FSTL3_HUMAN
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 03-AUG-2022, entry version 179.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Magaud J.-P.,
RA Rimokh R.;
RT "FLRG (follistatin-related gene), a new target of chromosomal rearrangement
RT 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., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., 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 [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 project:
RT 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 verified
RT 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 follistatin
RT 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., Corbo L.,
RA Magaud J.P., Rimokh R.;
RT "Transcription activation of FLRG and follistatin by activin A, through
RT Smad proteins, participates in a negative feedback loop to modulate activin
RT 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 follistatin
RT 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 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 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 of
RT 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., Rimokh R.;
RT "AF10-dependent transcription is enhanced by its interaction with 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., Kurisaki A.,
RA Hashimoto O., Ohuchi H., Kurose H., Mori K., Kagami S., 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 phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 27-263 IN COMPLEX WITH INHBA,
RP 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 GDF8,
RP 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 antagonizing
CC protein for members of the TGF-beta family, such us activin, BMP2 and
CC MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular
CC signaling; more effective on activin A than on activin B. Involved in
CC bone formation; inhibits osteoclast differentiationc. Involved in
CC hematopoiesis; involved in differentiation of hemopoietic progenitor
CC cells, increases hematopoietic cell adhesion to fibronectin and seems
CC to contribute to the adhesion of hematopoietic precursor cells to the
CC bone 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. Interacts
CC with ADAM12. Isoform 2 interacts with MLLT10; the interaction enhances
CC MLLT10 in vitro transcriptional activity and self-association.
CC Interacts with MSTN. {ECO:0000269|PubMed:12697670,
CC ECO:0000269|PubMed:15574124, ECO:0000269|PubMed:16336961,
CC ECO:0000269|PubMed:17868029, ECO:0000269|PubMed:17878677,
CC ECO:0000269|PubMed:18768470, ECO:0000269|PubMed:22052913}.
CC -!- INTERACTION:
CC O95633; O43184-2: ADAM12; NbExp=4; IntAct=EBI-2625790, EBI-2625865;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Note=Although alternative
CC initiation has been demonstrated and resulted in different
CC localization, the major source of nuclear FSTL3 appears not to depend
CC 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 a
CC 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 and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FSTL3ID111ch19p13.html";
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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 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 AlphaFoldDB; O95633; -.
DR BMRB; O95633; -.
DR SMR; O95633; -.
DR BioGRID; 115562; 4.
DR IntAct; O95633; 2.
DR STRING; 9606.ENSP00000166139; -.
DR MEROPS; I01.968; -.
DR GlyGen; O95633; 3 sites.
DR iPTMnet; O95633; -.
DR PhosphoSitePlus; O95633; -.
DR BioMuta; FSTL3; -.
DR EPD; O95633; -.
DR jPOST; O95633; -.
DR MassIVE; O95633; -.
DR MaxQB; O95633; -.
DR PaxDb; O95633; -.
DR PeptideAtlas; O95633; -.
DR PRIDE; O95633; -.
DR ProteomicsDB; 50968; -. [O95633-1]
DR ProteomicsDB; 50969; -. [O95633-2]
DR TopDownProteomics; O95633-1; -. [O95633-1]
DR Antibodypedia; 22353; 244 antibodies from 26 providers.
DR DNASU; 10272; -.
DR Ensembl; ENST00000166139.9; ENSP00000166139.3; ENSG00000070404.10. [O95633-1]
DR GeneID; 10272; -.
DR KEGG; hsa:10272; -.
DR MANE-Select; ENST00000166139.9; ENSP00000166139.3; NM_005860.3; NP_005851.1.
DR UCSC; uc002lpk.2; human. [O95633-1]
DR CTD; 10272; -.
DR DisGeNET; 10272; -.
DR GeneCards; FSTL3; -.
DR HGNC; HGNC:3973; FSTL3.
DR HPA; ENSG00000070404; Low tissue specificity.
DR MIM; 605343; gene.
DR neXtProt; NX_O95633; -.
DR OpenTargets; ENSG00000070404; -.
DR PharmGKB; PA28390; -.
DR VEuPathDB; HostDB:ENSG00000070404; -.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000161332; -.
DR HOGENOM; CLU_050745_1_0_1; -.
DR InParanoid; O95633; -.
DR OMA; YISSCHM; -.
DR PhylomeDB; O95633; -.
DR TreeFam; TF106409; -.
DR PathwayCommons; O95633; -.
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 SignaLink; O95633; -.
DR SIGNOR; O95633; -.
DR BioGRID-ORCS; 10272; 15 hits in 1084 CRISPR screens.
DR ChiTaRS; FSTL3; human.
DR EvolutionaryTrace; O95633; -.
DR GeneWiki; FSTL3; -.
DR GenomeRNAi; 10272; -.
DR Pharos; O95633; Tbio.
DR PRO; PR:O95633; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O95633; protein.
DR Bgee; ENSG00000070404; Expressed in right coronary artery and 117 other tissues.
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:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048185; F:activin binding; IPI:UniProtKB.
DR GO; GO:0001968; F:fibronectin binding; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IDA:UniProtKB.
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:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR Gene3D; 3.90.290.10; -; 1.
DR IDEAL; IID00192; -.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Nucleus;
KW Osteogenesis; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat;
KW Secreted; Signal; Transcription; Transcription regulation.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 27..263
FT /note="Follistatin-related protein 3"
FT /id="PRO_0000010115"
FT DOMAIN 36..107
FT /note="TB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 99..119
FT /note="Follistatin-like 1"
FT DOMAIN 113..169
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 170..193
FT /note="Follistatin-like 2"
FT DOMAIN 189..245
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 242..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 255
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22052913"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18768470"
FT DISULFID 38..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 48..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 62..95
FT /evidence="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
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038553"
FT MUTAGEN 27
FT /note="M->A: Nuclear localization."
FT /evidence="ECO:0000269|PubMed:16150905"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:3SEK"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3SEK"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3B4V"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:3SEK"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3SEK"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:3SEK"
FT STRAND 237..241
FT /evidence="ECO:0007829|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
