GDF10_HUMAN
ID GDF10_HUMAN Reviewed; 478 AA.
AC P55107; Q5VSQ8; Q9UCX6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
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|HGNC:HGNC:4215}; Synonyms=BMP3B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Femur;
RX PubMed=8670277; DOI=10.1006/bbrc.1996.0889;
RA Hino J., Takao M., Takeshita N., Konno Y., Nishizawa T., Matsuo H.,
RA Kangawa K.;
RT "cDNA cloning and genomic structure of human bone morphogenetic protein-3B
RT (BMP-3b).";
RL Biochem. Biophys. Res. Commun. 223:304-310(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE OF 360-478.
RC 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).
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: Expressed in femur, brain, lung, skeletal muscle,
CC pancreas and testis. {ECO:0000269|PubMed:8670277}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; D49493; BAA08453.1; -; Genomic_DNA.
DR EMBL; D49492; BAA08452.1; -; mRNA.
DR EMBL; AL731561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471251; EAW50661.1; -; Genomic_DNA.
DR EMBL; L42113; AAL77527.1; -; mRNA.
DR CCDS; CCDS73117.1; -.
DR PIR; JC4838; JC4838.
DR RefSeq; NP_004953.1; NM_004962.4.
DR AlphaFoldDB; P55107; -.
DR SMR; P55107; -.
DR BioGRID; 108931; 24.
DR IntAct; P55107; 9.
DR STRING; 9606.ENSP00000464145; -.
DR GlyGen; P55107; 4 sites.
DR iPTMnet; P55107; -.
DR PhosphoSitePlus; P55107; -.
DR BioMuta; GDF10; -.
DR DMDM; 1705471; -.
DR MassIVE; P55107; -.
DR PaxDb; P55107; -.
DR PeptideAtlas; P55107; -.
DR PRIDE; P55107; -.
DR ProteomicsDB; 56792; -.
DR Antibodypedia; 73579; 283 antibodies from 28 providers.
DR DNASU; 2662; -.
DR Ensembl; ENST00000580279.2; ENSP00000464145.1; ENSG00000266524.3.
DR GeneID; 2662; -.
DR KEGG; hsa:2662; -.
DR MANE-Select; ENST00000580279.2; ENSP00000464145.1; NM_004962.5; NP_004953.1.
DR UCSC; uc001jfb.4; human.
DR CTD; 2662; -.
DR DisGeNET; 2662; -.
DR GeneCards; GDF10; -.
DR HGNC; HGNC:4215; GDF10.
DR HPA; ENSG00000266524; Tissue enhanced (lung, retina).
DR MIM; 601361; gene.
DR neXtProt; NX_P55107; -.
DR OpenTargets; ENSG00000266524; -.
DR PharmGKB; PA28630; -.
DR VEuPathDB; HostDB:ENSG00000266524; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000157214; -.
DR HOGENOM; CLU_020515_10_0_1; -.
DR InParanoid; P55107; -.
DR OMA; FHFYADK; -.
DR OrthoDB; 1002140at2759; -.
DR PhylomeDB; P55107; -.
DR TreeFam; TF316134; -.
DR PathwayCommons; P55107; -.
DR SignaLink; P55107; -.
DR BioGRID-ORCS; 2662; 17 hits in 1061 CRISPR screens.
DR ChiTaRS; GDF10; human.
DR GeneWiki; GDF10; -.
DR GenomeRNAi; 2662; -.
DR Pharos; P55107; Tbio.
DR PRO; PR:P55107; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P55107; protein.
DR Bgee; ENSG00000266524; Expressed in right lung and 114 other tissues.
DR Genevisible; P55107; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
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; TAS:ProtInc.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0042698; P:ovulation cycle; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0030278; P:regulation of ossification; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:ProtInc.
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_0000033844"
FT CHAIN 369..478
FT /note="Growth/differentiation factor 10"
FT /id="PRO_0000033845"
FT REGION 266..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
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; 53122 MW; 80AE0FA4C50B23A9 CRC64;
MAHVPARTSP GPGPQLLLLL LPLFLLLLRD VAGSHRAPAW SALPAAADGL QGDRDLQRHP
GDAAATLGPS AQDMVAVHMH RLYEKYSRQG ARPGGGNTVR SFRARLEVVD QKAVYFFNLT
SMQDSEMILT ATFHFYSEPP RWPRALEVLC KPRAKNASGR PLPLGPPTRQ HLLFRSLSQN
TATQGLLRGA MALAPPPRGL WQAKDISPIV KAARRDGELL LSAQLDSEER DPGVPRPSPY
APYILVYAND LAISEPNSVA VTLQRYDPFP AGDPEPRAAP NNSADPRVRR AAQATGPLQD
NELPGLDERP PRAHAQHFHK HQLWPSPFRA LKPRPGRKDR RKKGQEVFMA ASQVLDFDEK
TMQKARRKQW DEPRVCSRRY LKVDFADIGW NEWIISPKSF DAYYCAGACE FPMPKIVRPS
NHATIQSIVR AVGIIPGIPE PCCVPDKMNS LGVLFLDENR NVVLKVYPNM SVDTCACR
