FSTL3_BOVIN
ID FSTL3_BOVIN Reviewed; 261 AA.
AC Q1LZB9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Follistatin-related protein 3;
DE AltName: Full=Follistatin-like protein 3;
DE Flags: Precursor;
GN Name=FSTL3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; BC116095; AAI16096.1; -; mRNA.
DR RefSeq; NP_001069178.1; NM_001075710.2.
DR AlphaFoldDB; Q1LZB9; -.
DR SMR; Q1LZB9; -.
DR STRING; 9913.ENSBTAP00000028801; -.
DR PaxDb; Q1LZB9; -.
DR Ensembl; ENSBTAT00000028801; ENSBTAP00000028801; ENSBTAG00000003018.
DR GeneID; 515367; -.
DR KEGG; bta:515367; -.
DR CTD; 10272; -.
DR VEuPathDB; HostDB:ENSBTAG00000003018; -.
DR VGNC; VGNC:29136; FSTL3.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000161332; -.
DR HOGENOM; CLU_050745_1_0_1; -.
DR InParanoid; Q1LZB9; -.
DR OMA; YISSCHM; -.
DR OrthoDB; 1460520at2759; -.
DR TreeFam; TF106409; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000003018; Expressed in ureter and 101 other tissues.
DR ExpressionAtlas; Q1LZB9; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
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..26
FT /evidence="ECO:0000250"
FT CHAIN 27..261
FT /note="Follistatin-related protein 3"
FT /id="PRO_0000318093"
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..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 104..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 121..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 125..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 135..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 195..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 200..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 211..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 261 AA; 27658 MW; 86E13C94E7B6BF8E CRC64;
MRPRAPGPLW PLPWGALAWA VGFVGSLGSG DPAPGGVCWL QQGREATCSL VLKTDVSQAE
CCASGNIDTA WSNFTHPGNK ISLLGFLGLV HCLPCKDSCE GVECGPGKAC RMLGGRPRCE
CAPDCTGLPA RLQVCGSDGA TYRDECELRA ARCRGHPDLR VMYRGRCRKS CAHVVCLRPQ
SCVVDQTGSA HCVVCRAAPC PAPSSPGQEL CGNNNVTYLS SCHLRQATCF LGRSIGVRHP
GSCAGTPEPL DPESEEEENF V
