ID   SOSD1_PONAB             Reviewed;         206 AA.
AC   Q5R5D2;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Sclerostin domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=SOSTDC1;
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: Directly antagonizes activity of BMP2, BMP4, BMP6 and BMP7 in
CC       a dose-dependent manner. Enhances Wnt signaling and inhibits TGF-beta
CC       signaling. May be involved in the onset of endometrial receptivity for
CC       implantation/sensitization for the decidual cell reaction (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with BMP2, BMP4, BMP6 and BMP7 with high affinity.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sclerostin family. {ECO:0000305}.
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DR   EMBL; CR860930; CAH93034.1; -; mRNA.
DR   RefSeq; NP_001126795.1; NM_001133323.1.
DR   AlphaFoldDB; Q5R5D2; -.
DR   SMR; Q5R5D2; -.
DR   STRING; 9601.ENSPPYP00000019915; -.
DR   Ensembl; ENSPPYT00000020701; ENSPPYP00000019915; ENSPPYG00000017767.
DR   GeneID; 100173799; -.
DR   KEGG; pon:100173799; -.
DR   CTD; 25928; -.
DR   eggNOG; ENOG502QV5G; Eukaryota.
DR   GeneTree; ENSGT00390000014900; -.
DR   HOGENOM; CLU_087969_0_0_1; -.
DR   InParanoid; Q5R5D2; -.
DR   OMA; KFWARRS; -.
DR   OrthoDB; 1511387at2759; -.
DR   TreeFam; TF353019; -.
DR   Proteomes; UP000001595; Chromosome 7.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0036122; F:BMP binding; IEA:Ensembl.
DR   GO; GO:0098821; F:BMP receptor activity; IEA:Ensembl.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0072148; P:epithelial cell fate commitment; IEA:Ensembl.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
DR   GO; GO:0060648; P:mammary gland bud morphogenesis; IEA:Ensembl.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0010454; P:negative regulation of cell fate commitment; IEA:Ensembl.
DR   GO; GO:2000016; P:negative regulation of determination of dorsal identity; IEA:Ensembl.
DR   GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
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   PANTHER; PTHR14903; PTHR14903; 1.
DR   Pfam; PF05463; Sclerostin; 1.
DR   PROSITE; PS01225; CTCK_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal;
KW   Wnt signaling pathway.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..206
FT                   /note="Sclerostin domain-containing protein 1"
FT                   /id="PRO_0000033182"
FT   DOMAIN          75..170
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   REGION          176..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..206
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        89..147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        100..163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        104..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
SQ   SEQUENCE   206 AA;  23297 MW;  0F8CCEBE364817E6 CRC64;
     MLPPAIHFYL LPLACILMKS CLAFKNDATE ILYSHVVKPV PAHPSSNSTL NQARNGGRHF
     SNTGLDRNTR VQVGCRELRS TKYISDGQCT SISPLKELVC AGECLPLSVL PNWIGGGYGT
     KYWSRRSSQE WRCVNDKTRT QRIQLQCQDG STRTYKITVV TACKCKRYTR QHNESSHNFE
     SMSPAKPVQH HRERKRASKS SKHSMS