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Endoglin

 EGLN_DANRE              Reviewed;         559 AA.
A0A1Z2R986; A0A286NMM4; A0A286NMM5; A0A286NMM6;
20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
27-SEP-2017, sequence version 1.
22-APR-2020, entry version 9.
RecName: Full=Endoglin {ECO:0000303|PubMed:28530658};
Flags: Precursor;
Name=eng {ECO:0000303|PubMed:28530658};
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955 {ECO:0000312|EMBL:ASA40290.1};
[1] {ECO:0000312|EMBL:ASA40290.1}
NUCLEOTIDE SEQUENCE [MRNA].
Han R., Zhang D., Yang J.;
"Tempo-spatial expression of endoglin in zebrafish.";
Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000312|EMBL:DAA80500.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=28530658; DOI=10.1038/ncb3528;
Sugden W.W., Meissner R., Aegerter-Wilmsen T., Tsaryk R., Leonard E.V.,
Bussmann J., Hamm M.J., Herzog W., Jin Y., Jakobsson L., Denz C.,
Siekmann A.F.;
"Endoglin controls blood vessel diameter through endothelial cell shape
changes in response to haemodynamic cues.";
Nat. Cell Biol. 19:653-665(2017).
-!- FUNCTION: Vascular endothelium glycoprotein that plays an important
role in the regulation of angiogenesis. Required for normal structure
and integrity of adult vasculature. Important for endothelial cell
shape changes in response to blood flow, which drive vascular
remodeling and establishment of normal vascular morphology during
angiogenesis. {ECO:0000269|PubMed:28530658}.
-!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P17813}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17813};
Single-pass type I membrane protein {ECO:0000255}.
-!- DEVELOPMENTAL STAGE: Detected in vascular tissue at 36-72 hours post-
fertilization, where it localizes to endothelial cells.
{ECO:0000269|PubMed:28530658}.
-!- DISRUPTION PHENOTYPE: Viable, with survival to adult stages. Brain
tissue shows widespread vascular malformations with localized widening
of blood vessels. During embryogenesis, blood vessel connectivity
between the dorsal aorta (DA), intersegmental vessels (ISVs) and
posterior cardinal vein (PCV) appears normal at 72 hours post-
fertilization (hpf). However, blood flow through ISVs is significantly
reduced. Blood vessel pruning is increased, probably due to aberrant
hemodynamics. Arterial ISVs have a slightly increased diameter, while
venous ISVs have greatly reduced diameter. The DA and PCV are both
significantly dilated. Endothelial cells in the DA show increased
surface area and abnormal morphology in response to blood flow. In
contrast, wild-type vessels respond to increased blood flow by an
initial expansion phase, followed by vessel contraction. klf2a-mediated
shear stress sensing is not affected. {ECO:0000269|PubMed:28530658}.
-!- CAUTION: Has low similarity to mammalian endoglins and lacks the
canonical ZP (zona pellucida) domain typically found in these proteins.
{ECO:0000305}.
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EMBL; KY398837; ASA40290.1; -; mRNA.
EMBL; MF788122; ASZ70605.1; -; mRNA.
EMBL; MF788123; ASZ70606.1; -; mRNA.
EMBL; MF788124; ASZ70607.1; -; mRNA.
EMBL; BK010322; DAA80500.1; -; mRNA.
RefSeq; XP_009300329.2; XM_009302054.2.
ZFIN; ZDB-GENE-170530-1; eng.
OrthoDB; 1263397at2759; -.
PRO; PR:A0A1Z2R986; -.
Proteomes; UP000000437; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:UniProtKB.
GO; GO:0001886; P:endothelial cell morphogenesis; IMP:UniProtKB.
InterPro; IPR001507; ZP_dom.
Pfam; PF00100; Zona_pellucida; 1.
2: Evidence at transcript level;
Angiogenesis; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1..20
/evidence="ECO:0000255"
CHAIN 21..559
/note="Endoglin"
/id="PRO_5011117380"
TOPO_DOM 21..473
/note="Extracellular"
/evidence="ECO:0000305"
TRANSMEM 474..494
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 495..559
/note="Cytoplasmic"
/evidence="ECO:0000305"
CARBOHYD 55
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 79
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 109
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 133
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 170
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 302
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 352
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
DISULFID 25..201
/evidence="ECO:0000250|UniProtKB:P17813"
DISULFID 47..174
/evidence="ECO:0000250|UniProtKB:P17813"
DISULFID 381..427
/evidence="ECO:0000250|UniProtKB:P17813"
DISULFID 404
/note="Interchain"
/evidence="ECO:0000250|UniProtKB:P17813"
SEQUENCE 559 AA; 61300 MW; 32634DF699D63F8A CRC64;
MKSICCVLVL CLLLCRRSTA SESICELKDV SGNSNDWIVL REKPLGCWTD FQTENGTEVH
IINLEDNPSV FTVNLLKANK SVVIFTSSSA QSSHAMLFDN PAVSIYVTNK TSLTFIHPTQ
KPLQILTAPP AGNVSAVLRW AAETFGGVTS VTNARNPKTI TFTGVKGSQN SSRCELMPET
PTEKPFIHLE LNEPIEALKS CYMKHEGEKL HIINIPDGVT IRHVSVHLLS DCNVVLRGPA
GTHWIIKNSL RIGILSNNQI HLQSFPLRPR MAISDNPTDI RQKALSYFSS GFISSYSEIR
LNVTNVELWI TDYSISSAPT EVEKTTPSPT SPPFPVQMQL FSSPDFTTPI DNNSRVLSDK
RVYAEISSQT FREASIRVSS CWVRSTPVTR EMPFREEPCF IKDCPKRLSF SFQILQDLPA
GSWDLECAVK LCGVKRINNE ESCTSETPVK RNVQVKPFTP TTNSCFEFGL SAVLGIAFGG
FLIGVLLTGA LWFIKIRTGH PVALGMRSTA AELSVLSISG CPCGLTKRQP VPTHPSPSEN
SSANASIGST QSTPTSSMA


