ID   BMP10_RAT               Reviewed;         421 AA.
AC   Q4AEG6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Bone morphogenetic protein 10;
DE            Short=BMP-10;
DE   Flags: Precursor;
GN   Name=Bmp10 {ECO:0000312|EMBL:BAE16990.1, ECO:0000312|RGD:1562986};
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] {ECO:0000312|EMBL:BAE16990.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Fischer 344/DuCrj {ECO:0000312|EMBL:BAE16989.1}, and LEC/Crj
RC   {ECO:0000312|EMBL:BAE16990.1};
RX   PubMed=15978772; DOI=10.1016/j.ygeno.2005.05.007;
RA   Tsuji A.B., Sugyo A., Ogiu T., Sagara M., Kimura T., Ishikawa A., Sudo H.,
RA   Ohtsuki M., Aburatani H., Imai T., Harada Y.N.;
RT   "Fine mapping of radiation susceptibility and gene expression analysis of
RT   LEC congenic rat lines.";
RL   Genomics 86:271-279(2005).
CC   -!- FUNCTION: Required for maintaining the proliferative activity of
CC       embryonic cardiomyocytes by preventing premature activation of the
CC       negative cell cycle regulator CDKN1C/p57KIP and maintaining the
CC       required expression levels of cardiogenic factors such as MEF2C and
CC       NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6,
CC       leading to activation of SMAD1, SMAD5 and SMAD8 transcription factors.
CC       Inhibits endothelial cell migration and growth. May reduce cell
CC       migration and cell matrix adhesion in breast cancer cell lines.
CC       {ECO:0000250|UniProtKB:O95393}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC       FBN1 (via N-terminal domain) and FBN2. Interacts with ENG (By
CC       similarity). {ECO:0000250|UniProtKB:O95393,
CC       ECO:0000250|UniProtKB:P12643}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P12643}.
CC   -!- MISCELLANEOUS: Does not appear to contribute to radiation
CC       susceptibility in the LEC strain. {ECO:0000269|PubMed:15978772}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000255}.
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DR   EMBL; AB158417; BAE16989.1; -; mRNA.
DR   EMBL; AB158418; BAE16990.1; -; mRNA.
DR   RefSeq; NP_001026994.1; NM_001031824.1.
DR   AlphaFoldDB; Q4AEG6; -.
DR   SMR; Q4AEG6; -.
DR   STRING; 10116.ENSRNOP00000012365; -.
DR   GlyCosmos; Q4AEG6; 2 sites, No reported glycans.
DR   GlyGen; Q4AEG6; 2 sites.
DR   PhosphoSitePlus; Q4AEG6; -.
DR   PaxDb; 10116-ENSRNOP00000012365; -.
DR   Ensembl; ENSRNOT00000012365.4; ENSRNOP00000012365.3; ENSRNOG00000009316.4.
DR   Ensembl; ENSRNOT00055022127; ENSRNOP00055017968; ENSRNOG00055012919.
DR   Ensembl; ENSRNOT00060053300; ENSRNOP00060044316; ENSRNOG00060030679.
DR   Ensembl; ENSRNOT00065024741; ENSRNOP00065019326; ENSRNOG00065014959.
DR   GeneID; 500245; -.
DR   KEGG; rno:500245; -.
DR   UCSC; RGD:1562986; rat.
DR   AGR; RGD:1562986; -.
DR   CTD; 27302; -.
DR   RGD; 1562986; Bmp10.
DR   eggNOG; KOG3900; Eukaryota.
DR   GeneTree; ENSGT00940000156279; -.
DR   HOGENOM; CLU_020515_2_0_1; -.
DR   InParanoid; Q4AEG6; -.
DR   OMA; SAQNKHD; -.
DR   OrthoDB; 2912454at2759; -.
DR   PhylomeDB; Q4AEG6; -.
DR   TreeFam; TF316134; -.
DR   Reactome; R-RNO-201451; Signaling by BMP.
