FSTL1_MACFA
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 03-AUG-2022, entry version 98.
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}.
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DR EMBL; AB039661; BAB20770.1; -; mRNA.
DR RefSeq; NP_001306351.1; NM_001319422.1.
DR AlphaFoldDB; Q9GKY0; -.
DR SMR; Q9GKY0; -.
DR STRING; 9541.XP_005548104.1; -.
DR MEROPS; I01.967; -.
DR Ensembl; ENSMFAT00000025999; ENSMFAP00000007309; ENSMFAG00000036133.
DR GeneID; 102131597; -.
DR CTD; 11167; -.
DR eggNOG; ENOG502QQAG; Eukaryota.
DR GeneTree; ENSGT00940000157784; -.
DR Proteomes; UP000233100; Chromosome 2.
DR Bgee; ENSMFAG00000036133; Expressed in heart and 13 other 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 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 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