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Pathways :
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Related Genes :
[ENG END] Endoglin (CD antigen CD105)
[Eng Edg] Endoglin (Cell surface MJ7/18 antigen) (CD antigen CD105)
[ENG] Endoglin (CD antigen CD105)
[Eng rCG_45763] Endoglin
[eng] Endoglin
[Eng] Endoglin
[Eng] Endoglin
[ENG] Endoglin
[ENG hCG_18549] Endoglin (Osler-Rendu-Weber syndrome 1), isoform CRA_a
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[ENG] Endoglin
[GDF2 BMP9] Growth/differentiation factor 2 (GDF-2) (Bone morphogenetic protein 9) (BMP-9)
[ENG] Endoglin
[Gdf2 Bmp9] Growth/differentiation factor 2 (GDF-2) (Bone morphogenetic protein 9) (BMP-9)

Bibliography :
[32611689] Correction for Kwon et al., "Hepatitis C Virus Core Protein Modulates Endoglin (CD105) Signaling Pathway for Liver Pathogenesis".
[32592434] Repeatable and objective method for evaluating angiogenesis using real-time RT-PCR of endoglin expression in canine tumors.
[32587778] Bevacizumab promotes active biological behaviors of human umbilical vein endothelial cells by activating TGFβ1 pathways off-VEGF signaling.
[32573726] Mutational and phenotypic characterisation of hereditary hemorrhagic telangiectasia.
[32550557] (CD166) as a gene expression marker for human mesenchymal stromal cell characterisation.
[32541930] PS1 FAD mutants decrease ephrinB2-regulated angiogenic functions, ischemia-induced brain neovascularization and neuronal survival.
[32538908] Whole-Mount In Situ Hybridization in Zebrafish Embryos and Tube Formation Assay in iPSC-ECs to Study the Role of Endoglin in Vascular Development.
[32530126] The Follistatin-like Protein 1 Pathway Is Important for Maintaining Healthy Articular Cartilage.
[32523017] Association of Alk1 and Endoglin Polymorphisms with Cardiovascular Damage.
[32522605] Bone morphogenetic protein receptors: Structure, function and targeting by selective small molecule kinase inhibitors.