ID   FSTL1_BOVIN             Reviewed;         307 AA.
AC   Q58D84;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   24-JAN-2024, entry version 128.
DE   RecName: Full=Follistatin-related protein 1;
DE   AltName: Full=Follistatin-like protein 1;
DE   Flags: Precursor;
GN   Name=FSTL1;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Plays
CC       a role in the development of the central nervous system, skeletal
CC       system, lungs, and ureter. Promotes endothelial cell survival,
CC       migration and differentiation into network structures in an AKT-
CC       dependent manner. Also promotes survival of cardiac myocytes (By
CC       similarity). Initiates various signaling cascades by activating
CC       different receptors on the cell surface such as DIP2A, TLR4 or BMP
CC       receptors (By similarity). {ECO:0000250|UniProtKB:Q12841,
CC       ECO:0000250|UniProtKB:Q62356}.
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. Interacts with BMP4. Interacts with CD14; this
CC       interaction promotes TL4-mediated signaling cascade (By similarity).
CC       {ECO:0000250|UniProtKB:Q12841, ECO:0000250|UniProtKB:Q62356,
CC       ECO:0000250|UniProtKB:Q62632}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; BC114758; AAI14759.1; -; mRNA.
DR   EMBL; BT021713; AAX46560.1; -; mRNA.
DR   RefSeq; NP_001017950.1; NM_001017950.2.
DR   RefSeq; XP_005200261.1; XM_005200204.2.
DR   AlphaFoldDB; Q58D84; -.
DR   SMR; Q58D84; -.
DR   STRING; 9913.ENSBTAP00000073919; -.
DR   MEROPS; I01.967; -.
DR   GlyCosmos; Q58D84; 3 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000029886; -.
DR   Ensembl; ENSBTAT00000029891.4; ENSBTAP00000029886.3; ENSBTAG00000022155.4.
DR   GeneID; 534482; -.
DR   KEGG; bta:534482; -.
DR   CTD; 11167; -.
DR   VEuPathDB; HostDB:ENSBTAG00000022155; -.
DR   VGNC; VGNC:29135; FSTL1.
DR   eggNOG; ENOG502QQAG; Eukaryota.
DR   GeneTree; ENSGT00940000157784; -.
DR   HOGENOM; CLU_038229_0_0_1; -.
DR   InParanoid; Q58D84; -.
DR   OMA; CIERCKP; -.
DR   OrthoDB; 3915502at2759; -.
DR   TreeFam; TF106409; -.
DR   Reactome; R-BTA-201451; Signaling by BMP.
DR   Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000022155; Expressed in subcutaneous adipose tissue and 106 other cell types or tissues.
DR   ExpressionAtlas; Q58D84; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
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   CDD; cd16233; EFh_SPARC_FSTL1; 1.
DR   CDD; cd00104; KAZAL_FS; 1.
DR   Gene3D; 3.30.60.30; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 1.
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   InterPro; IPR036773; TB_dom_sf.
DR   PANTHER; PTHR10913; FOLLISTATIN-RELATED; 1.
DR   PANTHER; PTHR10913:SF13; FOLLISTATIN-RELATED PROTEIN 1; 1.
DR   Pfam; PF09289; FOLN; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   SMART; SM00274; FOLN; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Heparin-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250|UniProtKB:Q12841"
FT   CHAIN           20..307
FT                   /note="Follistatin-related protein 1"
FT                   /id="PRO_0000318092"
FT   DOMAIN          29..52
FT                   /note="Follistatin-like"
FT   DOMAIN          47..99
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          143..177
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          192..227
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          232..286
FT                   /note="VWFC"
FT   MOD_RES         164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12841"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..41
FT                   /evidence="ECO:0000250|UniProtKB:Q62356"
FT   DISULFID        35..51
FT                   /evidence="ECO:0000250|UniProtKB:Q62356"
FT   DISULFID        53..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        57..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        65..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   307 AA;  34856 MW;  A4A8D1CE4F519A9F CRC64;
     MMWRRWLALA LVAVAWVHAE EQVRSKSKIC ANVFCGAGRE CAVTEKGEPT CLCIEQCKPH
     KRPVCGSNGK TYLNHCELHR DACLTGSKIQ VDYDGHCKEK KSVSPSASPV VCYQSNRDEL
     RRRIIQWLEA EIIPDGWFSK GSNYSEILDK YFKNFDNGDS RLDSSEFLKF VEQNETAINI
     TTYADQENNK LLRGLCVDAL IELSDENADW KLSFQEFLKC LNPSFNPPEK KCALEDETYA
     DGAETEVDCN RCVCACGNWV CTAMTCDGKN QKGAQTQAEE EMTRYVQELQ KHQETAEKSK
     RVSTKEI
//