ID FST_HUMAN Reviewed; 344 AA. AC P19883; B5BU94; Q9BTH0; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 2. DT 02-OCT-2024, entry version 218. DE RecName: Full=Follistatin {ECO:0000303|PubMed:3380788}; DE Short=FS; DE AltName: Full=Activin-binding protein {ECO:0000250|UniProtKB:P21674}; DE Flags: Precursor; GN Name=FST {ECO:0000312|HGNC:HGNC:3971}; 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] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2). RX PubMed=3380788; DOI=10.1073/pnas.85.12.4218; RA Shimasaki S., Koga M., Esch F., Cooksey K., Mercado M., Koba A., Ueno N., RA Ying S.-Y., Ling N., Guillemin R.; RT "Primary structure of the human follistatin precursor and its genomic RT organization."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4218-4222(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pancreas; 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 [5] RP PROTEIN SEQUENCE OF 30-44. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [6] RP TISSUE SPECIFICITY. RX PubMed=15472207; DOI=10.1210/jc.2004-0162; RA Schneyer A.L., Wang Q., Sidis Y., Sluss P.M.; RT "Differential distribution of follistatin isoforms: application of a new RT FS315-specific immunoassay."; RL J. Clin. Endocrinol. Metab. 89:5067-5075(2004). RN [7] RP TISSUE SPECIFICITY, AND VARIANT TYR-56. RX PubMed=31215115; DOI=10.1002/humu.23793; RA Cox T.C., Lidral A.C., McCoy J.C., Liu H., Cox L.L., Zhu Y., Anderson R.D., RA Moreno Uribe L.M., Anand D., Deng M., Richter C.T., Nidey N.L., RA Standley J.M., Blue E.E., Chong J.X., Smith J.D., Kirk E.P., Venselaar H., RA Krahn K.N., van Bokhoven H., Zhou H., Cornell R.A., Glass I.A., RA Bamshad M.J., Nickerson D.A., Murray J.C., Lachke S.A., Thompson T.B., RA Buckley M.F., Roscioli T.; RT "Mutations in GDF11 and the extracellular antagonist, Follistatin, as a RT likely cause of Mendelian forms of orofacial clefting in humans."; RL Hum. Mutat. 40:1813-1825(2019). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-317 IN COMPLEX WITH ACTIVIN A, RP AND DISULFIDE BONDS. RX PubMed=16198295; DOI=10.1016/j.devcel.2005.09.008; RA Thompson T.B., Lerch T.F., Cook R.W., Woodruff T.K., Jardetzky T.S.; RT "The structure of the follistatin:activin complex reveals antagonism of RT both type I and type II receptor binding."; RL Dev. Cell 9:535-543(2005). RN [9] RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 30-344 IN COMPLEX WITH ACTIVIN A, RP AND DISULFIDE BONDS. RX PubMed=17409095; DOI=10.1074/jbc.m700737200; RA Lerch T.F., Shimasaki S., Woodruff T.K., Jardetzky T.S.; RT "Structural and biophysical coupling of heparin and activin binding to RT follistatin isoform functions."; RL J. Biol. Chem. 282:15930-15939(2007). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 30-317 IN COMPLEX WITH MOUSE RP MSTN, AND DISULFIDE BONDS. RX PubMed=19644449; DOI=10.1038/emboj.2009.205; RA Cash J.N., Rejon C.A., McPherron A.C., Bernard D.J., Thompson T.B.; RT "The structure of myostatin:follistatin 288: insights into receptor RT utilization and heparin binding."; RL EMBO J. 28:2662-2676(2009). RN [11] {ECO:0007744|PDB:5JHW} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 299-407 IN COMPLEX WITH GDF11, RP AND DISULFIDE BONDS. RX PubMed=28257634; DOI=10.1186/s12915-017-0350-1; RA Walker R.G., Czepnik M., Goebel E.J., McCoy J.C., Vujic A., Cho M., Oh J., RA Aykul S., Walton K.L., Schang G., Bernard D.J., Hinck A.P., Harrison C.A., RA Martinez-Hackert E., Wagers A.J., Lee R.T., Thompson T.B.; RT "Structural basis for potency differences between GDF8 and GDF11."; RL BMC Biol. 15:19-19(2017). CC -!- FUNCTION: Binds directly to activin and functions as an activin CC antagonist. Specific inhibitor of the biosynthesis and secretion of CC pituitary follicle stimulating hormone (FSH). CC -!