ID EGLN_HUMAN Reviewed; 658 AA. AC P17813; Q14248; Q14926; Q5T9C0; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 230. DE RecName: Full=Endoglin; DE AltName: CD_antigen=CD105; DE Flags: Precursor; GN Name=ENG; Synonyms=END; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), FUNCTION, SUBCELLULAR LOCATION, RP SUBUNIT, AND ALTERNATIVE SPLICING. RX PubMed=8370410; DOI=10.1002/eji.1830230943; RA Bellon T., Corbi A., Lastres P., Cales C., Cebrian M., Vera S., RA Cheifetz S., Massague J., Letarte M., Bernabeu C.; RT "Identification and expression of two forms of the human transforming RT growth factor-beta-binding protein endoglin with distinct cytoplasmic RT regions."; RL Eur. J. Immunol. 23:2340-2345(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 14-658, PROTEIN SEQUENCE OF RP 26-36 (ISOFORM LONG), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Umbilical vein; RX PubMed=1692830; DOI=10.1016/s0021-9258(19)38892-1; RA Gougos A., Letarte M.; RT "Primary structure of endoglin, an RGD-containing glycoprotein of human RT endothelial cells."; RL J. Biol. Chem. 265:8361-8364(1990). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-378, FUNCTION, AND INVOLVEMENT IN RP HHT1. RX PubMed=7894484; DOI=10.1038/ng1294-345; RA McAllister K.A., Grogg K.M., Johnson D.W., Gallione C.J., Baldwin M.A., RA Jackson C.E., Helmbold E.A., Markel D.S., McKinnon W.C., Murrell J., RA McCormick M.K., Pericak-Vance M.A., Heutink P., Oostra B.A., Haitjema T., RA Westerman C.J., Porteous M.E., Guttmacher A.E., Letarte M., Marchuk D.A.; RT "Endoglin, a TGF-beta binding protein of endothelial cells, is the gene for RT hereditary haemorrhagic telangiectasia type 1."; RL Nat. Genet. 8:345-351(1994). RN [6] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=1326540; DOI=10.1016/s0021-9258(18)41732-2; RA Cheifetz S., Bellon T., Cales C., Vera S., Bernabeu C., Massague J., RA Letarte M.; RT "Endoglin is a component of the transforming growth factor-beta receptor RT system in human endothelial cells."; RL J. Biol. Chem. 267:19027-19030(1992). RN [7] RP INTERACTION WITH DYNLT4. RX PubMed=16982625; DOI=10.1074/jbc.m608614200; RA Meng Q.-J., Lux A., Holloschi A., Li J., Hughes J.M.X., Foerg T., RA McCarthy J.E.G., Heagerty A.M., Kioschis P., Hafner M., Garland J.M.; RT "Identification of Tctex2beta, a novel dynein light chain family member RT that interacts with different transforming growth factor-beta receptors."; RL J. Biol. Chem. 281:37069-37080(2006). RN [8] RP INTERACTION WITH ARRB2, SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF RP THR-650. RX PubMed=17540773; DOI=10.1074/jbc.m700176200; RA Lee N.Y., Blobe G.C.; RT "The interaction of endoglin with beta-arrestin2 regulates transforming RT growth factor-beta-mediated ERK activation and migration in endothelial RT cells."; RL J. Biol. Chem. 282:21507-21517(2007). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [10] RP FUNCTION, AND INTERACTION WITH GDF2 AND BMP10. RX PubMed=21737454; DOI=10.1074/jbc.m111.260133; RA Castonguay R., Werner E.D., Matthews R.G., Presman E., Mulivor A.W., RA Solban N., Sako D., Pearsall R.S., Underwood K.W., Seehra J., Kumar R., RA Grinberg A.V.; RT "Soluble endoglin specifically binds bone morphogenetic proteins 9 and 10 RT via its orphan domain, inhibits blood vessel formation, and suppresses RT tumor growth."; RL J. Biol. Chem. 286:30034-30046(2011). RN [11] RP INTERACTION WITH GDF2 AND ACVRL1, AND SUBUNIT. RX PubMed=22347366; DOI=10.1371/journal.pone.0029948; RA Alt A., Miguel-Romero L., Donderis J., Aristorena M., Blanco F.J., RA Round A., Rubio V., Bernabeu C., Marina A.; RT "Structural and functional insights into endoglin ligand recognition and RT binding."; RL PLoS ONE 