FSTL1_RAT
ID FSTL1_RAT Reviewed; 306 AA.
AC Q62632;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Follistatin-related protein 1;
DE AltName: Full=Follistatin-like protein 1;
DE Flags: Precursor;
GN Name=Fstl1; Synonyms=Frp;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=7957230; DOI=10.1111/j.1432-1033.1994.0937b.x;
RA Zwijsen A., Blockx H., van Arnhem W., Willems J., Fransen L., Devos K.,
RA Raymackers J., van de Voorde A., Slegers H.;
RT "Characterization of a rat C6 glioma-secreted follistatin-related protein
RT (FRP). Cloning and sequence of the human homologue.";
RL Eur. J. Biochem. 225:937-946(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH SCN10A.
RX PubMed=12591166; DOI=10.1016/s0169-328x(02)00661-7;
RA Malik-Hall M., Poon W.-Y.L., Baker M.D., Wood J.N., Okuse K.;
RT "Sensory neuron proteins interact with the intracellular domains of sodium
RT channel NaV1.8.";
RL Brain Res. Mol. Brain Res. 110:298-304(2003).
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
CC (PubMed:12591166). Interacts with DIP2A; DIP2A may act as a cell
CC surface receptor for FSTL1. Interacts with BMP4. Interacts with CD14;
CC this interaction promotes TL4-mediated signaling cascade (By
CC similarity). {ECO:0000250|UniProtKB:Q12841,
CC ECO:0000250|UniProtKB:Q62356, ECO:0000269|PubMed:12591166}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; U06864; AAA66063.1; -; mRNA.
DR EMBL; BC087014; AAH87014.1; -; mRNA.
DR PIR; S51361; S51361.
DR RefSeq; NP_077345.1; NM_024369.2.
DR AlphaFoldDB; Q62632; -.
DR SMR; Q62632; -.
DR IntAct; Q62632; 1.
DR MEROPS; I01.967; -.
DR GlyGen; Q62632; 3 sites.
DR PhosphoSitePlus; Q62632; -.
DR jPOST; Q62632; -.
DR PaxDb; Q62632; -.
DR Ensembl; ENSRNOT00000103472; ENSRNOP00000095289; ENSRNOG00000002746.
DR GeneID; 79210; -.
DR KEGG; rno:79210; -.
DR UCSC; RGD:68955; rat.
DR CTD; 11167; -.
DR RGD; 68955; Fstl1.
DR eggNOG; ENOG502QQAG; Eukaryota.
DR GeneTree; ENSGT00940000157784; -.
DR HOGENOM; CLU_038229_0_0_1; -.
DR InParanoid; Q62632; -.
DR OMA; HRIIQWL; -.
DR OrthoDB; 1079836at2759; -.
DR PhylomeDB; Q62632; -.
DR Reactome; R-RNO-201451; Signaling by BMP.
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:Q62632; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000002746; Expressed in esophagus and 19 other tissues.
DR ExpressionAtlas; Q62632; baseline and differential.
DR Genevisible; Q62632; RN.
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; ISO:RGD.
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 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 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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heparin-binding;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:7957230"
FT CHAIN 19..306
FT /note="Follistatin-related protein 1"
FT /id="PRO_0000010114"
FT DOMAIN 28..51
FT /note="Follistatin-like"
FT DOMAIN 46..98
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 142..176
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 191..226
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 231..285
FT /note="VWFC"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12841"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..40
FT /evidence="ECO:0000250|UniProtKB:Q62356"
FT DISULFID 34..50
FT /evidence="ECO:0000250|UniProtKB:Q62356"
FT DISULFID 52..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 56..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 64..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 306 AA; 34622 MW; 46E197AC7EE0F3D4 CRC64;
MWKRWLALAL VTIALVHGEE EQRSKSKICA NVFCGAGREC AVTEKGEPTC LCIEQCKPHK
RPVCGSNGKT YLNHCELHRD ACLTGSKIQV DYDGHCKEKK SVSPSASPVV CYQANRDELR
RRIIQWLEAE IIPDGWFSKG SNYSEILDKY FKSFDNGDSH LDSSEFLKFV EQNETAVNIT
AYPNQENNKL LRGLCVDALI ELSDENADWK LSFQEFLKCL NPSFNPPEKK CALEDETYAD
GAETEVDCNR CVCSCGHWVC TAMTCDGKNQ KGVQTHTEEE MTRYAQELQK HQGTAEKTKK
VNTKEI
