GDF10_MOUSE
ID GDF10_MOUSE Reviewed; 476 AA.
AC P97737; Q6PE07;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Growth/differentiation factor 10;
DE Short=GDF-10;
DE AltName: Full=Bone morphogenetic protein 3B;
DE Short=BMP-3B;
DE Flags: Precursor;
GN Name=Gdf10 {ECO:0000312|MGI:MGI:95684}; Synonyms=Bmp3b;
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 TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Uterus;
RX PubMed=8679252; DOI=10.3109/08977199509028956;
RA Cunningham N.S., Jenkins N.A., Gilbert D.J., Copeland N.G., Reddi A.H.,
RA Lee S.-J.;
RT "Growth/differentiation factor-10: a new member of the transforming growth
RT factor-beta superfamily related to bone morphogenetic protein-3.";
RL Growth Factors 12:99-109(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=10419686; DOI=10.1006/dbio.1999.9326;
RA Zhao R., Lawler A.M., Lee S.J.;
RT "Characterization of GDF-10 expression patterns and null mice.";
RL Dev. Biol. 212:68-79(1999).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=21712809; DOI=10.1038/ijo.2011.124;
RA Hino J., Miyazawa T., Miyazato M., Kangawa K.;
RT "Bone morphogenetic protein-3b (BMP-3b) is expressed in adipocytes and
RT inhibits adipogenesis as a unique complex.";
RL Int. J. Obes. Relat. Metab. Disord. 36:725-734(2012).
RN [5]
RP FUNCTION.
RX PubMed=22155034; DOI=10.1016/j.mce.2011.11.023;
RA Matsumoto Y., Otsuka F., Hino J., Miyoshi T., Takano M., Miyazato M.,
RA Makino H., Kangawa K.;
RT "Bone morphogenetic protein-3b (BMP-3b) inhibits osteoblast differentiation
RT via Smad2/3 pathway by counteracting Smad1/5/8 signaling.";
RL Mol. Cell. Endocrinol. 350:78-86(2012).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=24963847; DOI=10.1002/glia.22710;
RA Mecklenburg N., Martinez-Lopez J.E., Moreno-Bravo J.A., Perez-Balaguer A.,
RA Puelles E., Martinez S.;
RT "Growth and differentiation factor 10 (Gdf10) is involved in Bergmann glial
RT cell development under Shh regulation.";
RL Glia 62:1713-1723(2014).
CC -!- FUNCTION: Growth factor involved in osteogenesis and adipogenesis.
CC Plays an inhibitory role in the process of osteoblast differentiation
CC via SMAD2/3 pathway (PubMed:22155034). Plays an inhibitory role in the
CC process of adipogenesis (PubMed:21712809).
CC {ECO:0000269|PubMed:21712809, ECO:0000269|PubMed:22155034}.
CC -!- SUBUNIT: Homodimer or heterodimer. Can form a non-covalent complex of
CC the mature region and the pro-region (PubMed:21712809).
CC {ECO:0000269|PubMed:21712809, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21712809}.
CC -!- TISSUE SPECIFICITY: Highly expressed in epididymal adipose tissue,
CC brain, bone and aorta and to a lesser extent in liver and spleen.
CC Expressed at higher levels in preadipocytes than in mature adipocytes
CC (PubMed:21712809). Strongly expressed in glial cells of the cerebellum
CC (PubMed:24963847). {ECO:0000269|PubMed:10419686,
CC ECO:0000269|PubMed:22155034, ECO:0000269|PubMed:24963847,
CC ECO:0000269|PubMed:8679252}.
CC -!- DEVELOPMENTAL STAGE: During embryogenes is expressed most prominently
CC in developing skeletal structures both in the craniofacial region and
CC in the vertebral column. {ECO:0000269|PubMed:10419686}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:10419686}.
CC -!- MISCELLANEOUS: 3T3-L1 cells endogenously secrete biologically active
CC Gdf10 as a unique complex that contains both the pro-region and the
CC mature region. {ECO:0000269|PubMed:21712809}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; S82648; AAB46753.1; -; mRNA.
