SOSD1_MOUSE
ID SOSD1_MOUSE Reviewed; 206 AA.
AC Q9CQN4; Q8CF09;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Sclerostin domain-containing protein 1;
DE AltName: Full=Ectodermal BMP inhibitor;
DE Short=Ectodin;
DE AltName: Full=Sclerostin-like protein;
DE AltName: Full=Uterine sensitization-associated gene 1 protein;
DE Short=USAG-1;
DE Flags: Precursor;
GN Name=Sostdc1; Synonyms=Sostl, Usag1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=12617826; DOI=10.1016/s1567-133x(02)00022-4;
RA Menke D.B., Page D.C.;
RT "Sexually dimorphic gene expression in the developing mouse gonad.";
RL Gene Expr. Patterns 2:359-367(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH BMP2; BMP4; BMP6 AND
RP BMP7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=14623234; DOI=10.1016/j.ydbio.2003.08.011;
RA Laurikkala J., Kassai Y., Pakkasjaervi L., Thesleff I., Itoh N.;
RT "Identification of a secreted BMP antagonist, ectodin, integrating BMP,
RT FGF, and SHH signals from the tooth enamel knot.";
RL Dev. Biol. 264:91-105(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA O'Shaughnessy R.F.L., Yeo W., Gautier J., Jahoda C.A.B., Christiano A.M.;
RT "A novel secreted WNT agonist is a requirement for epithelial-mesenchymal
RT interactions.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15020244; DOI=10.1016/j.bbrc.2004.02.075;
RA Yanagita M., Oka M., Watabe T., Iguchi H., Niida A., Takahashi S.,
RA Akiyama T., Miyazono K., Yanagisawa M., Sakurai T.;
RT "USAG-1: a bone morphogenetic protein antagonist abundantly expressed in
RT the kidney.";
RL Biochem. Biophys. Res. Commun. 316:490-500(2004).
CC -!- FUNCTION: May be involved in the onset of endometrial receptivity for
CC implantation/sensitization for the decidual cell reaction. Enhances Wnt
CC signaling and inhibits TGF-beta signaling (By similarity). Directly
CC antagonizes activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent
CC manner. {ECO:0000250, ECO:0000269|PubMed:14623234}.
CC -!- SUBUNIT: Interacts with BMP2, BMP4, BMP6 and BMP7 with high affinity.
CC {ECO:0000269|PubMed:14623234}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14623234}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney at renal collecting
CC ducts level and weakly in brain. {ECO:0000269|PubMed:14623234,
CC ECO:0000269|PubMed:15020244}.
CC -!- DEVELOPMENTAL STAGE: Expression was first detected at 11 dpc throughout
CC the surface of the embryo, and it was most intense in the head region
CC on the surfaces of the mandibular, maxillary, and frontonasal
CC processes. At 11.5 dpc expression is detected in the first and second
CC branchial arches, pharynx and metanephros. At 12 dpc-14 dpc, expression
CC was intense and strikingly confined to developing ectodermal organs.
CC The vibrissae, tylotrich hair follicles, tongue papillae, and tooth
CC germs as well as the ear auricle. Also expressed intensely in kidney
CC epithelium in the stalk and tips of ureter as well as in the spermatic
CC ducts in the testis. At 17.5 dpc strong expression was restricted to
CC kidney tubules and ameloblasts in teeth, and moderate expression was
CC observed in hair follicles, choroids plexus of the fourth cerebral
CC ventricle of the brain. First detected on 12.5 dpc in interstitial cell
CC of the testis and increased towards 14.5 dpc. On 8 dpp (day post
CC partum) highly expression was detected in kidney and weakly in skin.
CC {ECO:0000269|PubMed:12617826, ECO:0000269|PubMed:14623234,
CC ECO:0000269|PubMed:15020244}.
CC -!- INDUCTION: Up-regulated by BMP2 and BMP7. Down-regulated by FGF4 and
CC SHH. {ECO:0000269|PubMed:14623234}.
CC -!- SIMILARITY: Belongs to the sclerostin family. {ECO:0000305}.
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DR EMBL; AY134666; AAN08617.1; -; mRNA.
DR EMBL; AB059271; BAC20332.1; -; mRNA.
DR EMBL; AY255635; AAQ83297.1; -; mRNA.
DR EMBL; AK002240; BAB21957.1; -; mRNA.
DR EMBL; AK002396; BAB22068.1; -; mRNA.
DR EMBL; AK007893; BAB25333.1; -; mRNA.
DR EMBL; AK007935; BAC25193.1; -; mRNA.
DR EMBL; AK007967; BAB25378.1; -; mRNA.
DR EMBL; BC021458; AAH21458.1; -; mRNA.
DR CCDS; CCDS25887.1; -.
DR RefSeq; NP_079588.1; NM_025312.3.
DR AlphaFoldDB; Q9CQN4; -.
DR SMR; Q9CQN4; -.
DR STRING; 10090.ENSMUSP00000040230; -.
DR GlyGen; Q9CQN4; 2 sites.
DR PhosphoSitePlus; Q9CQN4; -.
DR MaxQB; Q9CQN4; -.
DR PaxDb; Q9CQN4; -.
DR PRIDE; Q9CQN4; -.
DR ProteomicsDB; 261113; -.
DR Antibodypedia; 56432; 149 antibodies from 17 providers.
DR DNASU; 66042; -.
DR Ensembl; ENSMUST00000041407; ENSMUSP00000040230; ENSMUSG00000036169.
DR GeneID; 66042; -.
DR KEGG; mmu:66042; -.
DR UCSC; uc007njx.2; mouse.
DR CTD; 25928; -.
DR MGI; MGI:1913292; Sostdc1.
DR VEuPathDB; HostDB:ENSMUSG00000036169; -.
DR eggNOG; ENOG502QV5G; Eukaryota.
DR GeneTree; ENSGT00390000014900; -.
DR HOGENOM; CLU_087969_0_0_1; -.
DR InParanoid; Q9CQN4; -.
DR OMA; KFWARRS; -.
DR OrthoDB; 1511387at2759; -.
DR PhylomeDB; Q9CQN4; -.
DR TreeFam; TF353019; -.
DR BioGRID-ORCS; 66042; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Sostdc1; mouse.
DR PRO; PR:Q9CQN4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9CQN4; protein.
DR Bgee; ENSMUSG00000036169; Expressed in choroid plexus epithelium and 225 other tissues.
DR Genevisible; Q9CQN4; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0036122; F:BMP binding; ISO:MGI.
DR GO; GO:0098821; F:BMP receptor activity; ISO:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0072148; P:epithelial cell fate commitment; IMP:MGI.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR GO; GO:0060648; P:mammary gland bud morphogenesis; IMP:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0010454; P:negative regulation of cell fate commitment; IMP:MGI.
DR GO; GO:2000016; P:negative regulation of determination of dorsal identity; ISO:MGI.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; ISO:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
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 1: Evidence at protein 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_0000033181"
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 69
FT /note="S -> R (in Ref. 4; BAC25193)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="S -> T (in Ref. 4; BAC25193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 23174 MW; 70D24819EB06CBC9 CRC64;
MLPPAIHLSL IPLLCILMRN CLAFKNDATE ILYSHVVKPV PAHPSSNSTL NQARNGGRHF
SSTGLDRNSR VQVGCRELRS TKYISDGQCT SISPLKELVC AGECLPLPVL PNWIGGGYGT
KYWSRRSSQE WRCVNDKTRT QRIQLQCQDG STRTYKITVV TACKCKRYTR QHNESSHNFE
SVSPAKPAQH HRERKRASKS SKHSLS
