FST_HUMAN
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 03-AUG-2022, entry version 206.
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="http://atlasgeneticsoncology.org/Genes/FSTID44477ch5q11.html";
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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; 28.
DR IntAct; P19883; 18.
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 GlyGen; P19883; 3 sites, 9 N-linked glycans (2 sites).
DR iPTMnet; P19883; -.
DR PhosphoSitePlus; P19883; -.
DR BioMuta; FST; -.
DR DMDM; 23831079; -.
DR EPD; P19883; -.
DR MassIVE; P19883; -.
DR MaxQB; P19883; -.
DR PaxDb; P19883; -.
DR PeptideAtlas; P19883; -.
DR PRIDE; P19883; -.
DR ProteomicsDB; 53700; -. [P19883-1]
DR ProteomicsDB; 53701; -. [P19883-2]
DR Antibodypedia; 11023; 596 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 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; RWTIFNG; -.
DR OrthoDB; 1460520at2759; -.
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 1087 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 151 other tissues.
DR ExpressionAtlas; P19883; baseline and differential.
DR Genevisible; P19883; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0001501; P:skeletal system development; IEA:Ensembl.
DR Gene3D; 3.90.290.10; -; 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; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR Pfam; PF09289; FOLN; 1.
DR Pfam; PF07648; Kazal_2; 3.
DR SMART; SM00274; FOLN; 3.
DR SMART; SM00280; KAZAL; 3.
DR SUPFAM; SSF100895; SSF100895; 3.
DR SUPFAM; SSF57581; SSF57581; 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; 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 unknown pathological significance)"
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
