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Endoglin (Cell surface MJ7/18 antigen) (CD antigen CD105)

 EGLN_MOUSE              Reviewed;         653 AA.
Q63961; Q61520; Q8K100;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
25-OCT-2017, entry version 135.
RecName: Full=Endoglin;
AltName: Full=Cell surface MJ7/18 antigen;
AltName: CD_antigen=CD105 {ECO:0000303|PubMed:10625534};
Flags: Precursor;
Name=Eng; Synonyms=Edg;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=8125301; DOI=10.1016/0378-1119(94)90808-7;
Ge A.Z., Butcher E.C.;
"Cloning and expression of a cDNA encoding mouse endoglin, an
endothelial cell TGF-beta ligand.";
Gene 138:201-206(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBUNIT, AND
INTERACTION WITH TGFB1.
STRAIN=CD-1; TISSUE=Placenta;
PubMed=8194490; DOI=10.1210/endo.134.6.8194490;
St Jacques S., Cymerman U., Pece N., Letarte M.;
"Molecular characterization and in situ localization of murine
endoglin reveal that it is a transforming growth factor-beta binding
protein of endothelial and stromal cells.";
Endocrinology 134:2645-2657(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Salivary gland;
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).
[6]
FUNCTION.
PubMed=17540773; DOI=10.1074/jbc.M700176200;
Lee N.Y., Blobe G.C.;
"The interaction of endoglin with beta-arrestin2 regulates
transforming growth factor-beta-mediated ERK activation and migration
in endothelial cells.";
J. Biol. Chem. 282:21507-21517(2007).
[7]
FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
SPECIFICITY.
PubMed=10625534; DOI=10.1006/dbio.1999.9534;
Arthur H.M., Ure J., Smith A.J., Renforth G., Wilson D.I., Torsney E.,
Charlton R., Parums D.V., Jowett T., Marchuk D.A., Burn J.,
Diamond A.G.;
"Endoglin, an ancillary TGFbeta receptor, is required for
extraembryonic angiogenesis and plays a key role in heart
development.";
Dev. Biol. 217:42-53(2000).
[8]
PHOSPHORYLATION AT SER-641 AND SER-644.
PubMed=20042635; DOI=10.1093/carcin/bgp327;
Ray B.N., Lee N.Y., How T., Blobe G.C.;
"ALK5 phosphorylation of the endoglin cytoplasmic domain regulates
Smad1/5/8 signaling and endothelial cell migration.";
Carcinogenesis 31:435-441(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
FUNCTION, AND INTERACTION WITH GDF2 AND BMP10.
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).
[11]
FUNCTION.
PubMed=23300529; DOI=10.1371/journal.pone.0050920;
Nolan-Stevaux O., Zhong W., Culp S., Shaffer K., Hoover J.,
Wickramasinghe D., Ruefli-Brasse A.;
"Endoglin requirement for BMP9 signaling in endothelial cells reveals
new mechanism of action for selective anti-endoglin antibodies.";
PLoS ONE 7:E50920-E50920(2012).
-!- FUNCTION: Vascular endothelium glycoprotein that plays an
important role in the regulation of angiogenesis
(PubMed:10625534). Required for normal structure and integrity of
adult vasculature (By similarity). Regulates the migration of
vascular endothelial cells (PubMed:17540773). Required for normal
extraembryonic angiogenesis and for embryonic heart development
(PubMed:10625534). May play a role in the binding of endothelial
cells to integrins. Acts as TGF-beta coreceptor and is involved in
the TGF-beta/BMP signaling cascade that ultimately leads to the
activation of SMAD transcription factors (PubMed:23300529).
Required for GDF2/BMP9 signaling through SMAD1 in endothelial
cells and modulates TGFB1 signaling through SMAD3 (By similarity).
{ECO:0000250|UniProtKB:P17813, ECO:0000269|PubMed:10625534,
ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:23300529}.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:8194490). Forms a
heteromeric complex with the signaling receptors for transforming
growth factor-beta: TGFBR1 and/or TGFBR2. Interacts with TGFB1
(PubMed:8194490). It is able to bind TGFB1 and TGFB2 with high
affinity, but not TGFB3. Interacts with GDF2, forming a
heterotetramer with a 2:2 stoichiometry. Interacts with ACVRL1.
Can form a heteromeric complex with GDF2 and ACVRL1. Interacts
with BMP10. Interacts with TCTEX1D4. Interacts with ARRB2.
{ECO:0000250|UniProtKB:P17813, ECO:0000269|PubMed:8194490}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8125301};
Single-pass type I membrane protein {ECO:0000305|PubMed:8125301}.
-!- TISSUE SPECIFICITY: Detected on blood vessels (at protein level)
(PubMed:8194490). Detected on adult pulmonary artery, capillaries
supporting the heart muscle and lung alveolar capillary
endothelial cells (PubMed:10625534). Endoglin is restricted to
endothelial cells in all tissues except bone marrow and is also
found in stromal cells within the connective tissue of intestine,
stomach, heart, skeletal muscle, uterus, ovary, oviduct, testis
and thymus (PubMed:8194490). {ECO:0000269|PubMed:8194490}.