DR EMBL; BC058358; AAH58358.1; -; mRNA.
DR CCDS; CCDS26927.1; -.
DR RefSeq; NP_665684.2; NM_145741.3.
DR AlphaFoldDB; P97737; -.
DR SMR; P97737; -.
DR STRING; 10090.ENSMUSP00000128621; -.
DR GlyGen; P97737; 4 sites.
DR PhosphoSitePlus; P97737; -.
DR MaxQB; P97737; -.
DR PaxDb; P97737; -.
DR PRIDE; P97737; -.
DR ProteomicsDB; 267784; -.
DR Antibodypedia; 73579; 283 antibodies from 28 providers.
DR DNASU; 14560; -.
DR Ensembl; ENSMUST00000168727; ENSMUSP00000128621; ENSMUSG00000021943.
DR GeneID; 14560; -.
DR KEGG; mmu:14560; -.
DR UCSC; uc007tab.1; mouse.
DR CTD; 2662; -.
DR MGI; MGI:95684; Gdf10.
DR VEuPathDB; HostDB:ENSMUSG00000021943; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000157214; -.
DR HOGENOM; CLU_020515_10_0_1; -.
DR InParanoid; P97737; -.
DR OMA; FHFYADK; -.
DR OrthoDB; 1002140at2759; -.
DR PhylomeDB; P97737; -.
DR TreeFam; TF316134; -.
DR BioGRID-ORCS; 14560; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Gdf10; mouse.
DR PRO; PR:P97737; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P97737; protein.
DR Bgee; ENSMUSG00000021943; Expressed in vault of skull and 229 other tissues.
DR Genevisible; P97737; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0042698; P:ovulation cycle; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0030278; P:regulation of ossification; IEA:Ensembl.
DR GO; GO:0071559; P:response to transforming growth factor beta; IEA:Ensembl.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR017197; BMP3/BMP3B.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR PIRSF; PIRSF037403; BMP3/GDF10; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Cytokine; Disulfide bond; Glycoprotein;
KW Growth factor; Osteogenesis; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..366
FT /evidence="ECO:0000255"
FT /id="PRO_0000033846"
FT CHAIN 367..476
FT /note="Growth/differentiation factor 10"
FT /id="PRO_0000033847"
FT REGION 39..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 374..441
FT /evidence="ECO:0000250"
FT DISULFID 403..473
FT /evidence="ECO:0000250"
FT DISULFID 407..475
FT /evidence="ECO:0000250"
FT DISULFID 440
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 142
FT /note="R -> G (in Ref. 1; AAB46753)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="G -> A (in Ref. 1; AAB46753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 52575 MW; FCFBD71BDBCE7E50 CRC64;
MAPGPARISL GSQLLPMVPL LLLLRGAGCG HRGPSWSSLP SAAAGLQGDR DSQQSPGDAA
AALGPGAQDM VAIHMLRLYE KYNRRGAPPG GGNTVRSFRA RLEMIDQKPV YFFNLTSMQD
SEMILTAAFH FYSEPPRWPR AREVFCKPRA KNASCRLLTP GLPARLHLIF RSLSQNTATQ
GLLRGAMALT PPPRGLWQAK DISSIIKAAR RDGELLLSAQ LDTGEKDPGV PRPSSHMPYI
LVYANDLAIS EPNSVAVSLQ RYDPFPAGDF EPGAAPNSSA DPRVRRAAQV SKPLQDNELP
GLDERPAPAL HAQNFHKHEF WSSPFRALKP RTGRKDRKKK DQDTFTAASS QVLDFDEKTM
QKARRRQWDE PRVCSRRYLK VDFADIGWNE WIISPKSFDA YYCAGACEFP MPKIVRPSNH
ATIQSIVRAV GIVPGIPEPC CVPDKMNSLG VLFLDENRNA VLKVYPNMSV ETCACR
