FSTL3_RAT
ID FSTL3_RAT Reviewed; 256 AA.
AC Q99PW7; Q54A93;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Uchiyama Y., Ohsawa Y., Kametaka S.;
RT "Rat follistatin-related protein FLRG (rat PCTF35, PC12 cell derived
RT trophic factor 35).";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Placenta;
RX PubMed=12493714; DOI=10.1095/biolreprod.102.008565;
RA Arai K.Y., Tsuchida K., Uehara K., Taya K., Sugino H.;
RT "Characterization of rat follistatin-related gene: effects of estrous cycle
RT stage and pregnancy on its messenger RNA expression in rat reproductive
RT tissues.";
RL Biol. Reprod. 68:199-206(2003).
CC -!- FUNCTION: The secreted form is a binding and antagonizing protein for
CC members of the TGF-beta family, such us activin, BMP2 and MSTN.
CC 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 differentiation. 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. The nuclear form is probably involved in
CC transcriptional regulation via interaction with MLLT10 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with INHBA and INHBB. Interacts with FN1. Interacts
CC with ADAM12. Interacts with MLLT10; the interaction enhances MLLT10 in
CC vitro transcriptional activity and self-association. Interacts with
CC MSTN (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Nucleus {ECO:0000250}.
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DR EMBL; AB021295; BAB32664.1; -; mRNA.
DR EMBL; AB071603; BAC16229.1; -; mRNA.
DR RefSeq; NP_446081.1; NM_053629.3.
DR AlphaFoldDB; Q99PW7; -.
DR SMR; Q99PW7; -.
DR STRING; 10116.ENSRNOP00000012578; -.
DR MEROPS; I01.968; -.
DR GlyGen; Q99PW7; 2 sites.
DR PhosphoSitePlus; Q99PW7; -.
DR PaxDb; Q99PW7; -.
DR Ensembl; ENSRNOT00000012578; ENSRNOP00000012578; ENSRNOG00000009311.
DR GeneID; 114031; -.
DR KEGG; rno:114031; -.
DR UCSC; RGD:621811; rat.
DR CTD; 10272; -.
DR RGD; 621811; Fstl3.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000161332; -.
DR HOGENOM; CLU_050745_1_0_1; -.
DR InParanoid; Q99PW7; -.
DR OMA; YISSCHM; -.
DR OrthoDB; 1460520at2759; -.
DR PhylomeDB; Q99PW7; -.
DR TreeFam; TF106409; -.
DR Reactome; R-RNO-2473224; Antagonism of Activin by Follistatin.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q99PW7; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000009311; Expressed in testis and 19 other tissues.
DR Genevisible; Q99PW7; RN.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0044306; C:neuron projection terminus; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0048185; F:activin binding; ISO:RGD.
DR GO; GO:0001968; F:fibronectin binding; ISO:RGD.
DR GO; GO:0030325; P:adrenal gland development; IEP:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071248; P:cellular response to metal ion; IEP:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0030324; P:lung development; IEP:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISO:RGD.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:RGD.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0090101; P:negative regulation of transmembrane receptor protein serine/threonine kinase signaling pathway; ISO:RGD.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR Gene3D; 3.90.290.10; -; 1.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Nucleus; Osteogenesis; Reference proteome;
KW Repeat; Secreted; Signal; Transcription; Transcription regulation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..256
FT /note="Follistatin-related protein 3"
FT /id="PRO_0000010117"
FT DOMAIN 34..105
FT /note="TB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 97..117
FT /note="Follistatin-like 1"
FT DOMAIN 111..167
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 168..191
FT /note="Follistatin-like 2"
FT DOMAIN 187..243
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 46..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 60..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 97..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 102..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 119..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 123..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 133..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 193..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 198..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 209..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 256 AA; 27109 MW; C8464166C0A1D56F CRC64;
MRPGALWPLL WGALVWAVGS VGAVMGSGDS VPGGVCWLQQ GKEATCSLVL KTQVSREECC
ASGNINTAWS NFTHPGNKIS LLGFLGLVHC LPCKDSCDGV ECGPGKACRM LGGRPHCECV
SNCEGVPAGF QVCGSDGATY RDECELRTAR CRGHPDLRVM YRGRCQKSCA QVVCPRPQSC
LVDQTGSAHC VVCRAAPCPV PPNPGQELCG NNNVTYISSC HLRQATCFLG RSIGVRHPGI
CTGGPKVPAE EEENFV