-!- DEVELOPMENTAL STAGE: Detected in embryo (at protein level).
Detected in endothelium from yolk sac vessels.
{ECO:0000269|PubMed:10625534}.
-!- DOMAIN: The ZP domain mediates dimerization.
{ECO:0000250|UniProtKB:P17813}.
-!- DOMAIN: The N-terminal OR region is composed of two intertwined
domains (OR1 and OR2) with a common, novel fold. Each contains 12
beta-strands that form a parallel beta-helix-like structure, plus
a single alpha-helix. The OR1 region mediates interaction with
GDF2. {ECO:0000250|UniProtKB:P17813}.
-!- DISRUPTION PHENOTYPE: Full embryonic lethality at about 10.5 dpc.
At 9.5 dpc, embryos display abnormal yolk sac vasculature and yolk
sac anemia. Mutant embryos are also anemic, probably due to
defective hematopoiesis in the yolk sac. In contrast, the
embryonic vasculature appears grossly normal in most cases, but
heart development is abnormal, and nearly all mutant embryos had
enlarged ventricles and dilated outflow tracts. Besides, many had
abnormal cardiac looping and displayed pericardial effusion.
Heterozygous mice have occasionally abnormally convoluted and
dilated blood vessels with disorganized smooth muscle cells
surrounding them; these blood vessels are very fragile and rupture
easily. {ECO:0000269|PubMed:10625534}.
-!- MISCELLANEOUS: Lacks a RGD motif, contrary to the human protein.
{ECO:0000305}.
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EMBL; S69407; AAB30196.1; -; mRNA.
EMBL; X77952; CAA54917.1; -; mRNA.
EMBL; AL772271; CAM16615.1; -; Genomic_DNA.
EMBL; CH466542; EDL08562.1; -; Genomic_DNA.
EMBL; BC029080; AAH29080.1; -; mRNA.
CCDS; CCDS15925.1; -.
PIR; I48341; I48341.
RefSeq; NP_031958.2; NM_007932.2.
UniGene; Mm.225297; -.
ProteinModelPortal; Q63961; -.
SMR; Q63961; -.
DIP; DIP-47636N; -.
IntAct; Q63961; 7.
MINT; MINT-4116867; -.
STRING; 10090.ENSMUSP00000009705; -.
iPTMnet; Q63961; -.
PhosphoSitePlus; Q63961; -.
EPD; Q63961; -.
MaxQB; Q63961; -.
PaxDb; Q63961; -.
PRIDE; Q63961; -.
Ensembl; ENSMUST00000009705; ENSMUSP00000009705; ENSMUSG00000026814.
GeneID; 13805; -.
KEGG; mmu:13805; -.
UCSC; uc008jgk.2; mouse.
CTD; 2022; -.
MGI; MGI:95392; Eng.
eggNOG; ENOG410IQ57; Eukaryota.
eggNOG; ENOG410YK9H; LUCA.
GeneTree; ENSGT00530000063861; -.
HOGENOM; HOG000112346; -.
HOVERGEN; HBG005573; -.
InParanoid; Q63961; -.
KO; K06526; -.
OMA; DANHNMQ; -.
OrthoDB; EOG091G030O; -.
TreeFam; TF337375; -.
PRO; PR:Q63961; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026814; -.
CleanEx; MM_ENG; -.
ExpressionAtlas; Q63961; baseline and differential.
Genevisible; Q63961; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0072563; C:endothelial microparticle; IDA:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0036122; F:BMP binding; IEA:Ensembl.
GO; GO:0005534; F:galactose binding; ISO:MGI.
GO; GO:0005539; F:glycosaminoglycan binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0050431; F:transforming growth factor beta binding; IDA:BHF-UCL.
GO; GO:0005072; F:transforming growth factor beta receptor, cytoplasmic mediator activity; ISO:MGI.
GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; ISO:MGI.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISO:MGI.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0048844; P:artery morphogenesis; IMP:BHF-UCL.
GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
GO; GO:1905222; P:atrioventricular canal morphogenesis; IMP:BHF-UCL.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:BHF-UCL.
GO; GO:0003209; P:cardiac atrium morphogenesis; IMP:BHF-UCL.
GO; GO:0003208; P:cardiac ventricle morphogenesis; IMP:BHF-UCL.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
GO; GO:0016477; P:cell migration; ISO:MGI.
GO; GO:0003273; P:cell migration involved in endocardial cushion formation; IMP:MGI.
GO; GO:0048870; P:cell motility; ISO:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0022009; P:central nervous system vasculogenesis; ISO:MGI.
GO; GO:0001300; P:chronological cell aging; IEP:BHF-UCL.
GO; GO:0070483; P:detection of hypoxia; ISO:MGI.
