ID FSTL1_MACFA Reviewed; 308 AA. AC Q9GKY0; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 102. DE RecName: Full=Follistatin-related protein 1; DE AltName: Full=Follistatin-like protein 1; DE Flags: Precursor; GN Name=FSTL1; Synonyms=OCC1; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=11168534; DOI=10.1046/j.0953-816x.2000.01390.x; RA Tochitani S., Liang F., Watakabe A., Hashikawa T., Yamamori T.; RT "The occ1 gene is preferentially expressed in the primary visual cortex in RT an activity-dependent manner: a pattern of gene expression related to the RT cytoarchitectonic area in adult macaque neocortex."; RL Eur. J. Neurosci. 13:297-307(2001). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB039661; BAB20770.1; -; mRNA. DR RefSeq; NP_001306351.1; NM_001319422.1. DR AlphaFoldDB; Q9GKY0; -. DR SMR; Q9GKY0; -. DR MEROPS; I01.967; -. DR GlyCosmos; Q9GKY0; 3 sites, No reported glycans. DR Ensembl; ENSMFAT00000025999.2; ENSMFAP00000007309.2; ENSMFAG00000036133.2. DR eggNOG; ENOG502QQAG; Eukaryota. DR GeneTree; ENSGT00940000157784; -. DR OrthoDB; 3915502at2759; -. DR Proteomes; UP000233100; Chromosome 2. DR Bgee; ENSMFAG00000036133; Expressed in heart and 13 other cell types or tissues. 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: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 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 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 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..20 FT /evidence="ECO:0000250|UniProtKB:Q12841" FT CHAIN 21..308 FT /note="Follistatin-related protein 1" FT /id="PRO_0000010112" FT DOMAIN 30..53 FT /note="Follistatin-like" FT DOMAIN 48..100 FT /note="Kazal-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DOMAIN 144..178 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 193..228 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 233..287 FT /note="VWFC" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q12841" FT CARBOHYD 144 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 175 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 180 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 31..42 FT /evidence="ECO:0000250|UniProtKB:Q62356" FT DISULFID 36..52 FT /evidence="ECO:0000250|UniProtKB:Q62356" FT DISULFID 54..84 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DISULFID 58..77 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" FT DISULFID 66..98 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798" SQ SEQUENCE 308 AA; 35000 MW; 4B2836D9CDF535D9 CRC64; MWKRWLALAL ALVAVAWVRA EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSISPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEI //