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   24-JAN-2024, entry version 97.
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   MEROPS; I01.967; -.
DR   GlyCosmos; Q5R9Y1; 3 sites, No reported glycans.
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; CIERCKP; -.
DR   OrthoDB; 3915502at2759; -.
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   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..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
//