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Bone morphogenetic protein 10 (BMP-10)

 BMP10_HUMAN             Reviewed;         424 AA.
O95393; Q53R17; Q6NTE0;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
27-SEP-2017, entry version 144.
RecName: Full=Bone morphogenetic protein 10;
Short=BMP-10;
Flags: Precursor;
Name=BMP10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Celeste A.J.;
"Homo sapiens bone morphogenetic protein 10 (BMP-10) mRNA.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION.
PubMed=16049014; DOI=10.1074/jbc.M504629200;
Mazerbourg S., Sangkuhl K., Luo C.-W., Sudo S., Klein C.,
Hsueh A.J.W.;
"Identification of receptors and signaling pathways for orphan bone
morphogenetic protein/growth differentiation factor ligands based on
genomic analyses.";
J. Biol. Chem. 280:32122-32132(2005).
[5]
FUNCTION.
PubMed=17068149; DOI=10.1182/blood-2006-07-034124;
David L., Mallet C., Mazerbourg S., Feige J.-J., Bailly S.;
"Identification of BMP9 and BMP10 as functional activators of the
orphan activin receptor-like kinase 1 (ALK1) in endothelial cells.";
Blood 109:1953-1961(2007).
[6]
INTERACTION WITH FBN1 AND FBN2.
PubMed=18339631; DOI=10.1074/jbc.M707820200;
Sengle G., Charbonneau N.L., Ono R.N., Sasaki T., Alvarez J.,
Keene D.R., Baechinger H.P., Sakai L.Y.;
"Targeting of bone morphogenetic protein growth factor complexes to
fibrillin.";
J. Biol. Chem. 283:13874-13888(2008).
[7]
INTERACTION WITH ENG.
PubMed=21737454; DOI=10.1074/jbc.M111.260133;
Castonguay R., Werner E.D., Matthews R.G., Presman E., Mulivor A.W.,
Solban N., Sako D., Pearsall R.S., Underwood K.W., Seehra J.,
Kumar R., Grinberg A.V.;
"Soluble endoglin specifically binds bone morphogenetic proteins 9 and
10 via its orphan domain, inhibits blood vessel formation, and
suppresses tumor growth.";
J. Biol. Chem. 286:30034-30046(2011).
[8]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=20608934; DOI=10.1111/j.1349-7006.2010.01648.x;
Ye L., Bokobza S., Li J., Moazzam M., Chen J., Mansel R.E.,
Jiang W.G.;
"Bone morphogenetic protein-10 (BMP-10) inhibits aggressiveness of
breast cancer cells and correlates with poor prognosis in breast
cancer.";
Cancer Sci. 101:2137-2144(2010).
-!- FUNCTION: Required for maintaining the proliferative activity of
embryonic cardiomyocytes by preventing premature activation of the
negative cell cycle regulator CDKN1C/p57KIP and maintaining the
required expression levels of cardiogenic factors such as MEF2C
and NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and
BMPR1B/ALK6, leading to activation of SMAD1, SMAD5 and SMAD8
transcription factors. Inhibits endothelial cell migration and
growth. May reduce cell migration and cell matrix adhesion in
breast cancer cell lines. {ECO:0000269|PubMed:16049014,
ECO:0000269|PubMed:17068149, ECO:0000269|PubMed:20608934}.
-!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts
with FBN1 (via N-terminal domain) and FBN2 (PubMed:18339631).
Interacts with ENG (PubMed:21737454).
{ECO:0000250|UniProtKB:P12643, ECO:0000269|PubMed:18339631,
ECO:0000269|PubMed:21737454}.
-!- INTERACTION:
P02730:SLC4A1; NbExp=4; IntAct=EBI-3922513, EBI-7576138;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in mammary epithelia (at protein
level). {ECO:0000269|PubMed:20608934}.
-!- INDUCTION: Down-regulated in some breast cancer subtypes and
breast cancer cell lines. {ECO:0000269|PubMed:20608934}.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Bone morphogenetic protein 10
entry;
URL="https://en.wikipedia.org/wiki/Bone_morphogenetic_protein_10";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF101441; AAC77462.1; -; mRNA.
EMBL; AC097495; AAY15075.1; -; Genomic_DNA.
EMBL; BC069080; AAH69080.1; -; mRNA.
EMBL; BC101734; AAI01735.1; -; mRNA.
EMBL; BC105063; AAI05064.1; -; mRNA.
CCDS; CCDS1890.1; -.
RefSeq; NP_055297.1; NM_014482.2.
UniGene; Hs.158317; -.
ProteinModelPortal; O95393; -.
BioGrid; 118125; 4.
