FSTL1_HUMAN
ID FSTL1_HUMAN Reviewed; 308 AA.
AC Q12841; A8K523; B4DTT5; D3DN90; Q549Z0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Follistatin-related protein 1;
DE AltName: Full=Follistatin-like protein 1;
DE Flags: Precursor;
GN Name=FSTL1; Synonyms=FRP;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=7957230; DOI=10.1111/j.1432-1033.1994.0937b.x;
RA Zwijsen A., Blockx H., van Arnhem W., Willems J., Fransen L., Devos K.,
RA Raymackers J., van de Voorde A., Slegers H.;
RT "Characterization of a rat C6 glioma-secreted follistatin-related protein
RT (FRP). Cloning and sequence of the human homologue.";
RL Eur. J. Biochem. 225:937-946(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Synovium;
RX PubMed=9786430; DOI=10.1093/intimm/10.9.1305;
RA Tanaka M., Ozaki S., Osakada F., Mori K., Okubo M., Nakao K.;
RT "Cloning of follistatin-related protein as a novel autoantigen in systemic
RT rheumatic diseases.";
RL Int. Immunol. 10:1305-1314(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=15638044;
RA Ehara Y., Sakurai D., Tsuchiya N., Nakano K., Tanaka Y., Yamaguchi A.,
RA Tokunaga K.;
RT "Follistatin-related protein gene (FRP) is expressed in the synovial
RT tissues of rheumatoid arthritis, but its polymorphisms are not associated
RT with genetic susceptibility.";
RL Clin. Exp. Rheumatol. 22:707-712(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [8]
RP PROTEIN SEQUENCE OF 21-35.
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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-175 AND ASN-180.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP INTERACTION WITH DIP2A.
RX PubMed=20860622; DOI=10.1111/j.1742-4658.2010.07816.x;
RA Tanaka M., Murakami K., Ozaki S., Imura Y., Tong X.P., Watanabe T.,
RA Sawaki T., Kawanami T., Kawabata D., Fujii T., Usui T., Masaki Y.,
RA Fukushima T., Jin Z.X., Umehara H., Mimori T.;
RT "DIP2 disco-interacting protein 2 homolog A (Drosophila) is a candidate
RT receptor for follistatin-related protein/follistatin-like 1--analysis of
RT their binding with TGF-beta superfamily proteins.";
RL FEBS J. 277:4278-4289(2010).
RN [11]
RP INTERACTION WITH DIP2A, AND FUNCTION.
RX PubMed=20054002; DOI=10.1074/jbc.m109.069468;
RA Ouchi N., Asaumi Y., Ohashi K., Higuchi A., Sono-Romanelli S., Oshima Y.,
RA Walsh K.;
RT "DIP2A functions as a FSTL1 receptor.";
RL J. Biol. Chem. 285:7127-7134(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION, AND INTERACTION WITH CD14.
RX PubMed=22265692; DOI=10.1016/j.febslet.2012.01.010;
RA Murakami K., Tanaka M., Usui T., Kawabata D., Shiomi A.,
RA Iguchi-Hashimoto M., Shimizu M., Yukawa N., Yoshifuji H., Nojima T.,
RA Ohmura K., Fujii T., Umehara H., Mimori T.;
RT "Follistatin-related protein/follistatin-like 1 evokes an innate immune
RT response via CD14 and toll-like receptor 4.";
RL FEBS Lett. 586:319-324(2012).
RN [14]
RP PHOSPHORYLATION AT SER-165.
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 [15]
RP FUNCTION, AND INTERACTION WITH BMP4.
RX PubMed=29212066; DOI=10.1159/000485759;
RA Jin X., Nie E., Zhou X., Zeng A., Yu T., Zhi T., Jiang K., Wang Y.,
RA Zhang J., You Y.;
RT "Fstl1 Promotes Glioma Growth Through the BMP4/Smad1/5/8 Signaling
RT Pathway.";
RL Cell. Physiol. Biochem. 44:1616-1628(2017).
