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Follistatin-related protein 1 (Follistatin-like protein 1)

 FSTL1_HUMAN             Reviewed;         308 AA.
Q12841; A8K523; B4DTT5; D3DN90; Q549Z0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 164.
RecName: Full=Follistatin-related protein 1;
AltName: Full=Follistatin-like protein 1;
Flags: Precursor;
Name=FSTL1; Synonyms=FRP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=7957230; DOI=10.1111/j.1432-1033.1994.0937b.x;
Zwijsen A., Blockx H., van Arnhem W., Willems J., Fransen L.,
Devos K., Raymackers J., van de Voorde A., Slegers H.;
"Characterization of a rat C6 glioma-secreted follistatin-related
protein (FRP). Cloning and sequence of the human homologue.";
Eur. J. Biochem. 225:937-946(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Synovium;
PubMed=9786430; DOI=10.1093/intimm/10.9.1305;
Tanaka M., Ozaki S., Osakada F., Mori K., Okubo M., Nakao K.;
"Cloning of follistatin-related protein as a novel autoantigen in
systemic rheumatic diseases.";
Int. Immunol. 10:1305-1314(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=15638044;
Ehara Y., Sakurai D., Tsuchiya N., Nakano K., Tanaka Y., Yamaguchi A.,
Tokunaga K.;
"Follistatin-related protein gene (FRP) is expressed in the synovial
tissues of rheumatoid arthritis, but its polymorphisms are not
associated with genetic susceptibility.";
Clin. Exp. Rheumatol. 22:707-712(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 21-35.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-175 AND ASN-180.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION AT SER-165.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
-!- FUNCTION: May modulate the action of some growth factors on cell
proliferation and differentiation. Binds heparin (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts with SCN10A.
-!- INTERACTION:
Q92624:APPBP2; NbExp=7; IntAct=EBI-2349801, EBI-743771;
P12643:BMP2; NbExp=2; IntAct=EBI-2349801, EBI-1029262;
P08571:CD14; NbExp=3; IntAct=EBI-2349801, EBI-3905196;
Q14689:DIP2A; NbExp=4; IntAct=EBI-2349801, EBI-2564275;
A4D1W7:INHBA; NbExp=2; IntAct=EBI-2349801, EBI-8307749;
P01137:TGFB1; NbExp=2; IntAct=EBI-2349801, EBI-779636;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q12841-1; Sequence=Displayed;
Name=2;
IsoId=Q12841-2; Sequence=VSP_055075;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Overexpressed in synovial tissues from
rheumatoid arthritis. {ECO:0000269|PubMed:15638044}.
-----------------------------------------------------------------------
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EMBL; U06863; AAA66062.1; -; mRNA.
EMBL; D89937; BAA28707.1; -; mRNA.
EMBL; AB119283; BAD12167.1; -; Genomic_DNA.
EMBL; AK289388; BAF82077.1; -; mRNA.
EMBL; AK291138; BAF83827.1; -; mRNA.
EMBL; AK300356; BAG62097.1; -; mRNA.
EMBL; AK312261; BAG35192.1; -; mRNA.
EMBL; AC063952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC078982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79526.1; -; Genomic_DNA.
EMBL; CH471052; EAW79527.1; -; Genomic_DNA.
EMBL; BC000055; AAH00055.1; -; mRNA.
CCDS; CCDS2998.1; -. [Q12841-1]
PIR; S51362; S51362.
RefSeq; NP_009016.1; NM_007085.4. [Q12841-1]
UniGene; Hs.269512; -.
ProteinModelPortal; Q12841; -.
SMR; Q12841; -.
BioGrid; 116338; 38.
IntAct; Q12841; 18.
MINT; MINT-7990618; -.
STRING; 9606.ENSP00000295633; -.
MEROPS; I01.967; -.
iPTMnet; Q12841; -.
PhosphoSitePlus; Q12841; -.
BioMuta; FSTL1; -.
DMDM; 2498390; -.
EPD; Q12841; -.
MaxQB; Q12841; -.
PaxDb; Q12841; -.
PeptideAtlas; Q12841; -.
PRIDE; Q12841; -.
Ensembl; ENST00000295633; ENSP00000295633; ENSG00000163430. [Q12841-1]
Ensembl; ENST00000424703; ENSP00000394355; ENSG00000163430. [Q12841-2]
GeneID; 11167; -.
KEGG; hsa:11167; -.
UCSC; uc003eds.4; human. [Q12841-1]
CTD; 11167; -.
DisGeNET; 11167; -.
EuPathDB; HostDB:ENSG00000163430.9; -.
GeneCards; FSTL1; -.
HGNC; HGNC:3972; FSTL1.
HPA; HPA035251; -.
MIM; 605547; gene.
neXtProt; NX_Q12841; -.
OpenTargets; ENSG00000163430; -.
PharmGKB; PA28389; -.
eggNOG; ENOG410IIPU; Eukaryota.
eggNOG; ENOG410ZJ7W; LUCA.
GeneTree; ENSGT00530000063333; -.
HOGENOM; HOG000007780; -.
HOVERGEN; HBG051665; -.
InParanoid; Q12841; -.
OMA; TTYADQE; -.
OrthoDB; EOG091G0YXX; -.
PhylomeDB; Q12841; -.
TreeFam; TF106409; -.
Reactome; R-HSA-201451; Signaling by BMP.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
ChiTaRS; FSTL1; human.
GeneWiki; FSTL1; -.
GenomeRNAi; 11167; -.
PMAP-CutDB; Q12841; -.
PRO; PR:Q12841; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000163430; -.
CleanEx; HS_FSTL1; -.
ExpressionAtlas; Q12841; baseline and differential.
Genevisible; Q12841; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008201; F:heparin binding; TAS:ProtInc.
GO; GO:0030509; P:BMP signaling pathway; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0042594; P:response to starvation; IEA:Ensembl.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR003645; Fol_N.
InterPro; IPR015369; Follistatin/Osteonectin_EGF.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR036058; Kazal_dom_sf.
Pfam; PF09289; FOLN; 1.
Pfam; PF07648; Kazal_2; 1.
SMART; SM00274; FOLN; 1.
SMART; SM00280; KAZAL; 1.
SUPFAM; SSF100895; SSF100895; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS50222; EF_HAND_2; 2.
PROSITE; PS51465; KAZAL_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Heparin-binding; Phosphoprotein;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 20 {ECO:0000269|PubMed:15340161}.
CHAIN 21 308 Follistatin-related protein 1.
/FTId=PRO_0000010111.
DOMAIN 30 53 Follistatin-like.
DOMAIN 48 100 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 144 178 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 193 228 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 233 287 VWFC.
MOD_RES 165 165 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 180 180 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 54 84 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 58 77 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 66 98 {ECO:0000255|PROSITE-ProRule:PRU00798}.
VAR_SEQ 22 56 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055075.
CONFLICT 221 221 C -> S (in Ref. 4; BAF83827).
{ECO:0000305}.
CONFLICT 226 226 F -> S (in Ref. 4; BAF83827).
{ECO:0000305}.
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


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