FSTL1_BOVIN
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 03-AUG-2022, entry version 121.
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.ENSBTAP00000029886; -.
DR MEROPS; I01.967; -.
DR PaxDb; Q58D84; -.
DR Ensembl; ENSBTAT00000029891; ENSBTAP00000029886; ENSBTAG00000022155.
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; HRIIQWL; -.
DR OrthoDB; 1079836at2759; -.
DR TreeFam; TF106409; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000022155; Expressed in subcutaneous adipose tissue and 106 other 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:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central.
DR Gene3D; 3.90.290.10; -; 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 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 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