CC -!- FUNCTION: Secreted glycoprotein that is involved in various
CC physiological processes, such as angiogenesis, regulation of the immune
CC response, cell proliferation and differentiation (PubMed:29212066,
CC PubMed:22265692). Plays a role in the development of the central
CC nervous system, skeletal system, lungs, and ureter (By similarity).
CC Promotes endothelial cell survival, migration and differentiation into
CC network structures in an AKT-dependent manner. Also promotes survival
CC of cardiac myocytes (By similarity). Initiates various signaling
CC cascades by activating different receptors on the cell surface such as
CC DIP2A, TLR4 or BMP receptors (PubMed:20054002, PubMed:22265692).
CC {ECO:0000250|UniProtKB:Q62356, ECO:0000269|PubMed:20054002,
CC ECO:0000269|PubMed:22265692, ECO:0000269|PubMed:29212066}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with SCN10A (By
CC similarity). Interacts with DIP2A; DIP2A may act as a cell surface
CC receptor for FSTL1 (PubMed:20860622, PubMed:20054002). Interacts with
CC BMP4 (PubMed:29212066). Interacts with CD14; this interaction promotes
CC TL4-mediated signaling cascade (PubMed:22265692).
CC {ECO:0000250|UniProtKB:Q62632, ECO:0000269|PubMed:20054002,
CC ECO:0000269|PubMed:20860622, ECO:0000269|PubMed:22265692,
CC ECO:0000269|PubMed:29212066}.
CC -!- INTERACTION:
CC Q12841; Q92624: APPBP2; NbExp=8; IntAct=EBI-2349801, EBI-743771;
CC Q12841; P12643: BMP2; NbExp=2; IntAct=EBI-2349801, EBI-1029262;
CC Q12841; P08571: CD14; NbExp=3; IntAct=EBI-2349801, EBI-3905196;
CC Q12841; Q14689: DIP2A; NbExp=4; IntAct=EBI-2349801, EBI-2564275;
CC Q12841; A4D1W7: INHBA; NbExp=2; IntAct=EBI-2349801, EBI-8307749;
CC Q12841; O43765: SGTA; NbExp=3; IntAct=EBI-2349801, EBI-347996;
CC Q12841; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2349801, EBI-5235340;
CC Q12841; P01137: TGFB1; NbExp=2; IntAct=EBI-2349801, EBI-779636;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q12841-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12841-2; Sequence=VSP_055075;
CC -!- TISSUE SPECIFICITY: Overexpressed in synovial tissues from rheumatoid
CC arthritis (PubMed:15638044). {ECO:0000269|PubMed:15638044}.
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DR EMBL; U06863; AAA66062.1; -; mRNA.
DR EMBL; D89937; BAA28707.1; -; mRNA.
DR EMBL; AB119283; BAD12167.1; -; Genomic_DNA.
DR EMBL; AK289388; BAF82077.1; -; mRNA.
DR EMBL; AK291138; BAF83827.1; -; mRNA.
DR EMBL; AK300356; BAG62097.1; -; mRNA.
DR EMBL; AK312261; BAG35192.1; -; mRNA.
DR EMBL; AC063952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC078982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79526.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79527.1; -; Genomic_DNA.
DR EMBL; BC000055; AAH00055.1; -; mRNA.
DR CCDS; CCDS2998.1; -. [Q12841-1]
DR PIR; S51362; S51362.
DR RefSeq; NP_009016.1; NM_007085.4. [Q12841-1]
DR AlphaFoldDB; Q12841; -.
DR SMR; Q12841; -.
DR BioGRID; 116338; 65.
DR IntAct; Q12841; 43.
DR MINT; Q12841; -.
DR STRING; 9606.ENSP00000295633; -.
DR MEROPS; I01.967; -.
DR GlyConnect; 1252; 9 N-Linked glycans (1 site).