- SUBUNIT: Monomer. Isoform 2/FS-288 interacts with GDF11 CC (PubMed:28257634). {ECO:0000269|PubMed:28257634, ECO:0000305}. CC -!- INTERACTION: CC P19883; P03950: ANG; NbExp=3; IntAct=EBI-1571188, EBI-525291; CC P19883; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-1571188, EBI-745073; CC P19883; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-1571188, EBI-744545; CC P19883; Q02930-3: CREB5; NbExp=5; IntAct=EBI-1571188, EBI-10192698; CC P19883; Q14689: DIP2A; NbExp=2; IntAct=EBI-1571188, EBI-2564275; CC P19883; P49639: HOXA1; NbExp=3; IntAct=EBI-1571188, EBI-740785; CC P19883; P10599: TXN; NbExp=3; IntAct=EBI-1571188, EBI-594644; CC P19883; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-1571188, EBI-740727; CC P19883; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-1571188, EBI-6427977; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=FS315, FS-315; CC IsoId=P19883-1; Sequence=Displayed; CC Name=2; Synonyms=FS288, FS-288; CC IsoId=P19883-2; Sequence=VSP_001565; CC -!- TISSUE SPECIFICITY: Isoform 1 is the predominant isoform in serum but CC is undetectable in follicular fluid. In the embryo, strong expression CC is seen in the palatal epithelia, including the medial edge epithelial CC and midline epithelial seam of the palatal shelves. Less pronounced CC expression is also seen throughout the palatal shelf and tongue CC mesenchyme (PubMed:31215115). {ECO:0000269|PubMed:15472207, CC ECO:0000269|PubMed:31215115}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44477/FST"; 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; M19481; AAA35851.1; -; Genomic_DNA. DR EMBL; M19480; AAA35851.1; JOINED; Genomic_DNA. DR EMBL; AB451330; BAG70144.1; -; mRNA. DR EMBL; AB451474; BAG70288.1; -; mRNA. DR EMBL; CH471123; EAW54880.1; -; Genomic_DNA. DR EMBL; BC004107; AAH04107.1; -; mRNA. DR CCDS; CCDS3959.1; -. [P19883-1] DR CCDS; CCDS43315.1; -. [P19883-2] DR PIR; A32141; A32141. DR RefSeq; NP_006341.1; NM_006350.3. [P19883-2] DR RefSeq; NP_037541.1; NM_013409.2. [P19883-1] DR PDB; 2B0U; X-ray; 2.80 A; C/D=30-317. DR PDB; 2P6A; X-ray; 3.40 A; C/D=30-344. DR PDB; 3HH2; X-ray; 2.15 A; C/D=30-317. DR PDB; 5JHW; X-ray; 2.35 A; C/D=30-317. DR PDBsum; 2B0U; -. DR PDBsum; 2P6A; -. DR PDBsum; 3HH2; -. DR PDBsum; 5JHW; -. DR AlphaFoldDB; P19883; -. DR SMR; P19883; -. DR BioGRID; 115731; 29. DR IntAct; P19883; 29. DR MINT; P19883; -. DR STRING; 9606.ENSP00000256759; -. DR DrugBank; DB01666; D-Myo-Inositol-Hexasulphate. DR MEROPS; I01.966; -. DR GlyConnect; 1251; 1 N-Linked glycan (1 site). DR GlyCosmos; P19883; 2 sites, 9 glycans. DR GlyGen; P19883; 3 sites, 9 N-linked glycans (2 sites). DR iPTMnet; P19883; -. DR PhosphoSitePlus; P19883; -. DR BioMuta; FST; -. DR DMDM; 23831079; -. DR MassIVE; P19883; -. DR PaxDb; 9606-ENSP00000256759; -. DR PeptideAtlas; P19883; -. DR ProteomicsDB; 53700; -. [P19883-1] DR ProteomicsDB; 53701; -. [P19883-2] DR Antibodypedia; 11023; 646 antibodies from 38 providers. DR DNASU; 10468; -. DR Ensembl; ENST00000256759.8; ENSP00000256759.3; ENSG00000134363.12. [P19883-1] DR Ensembl; ENST00000396947.7; ENSP00000380151.2; ENSG00000134363.12. [P19883-2] DR GeneID; 10468; -. DR KEGG; hsa:10468; -. DR MANE-Select; ENST00000256759.8; ENSP00000256759.3; NM_013409.3; NP_037541.1. DR UCSC; uc003jpc.4; human. [P19883-1] DR AGR; HGNC:3971; -. DR CTD; 10468; -. DR DisGeNET; 10468; -. DR GeneCards; FST; -. DR HGNC; HGNC:3971; FST. DR HPA; ENSG00000134363; Tissue enhanced (liver). DR MIM; 136470; gene. DR neXtProt; NX_P19883; -. DR OpenTargets; ENSG00000134363; -. DR PharmGKB; PA28388; -. DR VEuPathDB; HostDB:ENSG00000134363; -. DR eggNOG; KOG3649; Eukaryota. DR GeneTree; ENSGT00940000157072; -. DR HOGENOM; CLU_050745_0_0_1; -. DR InParanoid; P19883; -. DR