ID EGLN_MOUSE Reviewed; 653 AA. AC Q63961; Q61520; Q8K100; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 29-MAY-2013, entry version 99. DE RecName: Full=Endoglin; DE AltName: Full=Cell surface MJ7/18 antigen; DE AltName: CD_antigen=CD105; DE Flags: Precursor; GN Name=Eng; Synonyms=Edg; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=8125301; DOI=10.1016/0378-1119(94)90808-7; RA Ge A.Z., Butcher E.C.; RT "Cloning and expression of a cDNA encoding mouse endoglin, an RT endothelial cell TGF-beta ligand."; RL Gene 138:201-206(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=CD-1; TISSUE=Placenta; RX PubMed=8194490; DOI=10.1210/en.134.6.2645; RA St Jacques S., Cymerman U., Pece N., Letarte M.; RT "Molecular characterization and in situ localization of murine RT endoglin reveal that it is a transforming growth factor-beta binding RT protein of endothelial and stromal cells."; RL Endocrinology 134:2645-2657(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PHOSPHORYLATION AT SER-641 AND SER-644. RX PubMed=20042635; DOI=10.1093/carcin/bgp327; RA Ray B.N., Lee N.Y., How T., Blobe G.C.; RT "ALK5 phosphorylation of the endoglin cytoplasmic domain regulates RT Smad1/5/8 signaling and endothelial cell migration."; RL Carcinogenesis 31:435-441(2010). CC -!- FUNCTION: Major glycoprotein of vascular endothelium. May play a CC critical role in the binding of endothelial cells to integrins CC and/or other RGD receptors (By similarity). CC -!- SUBUNIT: Homodimer that forms a heteromeric complex with the CC signaling receptors for transforming growth factor-beta: TGFBR1 CC and/or TGFBR2. It is able to bind TGF-beta 1, and 3 efficiently CC and TGF-beta 2 less efficiently. Interacts with TCTEX1D4. CC Interacts with ARRB2 (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- TISSUE SPECIFICITY: Endoglin is restricted to endothelial cells in CC all tissues except bone marrow and is also found in stromal cells CC within the connective tissue of intestine, stomach, heart, CC skeletal muscle, uterus, ovary, oviduct, testis and thymus. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S69407; AAB30196.1; -; mRNA. DR EMBL; X77952; CAA54917.1; -; mRNA. DR EMBL; AL772271; CAM16615.1; -; Genomic_DNA. DR EMBL; CH466542; EDL08562.1; -; Genomic_DNA. DR EMBL; BC029080; AAH29080.1; -; mRNA. DR IPI; IPI00323857; -. DR PIR; I48341; I48341. DR RefSeq; NP_031958.2; NM_007932.2. DR UniGene; Mm.225297; -. DR ProteinModelPortal; Q63961; -. DR SMR; Q63961; 445-557. DR MINT; MINT-4116867; -. DR PhosphoSite; Q63961; -. DR PaxDb; Q63961; -. DR PRIDE; Q63961; -. DR Ensembl; ENSMUST00000009705; ENSMUSP00000009705; ENSMUSG00000026814. DR GeneID; 13805; -. DR KEGG; mmu:13805; -. DR UCSC; uc008jgk.2; mouse. DR CTD; 2022; -. DR MGI; MGI:95392; Eng. DR eggNOG; NOG46276; -. DR GeneTree; ENSGT00530000063861; -. DR HOGENOM; HOG000112346; -. DR HOVERGEN; HBG005573; -. DR InParanoid; Q8K100; -. DR KO; K06526; -. DR OMA; SWLIDAN; -. DR OrthoDB; EOG4WWRJG; -. DR NextBio; 284580; -. DR ArrayExpress; Q63961; -. DR Bgee; Q63961; -. DR CleanEx; MM_ENG; -. DR Genevestigator; Q63961; -. DR GermOnline; ENSMUSG00000026814; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IEA:Compara. DR GO; GO:0072563; C:endothelial microparticle; IDA:BHF-UCL. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Compara. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:Compara. DR GO; GO:0005534; F:galactose binding; IEA:Compara. DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Compara. DR GO; GO:0050431; F:transforming growth factor beta binding; IDA:BHF-UCL. DR GO; GO:0005072; F:transforming growth factor beta receptor, cytoplasmic mediator activity; IEA:Compara. DR GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IEA:Compara. DR GO; GO:0048844; P:artery morphogenesis; IMP:BHF-UCL. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0060326; P:cell chemotaxis; IEA:Compara. DR GO; GO:0003273; P:cell migration involved in endocardial cushion formation; IMP:MGI. DR GO; GO:0022009; P:central nervous system vasculogenesis; IEA:Compara. DR GO; GO:0001300; P:chronological cell aging; IEP:BHF-UCL. DR GO; GO:0070483; P:detection of hypoxia; IEA:Compara. DR GO; GO:0022617; P:extracellular matrix disassembly; IEA:Compara. DR GO; GO:0001947; P:heart looping; IMP:BHF-UCL. DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Compara. DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Compara. DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IEA:Compara. DR GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IEA:Compara. DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; IEA:Compara. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara. DR GO; GO:0001569; P:patterning of blood vessels; IMP:BHF-UCL. DR GO; GO:0045766; P:positive regulation of angiogenesis; TAS:DFLAT. DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Compara. DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IEA:Compara. DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IEA:Compara. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara. DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; TAS:MGI. DR GO; GO:0048745; P:smooth muscle tissue development; IMP:BHF-UCL. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IC:BHF-UCL. DR GO; GO:0001570; P:vasculogenesis; IMP:BHF-UCL. DR GO; GO:0048845; P:venous blood vessel morphogenesis; IMP:BHF-UCL. DR GO; GO:0042060; P:wound healing; IEA:Compara. DR InterPro; IPR001507; ZP_dom. DR Pfam; PF00100; Zona_pellucida; 2. DR SMART; SM00241; ZP; 1. PE 1: Evidence at protein level; KW Cell adhesion; Complete proteome; Glycoprotein; Membrane; KW Phosphoprotein; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 26 Potential. FT CHAIN 27 653 Endoglin. FT /FTId=PRO_0000021157. FT TOPO_DOM 27 581 Extracellular (Potential). FT TRANSMEM 582 606 Helical; (Potential). FT TOPO_DOM 607 653 Cytoplasmic (Potential). FT COMPBIAS 336 574 Ser/Thr-rich. FT MOD_RES 641 641 Phosphoserine; by TGFBR1. FT MOD_RES 644 644 Phosphoserine; by TGFBR1. FT CARBOHYD 89 89 N-linked (GlcNAc...) (Potential). FT CARBOHYD 135 135 N-linked (GlcNAc...) (Potential). FT CARBOHYD 266 266 N-linked (GlcNAc...) (Potential). FT CARBOHYD 307 307 N-linked (GlcNAc...) (Potential). FT CARBOHYD 322 322 N-linked (GlcNAc...) (Potential). FT CONFLICT 94 94 Q -> R (in Ref. 2; CAA54917). FT CONFLICT 287 287 V -> D (in Ref. 1; AAB30196). FT CONFLICT 572 572 I -> V (in Ref. 2; CAA54917). SQ 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 //