EGLN_DANRE
ID EGLN_DANRE Reviewed; 559 AA.
AC A0A1Z2R986; A0A286NMM4; A0A286NMM5; A0A286NMM6;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Endoglin {ECO:0000303|PubMed:28530658};
DE Flags: Precursor;
GN Name=eng {ECO:0000303|PubMed:28530658};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:ASA40290.1};
RN [1] {ECO:0000312|EMBL:ASA40290.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Han R., Zhang D., Yang J.;
RT "Tempo-spatial expression of endoglin in zebrafish.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:DAA80500.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28530658; DOI=10.1038/ncb3528;
RA Sugden W.W., Meissner R., Aegerter-Wilmsen T., Tsaryk R., Leonard E.V.,
RA Bussmann J., Hamm M.J., Herzog W., Jin Y., Jakobsson L., Denz C.,
RA Siekmann A.F.;
RT "Endoglin controls blood vessel diameter through endothelial cell shape
RT changes in response to haemodynamic cues.";
RL Nat. Cell Biol. 19:653-665(2017).
CC -!- FUNCTION: Vascular endothelium glycoprotein that plays an important
CC role in the regulation of angiogenesis. Required for normal structure
CC and integrity of adult vasculature. Important for endothelial cell
CC shape changes in response to blood flow, which drive vascular
CC remodeling and establishment of normal vascular morphology during
CC angiogenesis. {ECO:0000269|PubMed:28530658}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P17813}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17813};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Detected in vascular tissue at 36-72 hours post-
CC fertilization, where it localizes to endothelial cells.
CC {ECO:0000269|PubMed:28530658}.
CC -!- DISRUPTION PHENOTYPE: Viable, with survival to adult stages. Brain
CC tissue shows widespread vascular malformations with localized widening
CC of blood vessels. During embryogenesis, blood vessel connectivity
CC between the dorsal aorta (DA), intersegmental vessels (ISVs) and
CC posterior cardinal vein (PCV) appears normal at 72 hours post-
CC fertilization (hpf). However, blood flow through ISVs is significantly
CC reduced. Blood vessel pruning is increased, probably due to aberrant
CC hemodynamics. Arterial ISVs have a slightly increased diameter, while
CC venous ISVs have greatly reduced diameter. The DA and PCV are both
CC significantly dilated. Endothelial cells in the DA show increased
CC surface area and abnormal morphology in response to blood flow. In
CC contrast, wild-type vessels respond to increased blood flow by an
CC initial expansion phase, followed by vessel contraction. klf2a-mediated
CC shear stress sensing is not affected. {ECO:0000269|PubMed:28530658}.
CC -!- CAUTION: Has low similarity to mammalian endoglins and lacks the
CC canonical ZP (zona pellucida) domain typically found in these proteins.
CC {ECO:0000305}.
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DR EMBL; KY398837; ASA40290.1; -; mRNA.
DR EMBL; MF788122; ASZ70605.1; -; mRNA.
DR EMBL; MF788123; ASZ70606.1; -; mRNA.
DR EMBL; MF788124; ASZ70607.1; -; mRNA.
DR EMBL; BK010322; DAA80500.1; -; mRNA.
DR RefSeq; XP_009300329.2; XM_009302054.2.
DR AlphaFoldDB; A0A1Z2R986; -.
DR SMR; A0A1Z2R986; -.
DR ZFIN; ZDB-GENE-170530-1; eng.
DR OrthoDB; 1263397at2759; -.
DR PRO; PR:A0A1Z2R986; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:UniProtKB.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IMP:UniProtKB.
DR GO; GO:1990266; P:neutrophil migration; IBA:GO_Central.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR Pfam; PF00100; Zona_pellucida; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..559
FT /note="Endoglin"
FT /id="PRO_5011117380"
FT TOPO_DOM 21..473
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 528..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 25..201
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 47..174
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 381..427
FT /evidence="ECO:0000250|UniProtKB:P17813"
FT DISULFID 404
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P17813"
SQ 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
