ID   SOST_BOVIN              Reviewed;         212 AA.
AC   Q9BG79;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Sclerostin {ECO:0000250|UniProtKB:Q99P68};
DE   Flags: Precursor;
GN   Name=SOST {ECO:0000250|UniProtKB:Q9BQB4};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 31-206.
RX   PubMed=11179006; DOI=10.1086/318811;
RA   Brunkow M.E., Gardner J.C., Van Ness J., Paeper B.W., Kovacevich B.R.,
RA   Proll S., Skonier J.E., Zhao L., Sabo P.J., Fu Y.H., Alisch R.S.,
RA   Gillett L., Colbert T., Tacconi P., Galas D., Hamersma H., Beighton P.,
RA   Mulligan J.T.;
RT   "Bone dysplasia sclerosteosis results from loss of the SOST gene product, a
RT   novel cystine knot-containing protein.";
RL   Am. J. Hum. Genet. 68:577-589(2001).
CC   -!- FUNCTION: Negative regulator of bone growth that acts through
CC       inhibition of Wnt signaling and bone formation. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with LRP4 (via the extracellular domain); the
CC       interaction facilitates the inhibition of Wnt signaling. Interacts with
CC       LRP5 (via the first two YWTD-EGF repeat domains); the interaction
CC       inhibits Wnt-mediated signaling. Interacts with LRP6. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sclerostin family. {ECO:0000305}.
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DR   EMBL; AAFC03014844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF326738; AAK13453.1; -; mRNA.
DR   AlphaFoldDB; Q9BG79; -.
DR   SMR; Q9BG79; -.
DR   STRING; 9913.ENSBTAP00000017458; -.
DR   PaxDb; Q9BG79; -.
DR   eggNOG; ENOG502QTBG; Eukaryota.
DR   InParanoid; Q9BG79; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0036122; F:BMP binding; IBA:GO_Central.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0030279; P:negative regulation of ossification; IEA:InterPro.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0001503; P:ossification; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR008835; Sclerostin/SOSTDC1.
DR   InterPro; IPR015665; SOST.
DR   PANTHER; PTHR14903; PTHR14903; 1.
DR   PANTHER; PTHR14903:SF4; PTHR14903:SF4; 1.
DR   Pfam; PF05463; Sclerostin; 1.
DR   SMART; SM00041; CT; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Heparin-binding;
KW   Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..212
FT                   /note="Sclerostin"
FT                   /id="PRO_0000181339"
FT   DOMAIN          81..171
FT                   /note="CTCK"
FT   REGION          179..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        79..133
FT                   /evidence="ECO:0000250"
FT   DISULFID        93..147
FT                   /evidence="ECO:0000250"
FT   DISULFID        104..164
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..166
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  23777 MW;  F3D373871A62CEA5 CRC64;
     MQLSLALCLV CLLVHAAFRV VEGQGWQAFK NDATEIIPEL GEYPEPLPEL NNKTMNRAEN
     GGRPPHHPFE TKDASEYSCR ELHFTRYVTD GPCRSAKPVT ELVCSGQCGP ARLLPNAIGR
     GKWWRPSGPD FRCIPDRYRA QRVQLLCPGG AAPRARKVRL VASCKCKRLT RFHNQSELKD
     FGPEAARPQT GRKLRPRARG TKASRAELEN AY