DR   Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR   PRO; PR:Q4AEG6; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0030018; C:Z disc; ISO:RGD.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; ISO:RGD.
DR   GO; GO:0005179; F:hormone activity; ISO:RGD.
DR   GO; GO:0033612; F:receptor serine/threonine kinase binding; ISO:RGD.
DR   GO; GO:0031433; F:telethonin binding; ISO:RGD.
DR   GO; GO:0032924; P:activin receptor signaling pathway; ISO:RGD.
DR   GO; GO:0007512; P:adult heart development; ISO:RGD.
DR   GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; ISO:RGD.
DR   GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR   GO; GO:0060038; P:cardiac muscle cell proliferation; ISO:RGD.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007507; P:heart development; ISO:RGD.
DR   GO; GO:0060347; P:heart trabecula formation; ISO:RGD.
DR   GO; GO:0001822; P:kidney development; ISO:RGD.
DR   GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISO:RGD.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR   GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:RGD.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISO:RGD.
DR   GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
DR   GO; GO:0061036; P:positive regulation of cartilage development; ISO:RGD.
DR   GO; GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0060298; P:positive regulation of sarcomere organization; ISO:RGD.
DR   GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:RGD.
DR   GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:RGD.
DR   GO; GO:1903242; P:regulation of cardiac muscle hypertrophy in response to stress; ISO:RGD.
DR   GO; GO:0045214; P:sarcomere organization; IMP:BHF-UCL.
DR   GO; GO:0055015; P:ventricular cardiac muscle cell development; ISO:RGD.
DR   GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:RGD.
DR   CDD; cd19401; TGF_beta_BMP10; 1.
DR   Gene3D; 2.60.120.970; -; 1.
DR   Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR001839; TGF-b_C.
DR   InterPro; IPR001111; TGF-b_propeptide.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848:SF39; BONE MORPHOGENETIC PROTEIN 10; 1.
DR   PANTHER; PTHR11848; TGF-BETA FAMILY; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   Pfam; PF00688; TGFb_propeptide; 1.
DR   PRINTS; PR00669; INHIBINA.
DR   SMART; SM00204; TGFB; 1.
DR   SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR   PROSITE; PS00250; TGF_BETA_1; 1.
DR   PROSITE; PS51362; TGF_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cleavage on pair of basic residues; Cytokine;
KW   Developmental protein; Disulfide bond; Glycoprotein; Growth factor;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..313
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310575"
FT   CHAIN           314..421
FT                   /note="Bone morphogenetic protein 10"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000310576"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        320..386
FT                   /evidence="ECO:0000250|UniProtKB:P12643"
FT   DISULFID        349..418
FT                   /evidence="ECO:0000250|UniProtKB:P12643"
FT   DISULFID        353..420
FT                   /evidence="ECO:0000250|UniProtKB:P12643"
FT   DISULFID        385
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P12643"
SQ   SEQUENCE   421 AA;  47767 MW;  94E1496B7BEDFD36 CRC64;
     MGSLVLPLSA VFCLVARLAS GSPIMGLEQS PLEEDMPFFD DIFTEQDGID FNTLLQSMKD
     EFLKTLNLSD IPPQDTGRVD PPEYMLELYN KFATDRTSMP SANIIRSFKN EDLFSQPVSF
     NGIRKYPLLF NVSIPHHEEV VMAELRLYTL VQRDRLMYDG VDRKIIIFEV LESADGSEDE
     RSMLVLVSTE IYGTNSEWET FDITDATRRW QKSGPSTHQL EIHIESRQNQ AEDTGRGQLE
     IDMSAQNKHD PLLVVFSDDQ SGDKEQKEEL NELISHEQDL DLGTDGFFGG PDEEALLQMR
     SNMIDDSTAR IRRNAKGNYC KKTPLYIDFK EIGWDSWIIA PPGYEAYECR GVCNYPLAEH
     LTPTKHAIIQ ALVHLKNSQK ASKACCVPTK LDPISILYLD KGVVTYKFKY EGMAVSECGC
     R
//