {ECO:0000269|PubMed:11948405, ECO:0000269|PubMed:15451575, CC ECO:0000269|PubMed:15574124, ECO:0000269|PubMed:16336961, CC ECO:0000269|PubMed:17868029, ECO:0000269|PubMed:17878677}. CC -!- SUBUNIT: Interacts with INHBA and INHBB. Interacts with FN1. CC Interacts with ADAM12. Isoform 2 interacts with MLLT10; the CC interaction enhances MLLT10 in vitro transcriptional activity and CC self-association. Interacts with MSTN. CC {ECO:0000269|PubMed:12697670, ECO:0000269|PubMed:15574124, CC ECO:0000269|PubMed:16336961, ECO:0000269|PubMed:17868029, CC ECO:0000269|PubMed:17878677, ECO:0000269|PubMed:18768470, CC ECO:0000269|PubMed:22052913}. CC -!- INTERACTION: CC O43184-2:ADAM12; NbExp=4; IntAct=EBI-2625790, EBI-2625865; CC -!- SUBCELLULAR LOCATION: Isoform 1: Secreted. CC -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus. Note=Although CC alternative initiation has been demonstrated and resulted in CC different localization, the major source of nuclear FSTL3 appears CC not to depend on translation initiation at Met-27 according to. CC {ECO:0000269|PubMed:16150905}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; CC IsoId=O95633-1; Sequence=Displayed; CC Name=2; CC IsoId=O95633-2; Sequence=VSP_038553; CC -!- TISSUE SPECIFICITY: Expressed in a wide range of tissues. CC {ECO:0000269|PubMed:11459787}. CC -!- DISEASE: Note=A chromosomal aberration involving FSTL3 is found in CC a case of B-cell chronic lymphocytic leukemia. Translocation CC t(11;19)(q13;p13) with CCDN1. {ECO:0000269|PubMed:9671416}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/FSTL3ID111ch19p13.html"; 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; U76702; AAC64321.1; -; mRNA. DR EMBL; AY358917; AAQ89276.1; -; mRNA. DR EMBL; AK291958; BAF84647.1; -; mRNA. DR EMBL; CH471242; EAW61165.1; -; Genomic_DNA. DR EMBL; BC005839; AAH05839.1; -; mRNA. DR CCDS; CCDS12040.1; -. [O95633-1] DR RefSeq; NP_005851.1; NM_005860.2. [O95633-1] DR UniGene; Hs.529038; -. DR PDB; 2KCX; NMR; -; A=97-169. DR PDB; 3B4V; X-ray; 2.48 A; C/D/G/H=27-263. DR PDB; 3SEK; X-ray; 2.40 A; C=36-244. DR PDBsum; 2KCX; -. DR PDBsum; 3B4V; -. DR PDBsum; 3SEK; -. DR ProteinModelPortal; O95633; -. DR SMR; O95633; -. DR BioGrid; 115562; 2. DR IntAct; O95633; 2. DR STRING; 9606.ENSP00000166139; -. DR MEROPS; I01.968; -. DR iPTMnet; O95633; -. DR PhosphoSitePlus; O95633; -. DR BioMuta; FSTL3; -. DR jPOST; O95633; -. DR MaxQB; O95633; -. DR PaxDb; O95633; -. DR PeptideAtlas; O95633; -. DR PRIDE; O95633; -. DR ProteomicsDB; 50968; -. DR ProteomicsDB; 50969; -. [O95633-2] DR TopDownProteomics; O95633-1; -. [O95633-1] DR Ensembl; ENST00000166139; ENSP00000166139; ENSG00000070404. [O95633-1] DR GeneID; 10272; -. DR KEGG; hsa:10272; -. DR UCSC; uc002lpk.2; human. [O95633-1] DR CTD; 10272; -. DR DisGeNET; 10272; -. DR EuPathDB; HostDB:ENSG00000070404.9; -. DR GeneCards; FSTL3; -. DR HGNC; HGNC:3973; FSTL3. DR HPA; CAB024899; -. DR HPA; HPA045378; -. DR MIM; 605343; gene. DR neXtProt; NX_O95633; -. DR OpenTargets; ENSG00000070404; -. DR PharmGKB; PA28390; -. DR eggNOG; KOG3649; Eukaryota. DR eggNOG; ENOG410YC3T; LUCA. DR GeneTree; ENSGT00940000161332; -. DR HOGENOM; HOG000261649; -. DR HOVERGEN; HBG051666; -. DR InParanoid; O95633; -. DR OMA; GAPGPLW; -. DR OrthoDB; 1460520at2759; -. DR PhylomeDB; O95633; -. DR TreeFam; TF106409; -. DR Reactome; R-HSA-2473224; Antagonism of Activin by Follistatin. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR SIGNOR; O95633; -. DR ChiTaRS; FSTL3; human. DR EvolutionaryTrace; O95633; -. DR GeneWiki; FSTL3; -. DR GenomeRNAi; 10272; -. DR PMAP-CutDB; O95633; -. DR PRO; PR:O95633; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000070404; Expressed in 138 organ(s), highest expression level in left adrenal gland. DR ExpressionAtlas; O95633; baseline and differential. DR Genevisible; O95633; HS. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0044306; C:neuron projection terminus; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0030141; C:secretory granule; IEA:Ensembl. DR GO; GO:0048185; F:activin binding; IPI:UniProtKB. DR GO; GO:0001968; F:fibronectin binding; IPI:UniProtKB. DR GO; GO:0030325; P:adrenal gland development; IEA:Ensembl. