ID   SOST_CHLAE              Reviewed;         213 AA.
AC   Q9BG78;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Sclerostin {ECO:0000250|UniProtKB:Q99P68};
DE   Flags: Precursor;
GN   Name=SOST {ECO:0000250|UniProtKB:Q9BQB4};
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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}.
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; AF326742; AAK13457.1; -; mRNA.
DR   AlphaFoldDB; Q9BG78; -.
DR   SMR; Q9BG78; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030279; P:negative regulation of ossification; IEA:InterPro.
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   Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..213
FT                   /note="Sclerostin"
FT                   /id="PRO_0000033176"
FT   DOMAIN          82..172
FT                   /note="CTCK"
FT   REGION          41..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        80..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        94..148
FT                   /evidence="ECO:0000250"
FT   DISULFID        105..165
FT                   /evidence="ECO:0000250"
FT   DISULFID        109..167
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  23908 MW;  6DA7B5EDE674728A CRC64;
     MQLPLALCLV CLLVHAAFRV VEGQGWQAFK NDATEIIPEL GEYPEPPPEL ENNKTMNRAE
     NGGRPPHHPF ETKDVSEYSC RELHFTRYVT DGPCRSAKPV TELVCSGQCG PARLLPNAIG
     RGKWWRPSGP DFRCIPDRYR AQRVQLLCPG GAAPRARKVR LVASCKCKRL TRFHNQSELK
     DFGPEAARPQ KGRKPRPRAR GAKANQAELE NAY