OMA; ANCVTCN; -. DR OrthoDB; 2875444at2759; -. DR PhylomeDB; P19883; -. DR TreeFam; TF106409; -. DR PathwayCommons; P19883; -. DR Reactome; R-HSA-2473224; Antagonism of Activin by Follistatin. DR SignaLink; P19883; -. DR SIGNOR; P19883; -. DR BioGRID-ORCS; 10468; 14 hits in 1165 CRISPR screens. DR ChiTaRS; FST; human. DR EvolutionaryTrace; P19883; -. DR GeneWiki; Follistatin; -. DR GenomeRNAi; 10468; -. DR Pharos; P19883; Tbio. DR PRO; PR:P19883; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P19883; protein. DR Bgee; ENSG00000134363; Expressed in stromal cell of endometrium and 153 other cell types or tissues. DR ExpressionAtlas; P19883; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0048185; F:activin binding; IPI:UniProtKB. DR GO; GO:0038102; F:activin receptor antagonist activity; IMP:UniProtKB. DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IEA:Ensembl. DR GO; GO:0036305; P:ameloblast differentiation; IEA:Ensembl. DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0008585; P:female gonad development; IEA:Ensembl. DR GO; GO:0007276; P:gamete generation; IEA:Ensembl. DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IDA:UniProtKB. DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl. DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl. DR GO; GO:0007389; P:pattern specification process; IEA:Ensembl. DR GO; GO:0051798; P:positive regulation of hair follicle development; IDA:MGI. DR GO; GO:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl. DR CDD; cd00104; KAZAL_FS; 2. DR Gene3D; 3.30.60.30; -; 3. DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 1. DR IDEAL; IID00339; -. DR InterPro; IPR003645; Fol_N. DR InterPro; IPR015369; Follistatin/Osteonectin_EGF. DR InterPro; IPR002350; Kazal_dom. DR InterPro; IPR036058; Kazal_dom_sf. DR InterPro; IPR050653; Prot_Inhib_GrowthFact_Antg. DR InterPro; IPR017878; TB_dom. DR InterPro; IPR036773; TB_dom_sf. DR PANTHER; PTHR10913:SF45; AGRIN; 1. DR PANTHER; PTHR10913; FOLLISTATIN-RELATED; 1. DR Pfam; PF09289; FOLN; 1. DR Pfam; PF21333; FST_N; 1. DR Pfam; PF07648; Kazal_2; 3. DR SMART; SM00274; FOLN; 3. DR SMART; SM00280; KAZAL; 3. DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 3. DR SUPFAM; SSF57581; TB module/8-cys domain; 1. DR PROSITE; PS51465; KAZAL_2; 3. DR PROSITE; PS51364; TB; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Proteomics identification; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..29 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 30..344 FT /note="Follistatin" FT /id="PRO_0000010103" FT DOMAIN 30..103 FT /note="TB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697" FT DOMAIN 94..117 FT /note="Follistatin-like 1" FT DOMAIN 112..166 FT /note="Kazal-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DOMAIN 167..190 FT /note="Follistatin-like 2" FT DOMAIN 186..241 FT /note="Kazal-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DOMAIN 244..268 FT /note="Follistatin-like 3" FT DOMAIN 264..318 FT /note="Kazal-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT REGION 314..344 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 320..334 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 124 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 288 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 32..55 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697, FT ECO:0000269|PubMed:16198295, ECO:0000269|PubMed:17409095, FT ECO:0000269|PubMed:19644449, ECO:0000269|PubMed:28257634, FT ECO:0007744|PDB:2B0U, ECO:0007744|PDB:2P6A, FT ECO:0007744|PDB:3HH2, ECO:0007744|PDB:5JHW" FT DISULFID 42..88 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697, FT ECO:0000269|PubMed:16198295, ECO:0000269|PubMed:17409095, FT ECO:0000269|PubMed:19644449, ECO:0000269|PubMed:28257634, FT