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0071248; P:cellular response to metal ion; IEA:Ensembl. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IDA:UniProtKB. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0008584; P:male gonad development; IEA:Ensembl. DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:UniProtKB. DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:UniProtKB. DR GO; GO:0090101; P:negative regulation of transmembrane receptor protein serine/threonine kinase signaling pathway; IDA:UniProtKB. DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW. DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR Gene3D; 3.90.290.10; -; 1. DR InterPro; IPR003645; Fol_N. DR InterPro; IPR015369; Follistatin/Osteonectin_EGF. DR InterPro; IPR002350; Kazal_dom. DR InterPro; IPR036058; Kazal_dom_sf. DR InterPro; IPR017878; TB_dom. DR InterPro; IPR036773; TB_dom_sf. DR Pfam; PF09289; FOLN; 1. DR Pfam; PF07648; Kazal_2; 2. DR SMART; SM00274; FOLN; 2. DR SMART; SM00280; KAZAL; 2. DR SUPFAM; SSF100895; SSF100895; 2. DR SUPFAM; SSF57581; SSF57581; 1. DR PROSITE; PS51465; KAZAL_2; 2. DR PROSITE; PS51364; TB; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Chromosomal rearrangement; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Nucleus; Osteogenesis; Phosphoprotein; Proto-oncogene; KW Reference proteome; Repeat; Secreted; Signal; Transcription; KW Transcription regulation. FT SIGNAL 1 26 {ECO:0000269|PubMed:15340161}. FT CHAIN 27 263 Follistatin-related protein 3. FT /FTId=PRO_0000010115. FT DOMAIN 36 107 TB. {ECO:0000255|PROSITE- FT ProRule:PRU00697}. FT DOMAIN 99 119 Follistatin-like 1. FT DOMAIN 113 169 Kazal-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00798}. FT DOMAIN 170 193 Follistatin-like 2. FT DOMAIN 189 245 Kazal-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00798}. FT MOD_RES 255 255 Phosphoserine; by FAM20C. FT {ECO:0000269|PubMed:26091039}. FT CARBOHYD 73 73 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22052913}. FT CARBOHYD 215 215 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:18768470}. FT DISULFID 38 61 {ECO:0000255|PROSITE-ProRule:PRU00697}. FT DISULFID 48 92 {ECO:0000255|PROSITE-ProRule:PRU00697}. FT DISULFID 62 95 {ECO:0000255|PROSITE-ProRule:PRU00697}. FT DISULFID 99 110 FT DISULFID 104 119 FT DISULFID 121 153 FT DISULFID 125 146 FT DISULFID 135 167 FT DISULFID 171 182 FT DISULFID 176 192 FT DISULFID 195 229 FT DISULFID 200 222 FT DISULFID 211 243 FT VAR_SEQ 1 26 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_038553. FT MUTAGEN 27 27 M->A: Nuclear localization. FT {ECO:0000269|PubMed:16150905}. FT STRAND 37 40 {ECO:0000244|PDB:3SEK}. FT STRAND 50 55 {ECO:0000244|PDB:3SEK}. FT HELIX 58 62 {ECO:0000244|PDB:3SEK}. FT STRAND 67 72 {ECO:0000244|PDB:3SEK}. FT HELIX 81 86 {ECO:0000244|PDB:3SEK}. FT STRAND 93 95 {ECO:0000244|PDB:3SEK}. FT STRAND 97 99 {ECO:0000244|PDB:3SEK}. FT STRAND 108 111 {ECO:0000244|PDB:3SEK}. FT STRAND 113 116 {ECO:0000244|PDB:3B4V}. FT STRAND 118 121 {ECO:0000244|PDB:3SEK}. FT STRAND 126 128 {ECO:0000244|PDB:3SEK}. FT STRAND 134 136 {ECO:0000244|PDB:3SEK}. FT STRAND 141 144 {ECO:0000244|PDB:3SEK}. FT HELIX 145 153 {ECO:0000244|PDB:3SEK}. FT STRAND 161 166 {ECO:0000244|PDB:3SEK}. FT STRAND 169 171 {ECO:0000244|PDB:3SEK}. FT STRAND 181 184 {ECO:0000244|PDB:3SEK}. FT STRAND 190 193 {ECO:0000244|PDB:3SEK}. FT STRAND 204 207 {ECO:0000244|PDB:3SEK}. FT STRAND 210 212 {ECO:0000244|PDB:3SEK}. FT STRAND 217 220 {ECO:0000244|PDB:3SEK}. FT HELIX 221 231 {ECO:0000244|PDB:3SEK}. FT STRAND 237 241 {ECO:0000244|PDB:3SEK}. SQ SEQUENCE 263 AA; 27663 MW; 6A9AB86ADD4FD09C CRC64; MRPGAPGPLW PLPWGALAWA VGFVSSMGSG NPAPGGVCWL QQGQEATCSL VLQTDVTRAE CCASGNIDTA WSNLTHPGNK INLLGFLGLV HCLPCKDSCD GVECGPGKAC RMLGGRPRCE CAPDCSGLPA RLQVCGSDGA TYRDECELRA ARCRGHPDLS VMYRGRCRKS CEHVVCPRPQ SCVVDQTGSA HCVVCRAAPC PVPSSPGQEL CGNNNVTYIS SCHMRQATCF LGRSIGVRHA GSCAGTPEEP PGGESAEEEE NFV //