IntAct; O95393; 13.
STRING; 9606.ENSP00000295379; -.
ChEMBL; CHEMBL3713453; -.
iPTMnet; O95393; -.
PhosphoSitePlus; O95393; -.
BioMuta; BMP10; -.
MaxQB; O95393; -.
PaxDb; O95393; -.
PeptideAtlas; O95393; -.
PRIDE; O95393; -.
DNASU; 27302; -.
Ensembl; ENST00000295379; ENSP00000295379; ENSG00000163217.
GeneID; 27302; -.
KEGG; hsa:27302; -.
UCSC; uc002sez.1; human.
CTD; 27302; -.
DisGeNET; 27302; -.
EuPathDB; HostDB:ENSG00000163217.1; -.
GeneCards; BMP10; -.
HGNC; HGNC:20869; BMP10.
MIM; 608748; gene.
neXtProt; NX_O95393; -.
OpenTargets; ENSG00000163217; -.
PharmGKB; PA134953092; -.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
GeneTree; ENSGT00760000118883; -.
HOGENOM; HOG000249477; -.
HOVERGEN; HBG106648; -.
InParanoid; O95393; -.
KO; K05503; -.
OMA; NVSIPHH; -.
OrthoDB; EOG091G075U; -.
PhylomeDB; O95393; -.
TreeFam; TF316134; -.
Reactome; R-HSA-201451; Signaling by BMP.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
SIGNOR; O95393; -.
GeneWiki; Bone_morphogenetic_protein_10; -.
GenomeRNAi; 27302; -.
PRO; PR:O95393; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163217; -.
CleanEx; HS_BMP10; -.
Genevisible; O95393; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005179; F:hormone activity; IDA:BHF-UCL.
GO; GO:0033612; F:receptor serine/threonine kinase binding; IDA:UniProtKB.
GO; GO:0031433; F:telethonin binding; IPI:BHF-UCL.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0032924; P:activin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007512; P:adult heart development; ISS:BHF-UCL.
GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0060038; P:cardiac muscle cell proliferation; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0060347; P:heart trabecula formation; ISS:BHF-UCL.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISS:BHF-UCL.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:BHF-UCL.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
GO; GO:0061036; P:positive regulation of cartilage development; IEA:Ensembl.
GO; GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; ISS:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0060298; P:positive regulation of sarcomere organization; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:1903242; P:regulation of cardiac muscle hypertrophy in response to stress; IDA:BHF-UCL.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0045214; P:sarcomere organization; ISS:BHF-UCL.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0055015; P:ventricular cardiac muscle cell development; ISS:BHF-UCL.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
Cell adhesion; Cleavage on pair of basic residues; Complete proteome;
Cytokine; Developmental protein; Disulfide bond; Glycoprotein;
Growth factor; Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 316 {ECO:0000255}.
/FTId=PRO_0000033888.
CHAIN 317 424 Bone morphogenetic protein 10.
/FTId=PRO_0000033889.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 131 131 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 323 389 {ECO:0000250}.
DISULFID 352 421 {ECO:0000250}.
DISULFID 356 423 {ECO:0000250}.
DISULFID 388 388 Interchain. {ECO:0000250}.
VARIANT 200 200 T -> S (in dbSNP:rs2231342).
/FTId=VAR_052572.
VARIANT 250 250 N -> K (in dbSNP:rs2231345).
/FTId=VAR_052573.
CONFLICT 143 143 A -> T (in Ref. 3; AAH69080).
{ECO:0000305}.
SEQUENCE 424 AA; 48047 MW; 3FDB3B7221BB2254 CRC64;
MGSLVLTLCA LFCLAAYLVS GSPIMNLEQS PLEEDMSLFG DVFSEQDGVD FNTLLQSMKD
EFLKTLNLSD IPTQDSAKVD PPEYMLELYN KFATDRTSMP SANIIRSFKN EDLFSQPVSF
NGLRKYPLLF NVSIPHHEEV IMAELRLYTL VQRDRMIYDG VDRKITIFEV LESKGDNEGE
RNMLVLVSGE IYGTNSEWET FDVTDAIRRW QKSGSSTHQL EVHIESKHDE AEDASSGRLE
IDTSAQNKHN PLLIVFSDDQ SSDKERKEEL NEMISHEQLP ELDNLGLDSF SSGPGEEALL
QMRSNIIYDS TARIRRNAKG NYCKRTPLYI DFKEIGWDSW IIAPPGYEAY ECRGVCNYPL
AEHLTPTKHA IIQALVHLKN SQKASKACCV PTKLEPISIL YLDKGVVTYK FKYEGMAVSE
CGCR


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