GDF10_RAT
ID GDF10_RAT Reviewed; 476 AA.
AC P55108;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Growth/differentiation factor 10;
DE Short=GDF-10;
DE AltName: Full=Bone morphogenetic protein 3B;
DE Short=BMP-3B;
DE AltName: Full=Bone-inducing protein;
DE Short=BIP;
DE Flags: Precursor;
GN Name=Gdf10 {ECO:0000312|RGD:621512}; Synonyms=Bmp3b;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Femur;
RX PubMed=8605043; DOI=10.1006/bbrc.1996.0289;
RA Takao M., Hino J., Takeshita N., Konno Y., Nishizawa T., Matsuo H.,
RA Kangawa K.;
RT "Identification of rat bone morphogenetic protein-3b (BMP-3b), a new member
RT of BMP-3.";
RL Biochem. Biophys. Res. Commun. 219:656-662(1996).
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. Plays an inhibitory role in the process of
CC adipogenesis. {ECO:0000250|UniProtKB:P97737}.
CC -!- SUBUNIT: Homodimer or heterodimer. Can form a non-covalent complex of
CC the mature region and the pro-region. {ECO:0000250|UniProtKB:P97737}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P97737}.
CC -!- TISSUE SPECIFICITY: Costa, costicartilage, femur, calvaria, trachea,
CC aorta and brain. Predominantly in the cerebellum.
CC {ECO:0000269|PubMed:8605043}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; D49494; BAA08454.1; -; mRNA.
DR PIR; JC4646; JC4646.
DR RefSeq; NP_077351.1; NM_024375.1.
DR AlphaFoldDB; P55108; -.
DR SMR; P55108; -.
DR GlyGen; P55108; 4 sites.
DR PRIDE; P55108; -.
DR Ensembl; ENSRNOT00000081183; ENSRNOP00000069581; ENSRNOG00000051993.
DR GeneID; 79216; -.
DR KEGG; rno:79216; -.
DR UCSC; RGD:621512; rat.
DR CTD; 2662; -.
DR RGD; 621512; Gdf10.
DR GeneTree; ENSGT00940000157214; -.
DR InParanoid; P55108; -.
DR OrthoDB; 1002140at2759; -.
DR PhylomeDB; P55108; -.
DR PRO; PR:P55108; -.
DR Proteomes; UP000002494; Chromosome 16.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
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; IEP:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IEP:RGD.
DR GO; GO:0042698; P:ovulation cycle; IEP:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:RGD.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0030278; P:regulation of ossification; IEP:RGD.
DR GO; GO:0071559; P:response to transforming growth factor beta; IEP:RGD.
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 2: Evidence at transcript 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_0000033848"
FT CHAIN 367..476
FT /note="Growth/differentiation factor 10"
FT /id="PRO_0000033849"
FT REGION 268..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..358
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"
SQ SEQUENCE 476 AA; 52961 MW; 873F4D4150C625EE CRC64;
MAPGLARISL RSQLLPLVPL LLLLRGAGCG HRVPSWSSLP SAADSVQRDR DLQQSPGDAA
AALGPGAQDI VAVHMLRLYE KYNRRGAPPG GGNTVRSFRA RLDVIDQKPV YFFNLTSMQD
SEMILTATFH FYSEPPRWPR AREVFCKPRA KNASCRLLTP GLPARLHLIF RSLSQNTATQ
GLLRGAMALT PPPRGLWQAK DISSIIKAAR RDGELLLSAQ LDSGEKDLGV PRPSSHMPYI
LVYANDLAIS EPNSVAVTLQ RYDPFPAGDF EPGAAPNSSA DPRVRRAAQV SKPLQDNELP
GLDERPAPAL HAQHFHKHEF WSSPFRALKP RTGRKDRKKK DQDTFTPSSS QVLDFDEKTM
QKARRRQWDE PRVCSRRYLK VDFADIGWNE WIISPKSFDA YYCAGACEFP MPKIVRPSNH
ATIQSIVRAV GIVPGIPEPC CVPDKMNSLG VLFLDENRNV VLKVYPNMSV ETCACR