DR GlyGen; Q12841; 4 sites, 8 N-linked glycans (1 site), 2 O-linked glycans (1 site).
DR iPTMnet; Q12841; -.
DR PhosphoSitePlus; Q12841; -.
DR BioMuta; FSTL1; -.
DR DMDM; 2498390; -.
DR EPD; Q12841; -.
DR jPOST; Q12841; -.
DR MassIVE; Q12841; -.
DR MaxQB; Q12841; -.
DR PaxDb; Q12841; -.
DR PeptideAtlas; Q12841; -.
DR PRIDE; Q12841; -.
DR ProteomicsDB; 5127; -.
DR ProteomicsDB; 58980; -. [Q12841-1]
DR Antibodypedia; 32794; 434 antibodies from 32 providers.
DR DNASU; 11167; -.
DR Ensembl; ENST00000295633.8; ENSP00000295633.3; ENSG00000163430.12. [Q12841-1]
DR Ensembl; ENST00000424703.6; ENSP00000394355.2; ENSG00000163430.12. [Q12841-2]
DR GeneID; 11167; -.
DR KEGG; hsa:11167; -.
DR MANE-Select; ENST00000295633.8; ENSP00000295633.3; NM_007085.5; NP_009016.1.
DR UCSC; uc003eds.4; human. [Q12841-1]
DR CTD; 11167; -.
DR DisGeNET; 11167; -.
DR GeneCards; FSTL1; -.
DR HGNC; HGNC:3972; FSTL1.
DR HPA; ENSG00000163430; Low tissue specificity.
DR MIM; 605547; gene.
DR neXtProt; NX_Q12841; -.
DR OpenTargets; ENSG00000163430; -.
DR PharmGKB; PA28389; -.
DR VEuPathDB; HostDB:ENSG00000163430; -.
DR eggNOG; ENOG502QQAG; Eukaryota.
DR GeneTree; ENSGT00940000157784; -.
DR HOGENOM; CLU_038229_0_0_1; -.
DR InParanoid; Q12841; -.
DR OMA; HRIIQWL; -.
DR OrthoDB; 1079836at2759; -.
DR PhylomeDB; Q12841; -.
DR TreeFam; TF106409; -.
DR PathwayCommons; Q12841; -.
DR Reactome; R-HSA-201451; Signaling by BMP.
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; Q12841; -.
DR SIGNOR; Q12841; -.
DR BioGRID-ORCS; 11167; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; FSTL1; human.
DR GeneWiki; FSTL1; -.
DR GenomeRNAi; 11167; -.
DR Pharos; Q12841; Tbio.
DR PRO; PR:Q12841; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q12841; protein.
DR Bgee; ENSG00000163430; Expressed in stromal cell of endometrium and 136 other tissues.
DR ExpressionAtlas; Q12841; baseline and differential.
DR Genevisible; Q12841; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; TAS:ProtInc.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045446; P:endothelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR015369; Follistatin/Osteonectin_EGF.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR Pfam; PF09289; FOLN; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR SMART; SM00274; FOLN; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Heparin-binding; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 21..308
FT /note="Follistatin-related protein 1"
FT /id="PRO_0000010111"
FT DOMAIN 30..53
FT /note="Follistatin-like"
FT DOMAIN 48..100
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 144..178
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 193..228
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 233..287
FT /note="VWFC"
FT MOD_RES 165
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT DISULFID 31..42
FT /evidence="ECO:0000250|UniProtKB:Q62356"
FT DISULFID 36..52
FT /evidence="ECO:0000250|UniProtKB:Q62356"
FT DISULFID 54..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 58..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 66..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 22..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055075"
FT CONFLICT 221
FT /note="C -> S (in Ref. 4; BAF83827)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="F -> S (in Ref. 4; BAF83827)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 34986 MW; BD4C651FAFF24800 CRC64;
MWKRWLALAL ALVAVAWVRA EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP
HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE
LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN
ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY
ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT
KRVSTKEI