GO; GO:0035912; P:dorsal aorta morphogenesis; IMP:BHF-UCL.
GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:BHF-UCL.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
GO; GO:0070278; P:extracellular matrix constituent secretion; IEA:Ensembl.
GO; GO:0022617; P:extracellular matrix disassembly; ISO:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISO:MGI.
GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0003148; P:outflow tract septum morphogenesis; IGI:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IGI:MGI.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:MGI.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:1905065; P:positive regulation of vascular smooth muscle cell differentiation; IMP:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0031960; P:response to corticosteroid; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; ISO:MGI.
GO; GO:0048745; P:smooth muscle tissue development; IMP:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IC:BHF-UCL.
GO; GO:0097084; P:vascular smooth muscle cell development; IMP:BHF-UCL.
GO; GO:0001570; P:vasculogenesis; IMP:BHF-UCL.
GO; GO:0048845; P:venous blood vessel morphogenesis; IMP:BHF-UCL.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
GO; GO:0042060; P:wound healing; ISO:MGI.
InterPro; IPR001507; ZP_dom.
Pfam; PF00100; Zona_pellucida; 1.
1: Evidence at protein level;
Angiogenesis; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 653 Endoglin.
/FTId=PRO_0000021157.
TOPO_DOM 27 581 Extracellular. {ECO:0000255}.
TRANSMEM 582 606 Helical. {ECO:0000255}.
TOPO_DOM 607 653 Cytoplasmic. {ECO:0000255}.
DOMAIN 363 510 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375}.
REGION 27 337 Required for interaction with GDF2.
{ECO:0000250|UniProtKB:P17813}.
REGION 27 47 OR1, N-terminal part.
{ECO:0000250|UniProtKB:P17813}.
REGION 48 201 OR2. {ECO:0000250|UniProtKB:P17813}.
REGION 202 330 OR1, C-terminal part.
{ECO:0000250|UniProtKB:P17813}.
REGION 270 282 Essential for interaction with GDF2.
{ECO:0000250|UniProtKB:P17813}.
COMPBIAS 336 574 Ser/Thr-rich.
MOD_RES 641 641 Phosphoserine; by TGFBR1.
{ECO:0000269|PubMed:20042635}.
MOD_RES 644 644 Phosphoserine; by TGFBR1.
{ECO:0000269|PubMed:20042635}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 31 209 {ECO:0000250|UniProtKB:P17813}.
DISULFID 54 184 {ECO:0000250|UniProtKB:P17813}.
DISULFID 244 330 {ECO:0000250|UniProtKB:P17813}.
DISULFID 350 382 {ECO:0000250|UniProtKB:P17813}.
DISULFID 363 442 {ECO:0000250|UniProtKB:P17813}.
DISULFID 394 412 {ECO:0000250|UniProtKB:P17813}.
DISULFID 493 549 {ECO:0000250|UniProtKB:P17813}.
DISULFID 516 516 Interchain.
{ECO:0000250|UniProtKB:P17813}.
CONFLICT 94 94 Q -> R (in Ref. 2; CAA54917).
{ECO:0000305}.
CONFLICT 287 287 V -> D (in Ref. 1; AAB30196).
{ECO:0000305}.
CONFLICT 572 572 I -> V (in Ref. 2; CAA54917).
{ECO:0000305}.
SEQUENCE 653 AA; 70021 MW; AD9DD2F823FB06A1 CRC64;
MDRGVLPLPI TLLFVIYSFV PTTGLAERVG CDLQPVDPTR GEVTFTTSQV SEGCVAQAAN
AVREVHVLFL DFPGMLSHLE LTLQASKQNG TETQEVFLVL VSNKNVFVKF QAPEIPLHLA
YDSSLVIFQG QPRVNITVLP SLTSRKQILD WAATKGAITS IAALDDPQSI VLQLGQDPKA
PFLCLPEAHK DMGATLEWQP RAQTPVQSCR LEGVSGHKEA YILRILPGSE AGPRTVTVMM
ELSCTSGDAI LILHGPPYVS WFIDINHSMQ ILTTGEYSVK IFPGSKVKGV ELPDTPQGLI
AEARKLNASI VTSFVELPLV SNVSLRASSC GGVFQTTPAP VVTTPPKDTC SPVLLMSLIQ
PKCGNQVMTL ALNKKHVQTL QCTITGLTFW DSSCQAEDTD DHLVLSSAYS SCGMKVTAHV
VSNEVIISFP SGSPPLRKKV QCIDMDSLSF QLGLYLSPHF LQASNTIELG QQAFVQVSVS
PLTSEVTVQL DSCHLDLGPE GDMVELIQSR TAKGSCVTLL SPSPEGDPRF SFLLRVYMVP
TPTAGTLSCN LALRPSTLSQ EVYKTVSMRL NIVSPDLSGK GLVLPSVLGI TFGAFLIGAL
LTAALWYIYS HTRGPSKREP VVAVAAPASS ESSSTNHSIG STQSTPCSTS SMA


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