ID   GDF10_BOVIN             Reviewed;         478 AA.
AC   Q08DX6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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; Synonyms=BMP3B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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       ECO:0000250|UniProtKB:Q7T2X6}.
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   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; BC123524; AAI23525.1; -; mRNA.
DR   RefSeq; NP_001069635.1; NM_001076167.2.
DR   AlphaFoldDB; Q08DX6; -.
DR   SMR; Q08DX6; -.
DR   STRING; 9913.ENSBTAP00000001351; -.
DR   PaxDb; Q08DX6; -.
DR   Ensembl; ENSBTAT00000001351; ENSBTAP00000001351; ENSBTAG00000001019.
DR   GeneID; 539510; -.
DR   KEGG; bta:539510; -.
DR   CTD; 2662; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001019; -.
DR   VGNC; VGNC:29299; GDF10.
DR   eggNOG; KOG3900; Eukaryota.
DR   GeneTree; ENSGT00940000157214; -.
DR   HOGENOM; CLU_020515_10_0_1; -.
DR   InParanoid; Q08DX6; -.
DR   OMA; FHFYADK; -.
DR   OrthoDB; 1002140at2759; -.
DR   TreeFam; TF316134; -.
DR   Proteomes; UP000009136; Chromosome 28.
DR   Bgee; ENSBTAG00000001019; Expressed in myometrium and 63 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0001649; P:osteoblast differentiation; IEA:InterPro.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
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..33
FT                   /evidence="ECO:0000255"
FT   PROPEP          34..368
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000285571"
FT   CHAIN           369..478
FT                   /note="Growth/differentiation factor 10"
FT                   /id="PRO_0000285572"
FT   REGION          34..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        376..443
FT                   /evidence="ECO:0000250"
FT   DISULFID        405..475
FT                   /evidence="ECO:0000250"
FT   DISULFID        409..477
FT                   /evidence="ECO:0000250"
FT   DISULFID        442
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  52626 MW;  6296B1722A8AE9DA CRC64;
     MARGPARTSL GPGSQQLPLL SLLLLLLLRD ADGSHTAAAR PPPPAAADGL AGDKNPQRSP
     GDVAAAQSPG AQDMVAVHML RLYEKYSRRG ARPGGGNTVR SFRARLEVVN QKAVYFFNLT
     SMQDSEMILT ATFHFYSEPQ WPPAREVPCK QRAKNASCRL LPPGPPARQH LLFRSLSQNT
     ATQGLLRGAM ALPPPPRGLW QAKDISLIVK AARRDGELLL SAQLDSGEKD TGVPRLGPHA
     PYILIYANDL AISEPNSVAV TLQRYDPFQA GDPEPGAAPN SSADPRVRRA TQATGPLQNN
     ELPGLDERPA QAPHAQHYHK HELWPNPLRA LKPRPGRKDR RKKGQDVFMA SSQVLDFDEK
     TMQKARKKQW DEPRVCSRRY LKVDFADIGW NEWIISPKSF DAYYCSGACE FPMPKMVRPS
     NHATIQSIVR AVGIVPGIPE PCCVPDKMSS LGVLFLDENR NVVLKVYPNM SVETCACR