ECO:0007744|PDB:2B0U, ECO:0007744|PDB:2P6A, FT ECO:0007744|PDB:3HH2, ECO:0007744|PDB:5JHW" FT DISULFID 56..91 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697, FT ECO:0000269|PubMed:16198295, ECO:0000269|PubMed:17409095, FT ECO:0000269|PubMed:19644449, ECO:0000269|PubMed:28257634, FT ECO:0007744|PDB:2B0U, ECO:0007744|PDB:2P6A, FT ECO:0007744|PDB:3HH2, ECO:0007744|PDB:5JHW" FT DISULFID 95..106 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 100..116 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 118..150 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 122..143 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 132..164 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 168..179 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 173..189 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 192..225 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 196..218 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 207..239 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 245..256 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 250..267 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 270..302 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 274..295 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT DISULFID 284..316 FT /evidence="ECO:0000269|PubMed:16198295, FT ECO:0000269|PubMed:17409095, ECO:0000269|PubMed:19644449, FT ECO:0000269|PubMed:28257634, ECO:0007744|PDB:2B0U, FT ECO:0007744|PDB:2P6A, ECO:0007744|PDB:3HH2, FT ECO:0007744|PDB:5JHW" FT VAR_SEQ 318..344 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:19054851" FT /id="VSP_001565" FT VARIANT 56 FT /note="C -> Y (found in patients with orofacial clefting; FT uncertain significance; dbSNP:rs1747328996)" FT /evidence="ECO:0000269|PubMed:31215115" FT /id="VAR_085164" FT VARIANT 152 FT /note="E -> Q (in dbSNP:rs11745088)" FT /id="VAR_049091" FT STRAND 31..36 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 42..49 FT /evidence="ECO:0007829|PDB:3HH2" FT HELIX 52..55 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:3HH2" FT HELIX 72..81 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 82..87 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:3HH2" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:2P6A" FT STRAND 114..118 FT /evidence="ECO:0007829|PDB:3HH2" FT HELIX 123..125 FT /evidence="ECO:0007829|PDB:2B0U" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 138..141 FT /evidence="ECO:0007829|PDB:3HH2" FT HELIX 142..151 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 178..181 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 185..190 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:2B0U" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:3HH2" FT HELIX 217..227 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:3HH2" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:3HH2" FT TURN 251..253 FT /evidence="ECO:0007829|PDB:2P6A" FT STRAND 255..259 FT /evidence="ECO:0007829|PDB:3HH2" FT TURN 260..263 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 264..268 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 283..285 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 290..293 FT /evidence="ECO:0007829|PDB:3HH2" FT HELIX 294..304 FT /evidence="ECO:0007829|PDB:3HH2" FT STRAND 310..314 FT /evidence="ECO:0007829|PDB:3HH2" SQ SEQUENCE 344 AA; 38007 MW; D9BB45055D84AC90 CRC64; MVRARHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL SKEECCSTGR LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELEVQY QGRCKKTCRD VFCPGSSTCV VDQTNNAYCV TCNRICPEPA SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI KAKSCEDIQC TGGKKCLWDF KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA ACSSGVLLEV KHSGSCNSIS EDTEEEEEDE DQDYSFPISS ILEW //