SOSD1_RAT
ID SOSD1_RAT Reviewed; 206 AA.
AC Q642G2; Q8CJA4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Sclerostin domain-containing protein 1;
DE AltName: Full=Uterine sensitization-associated gene 1 protein;
DE Short=USAG-1;
DE AltName: Full=Wnt-signaling modulator;
DE Flags: Precursor;
GN Name=Sostdc1; Synonyms=Usag1, Wise;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RX PubMed=12390898; DOI=10.1095/biolreprod.102.006858;
RA Simmons D.G., Kennedy T.G.;
RT "Uterine sensitization-associated gene-1: a novel gene induced within the
RT rat endometrium at the time of uterine receptivity/sensitization for the
RT decidual cell reaction.";
RL Biol. Reprod. 67:1638-1645(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15373764; DOI=10.1111/j.0022-202x.2004.23410.x;
RA O'Shaughnessy R.F.L., Yeo W., Gautier J., Jahoda C.A.B., Christiano A.M.;
RT "The WNT signalling modulator, Wise, is expressed in an interaction-
RT dependent manner during hair-follicle cycling.";
RL J. Invest. Dermatol. 123:613-621(2004).
CC -!- FUNCTION: Directly antagonizes activity of BMP2, BMP4, BMP6 and BMP7 in
CC a dose-dependent manner (By similarity). May be involved in the onset
CC of endometrial receptivity for implantation/sensitization for the
CC decidual cell reaction. Enhances Wnt signaling and inhibits TGF-beta
CC signaling. {ECO:0000250, ECO:0000269|PubMed:12390898,
CC ECO:0000269|PubMed:15373764}.
CC -!- SUBUNIT: Interacts with BMP2, BMP4, BMP6 and BMP7 with high affinity.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15373764}.
CC -!- TISSUE SPECIFICITY: Highly expressed within the maximally
CC sensitized/receptive endometrium. Weakly expressed in brain, kidney and
CC the female reproductive tract. Expressed in the dermal papilla (DP) and
CC at high level in the precortex of both anagen vibrissae and pelage
CC follicles. Dynymic expression during the hair cycle.
CC {ECO:0000269|PubMed:12390898, ECO:0000269|PubMed:15373764}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in epidermis, dermis and the
CC outermost periderm layer in the 17 day post-coitum (dpc).
CC {ECO:0000269|PubMed:15373764}.
CC -!- INDUCTION: Up-regulated at day 5 pregnant or pseudopregnant of the
CC uterine glandular epithelial cells, at time of maximal sensitization
CC for the decidual cell reaction. Down-regulated at day 6 refractory
CC uterus. {ECO:0000269|PubMed:12390898}.
CC -!- SIMILARITY: Belongs to the sclerostin family. {ECO:0000305}.
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DR EMBL; AF411056; AAN45848.1; -; mRNA.
DR EMBL; BC081710; AAH81710.1; -; mRNA.
DR RefSeq; NP_714959.1; NM_153737.1.
DR AlphaFoldDB; Q642G2; -.
DR SMR; Q642G2; -.
DR STRING; 10116.ENSRNOP00000008106; -.
DR GlyGen; Q642G2; 2 sites.
DR PaxDb; Q642G2; -.
DR PRIDE; Q642G2; -.
DR Ensembl; ENSRNOT00000008106; ENSRNOP00000008106; ENSRNOG00000005770.
DR GeneID; 266803; -.
DR KEGG; rno:266803; -.
DR UCSC; RGD:628877; rat.
DR CTD; 25928; -.
DR RGD; 628877; Sostdc1.
DR eggNOG; ENOG502QV5G; Eukaryota.
DR GeneTree; ENSGT00390000014900; -.
DR HOGENOM; CLU_087969_0_0_1; -.
DR InParanoid; Q642G2; -.
DR OMA; KFWARRS; -.
DR OrthoDB; 1511387at2759; -.
DR PhylomeDB; Q642G2; -.
DR TreeFam; TF353019; -.
DR PRO; PR:Q642G2; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000005770; Expressed in kidney and 16 other tissues.
DR Genevisible; Q642G2; RN.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0036122; F:BMP binding; ISO:RGD.
DR GO; GO:0098821; F:BMP receptor activity; ISO:RGD.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; NAS:RGD.
DR GO; GO:0072148; P:epithelial cell fate commitment; IEA:Ensembl.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0060648; P:mammary gland bud morphogenesis; ISO:RGD.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0010454; P:negative regulation of cell fate commitment; ISO:RGD.
DR GO; GO:2000016; P:negative regulation of determination of dorsal identity; ISO:RGD.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; ISO:RGD.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0007389; P:pattern specification process; ISO:RGD.
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_0000033183"
FT DOMAIN 75..170
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 42..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT CONFLICT 187
FT /note="P -> L (in Ref. 1; AAN45848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 23136 MW; 52BD602431C6DD15 CRC64;
MLPPAIHLSL IPLLCILMKN CLAFKNDATE ILYSHVVKPV SAHPSSNSTL NQARNGGRHF
SSTGLDRNSR VQVGCRELRS TKYISDGQCT SISPLKELVC AGECLPLPVL PNWIGGGYGT
KYWSRRSSQE WRCVNDKTRT QRIQLQCQDG STRTYKITVV TACKCKRYTR QHNESSHNFE
SVSPAKPAQH HRERKRASKS SKHSLS