FSTL1_PONAB
ID FSTL1_PONAB Reviewed; 306 AA.
AC Q5R9Y1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Follistatin-related protein 1;
DE AltName: Full=Follistatin-like protein 1;
DE Flags: Precursor;
GN Name=FSTL1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91429.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR859249; CAH91429.1; ALT_INIT; mRNA.
DR RefSeq; NP_001125838.1; NM_001132366.1.
DR AlphaFoldDB; Q5R9Y1; -.
DR SMR; Q5R9Y1; -.
DR STRING; 9601.ENSPPYP00000015102; -.
DR MEROPS; I01.967; -.
DR GeneID; 100172767; -.
DR KEGG; pon:100172767; -.
DR CTD; 11167; -.
DR eggNOG; ENOG502QQAG; Eukaryota.
DR HOGENOM; CLU_038229_0_0_1; -.
DR InParanoid; Q5R9Y1; -.
DR OMA; HRIIQWL; -.
DR OrthoDB; 1079836at2759; -.
DR TreeFam; TF106409; -.
DR Proteomes; UP000001595; Unplaced.
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: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..18
FT /evidence="ECO:0000250|UniProtKB:Q12841"
FT CHAIN 19..306
FT /note="Follistatin-related protein 1"
FT /id="PRO_0000329283"
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; 34829 MW; 838A0DC9BEC99D9B CRC64;
MWKRWLALAL VAVAWVRAEE ELRSKSKICA NVFCGAGREC AVTEKGEPTC LCIEQCKPHK
RPVCGSNGKT YLNHCELHRD ACLTGSKIQV DYDGHCKEKK SVSPSASPVV CYQSNRDELR
RRIIQWLEAE IIPDGWFSRG SNYSEILDKY FKNFDNGDSR LDSSEFLKFV EQNETAINIT
TYPDQENNKL LRGLCVDALI ELSDENADWK LSFQEFLKCL NPSFNPPEKK CALEDETYAD
GAETEVDCNR CVCACGNWVC TAMTCDGKNQ KGAQTQTEEE MTRYVQELQK HQETAEKTKR
VSTKEI