7:E29948-E29948(2012). RN [12] RP FUNCTION. RX PubMed=23300529; DOI=10.1371/journal.pone.0050920; RA Nolan-Stevaux O., Zhong W., Culp S., Shaffer K., Hoover J., RA Wickramasinghe D., Ruefli-Brasse A.; RT "Endoglin requirement for BMP9 signaling in endothelial cells reveals new RT mechanism of action for selective anti-endoglin antibodies."; RL PLoS ONE 7:E50920-E50920(2012). RN [13] {ECO:0007744|PDB:5HZV, ECO:0007744|PDB:5HZW, ECO:0007744|PDB:5I04} RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 26-337, X-RAY CRYSTALLOGRAPHY RP (2.70 ANGSTROMS) OF 338-581, X-RAY CRYSTALLOGRAPHY (4.45 ANGSTROMS) OF RP 26-337 IN COMPLEX WITH GDF2, INTERACTION WITH GDF2 AND ACVRL1, SUBUNIT, RP DOMAIN, DISULFIDE BONDS, AND MUTAGENESIS OF ASP-246; 270-GLN-ILE-271; RP TYR-277; SER-278; PHE-282; PHE-290; CYS-350; CYS-382 AND CYS-516. RX PubMed=28564608; DOI=10.1016/j.celrep.2017.05.011; RA Saito T., Bokhove M., Croci R., Zamora-Caballero S., Han L., Letarte M., RA de Sanctis D., Jovine L.; RT "Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP RT Signaling and HHT1."; RL Cell Rep. 19:1917-1928(2017). RN [14] RP VARIANT HHT1 192-ARG--PRO-198 DEL, AND VARIANT MET-5. RX PubMed=9245986; DOI=10.1086/513906; RA Shovlin C.L., Hughes J.M.B., Scott J., Seidman C.E., Seidman J.G.; RT "Characterization of endoglin and identification of novel mutations in RT hereditary hemorrhagic telangiectasia."; RL Am. J. Hum. Genet. 61:68-79(1997). RN [15] RP VARIANT HHT1 ASP-160. RX PubMed=9157574; RA Yamaguchi H., Azuma H., Shigekiyo T., Inoue H., Saito S.; RT "A novel missense mutation in the endoglin gene in hereditary hemorrhagic RT telangiectasia."; RL Thromb. Haemost. 77:243-247(1997). RN [16] RP VARIANTS HHT1 VAL-52; ARG-53; CYS-149 AND PRO-306. RX PubMed=9554745; RX DOI=10.1002/(sici)1098-1004(1998)11:4<286::aid-humu6>3.0.co;2-b; RA Gallione C.J., Klaus D.J., Yeh E.Y., Stenzel T.T., Xue Y., Anthony K.B., RA McAllister K.A., Baldwin M.A., Berg J.N., Lux A., Smith J.D., Vary C.P.H., RA Craigen W.J., Westermann C.J.J., Warner M.L., Miller Y.E., Jackson C.E., RA Guttmacher A.E., Marchuk D.A.; RT "Mutation and expression analysis of the endoglin gene in hereditary RT hemorrhagic telangiectasia reveals null alleles."; RL Hum. Mutat. 11:286-294(1998). RN [17] RP VARIANTS HHT1 VAL-52; ARG-53; CYS-149 AND PRO-221, SUBCELLULAR LOCATION, RP AND CHARACTERIZATION OF VARIANTS HHT1 VAL-52; ARG-53; CYS-149 AND PRO-221. RX PubMed=10545596; DOI=10.1093/hmg/8.12.2171; RA Pece-Barbara N., Cymerman U., Vera S., Marchuk D.A., Letarte M.; RT "Expression analysis of four endoglin missense mutations suggests that RT haploinsufficiency is the predominant mechanism for hereditary hemorrhagic RT telangiectasia type 1."; RL Hum. Mol. Genet. 8:2171-2181(1999). RN [18] RP VARIANT HHT1 VAL-413. RX PubMed=10982033; DOI=10.1007/s004390000326; RA Gallione C.J., Scheessele E.A., Reinhardt D., Duits A.J., Berg J.N., RA Westermann C.J.J., Marchuk D.A.; RT "Two common endoglin mutations in families with hereditary hemorrhagic RT telangiectasia in the Netherlands Antilles: evidence for a founder RT effect."; RL Hum. Genet. 107:40-44(2000). RN [19] RP VARIANT HHT1 ARG-53, AND TISSUE SPECIFICITY. RX PubMed=10625079; DOI=10.1203/00006450-200001000-00008; RA Cymerman U., Vera S., Pece-Barbara N., Bourdeau A., White R.I. Jr., RA Dunn J., Letarte M.; RT "Identification of hereditary hemorrhagic telangiectasia type 1 in newborns RT by protein expression and mutation analysis of endoglin."; RL Pediatr. Res. 47:24-35(2000). RN [20] RP VARIANTS HHT1 PRO-8; PHE-49; ARG-107; CYS-207 DEL; THR-263; 232-ARG-THR-233 RP DEL; ILE-263 DEL; SER-412 AND MET-504. RX PubMed=15024723; DOI=10.1002/humu.20017; RG French Rendu-Osler network; RA Lesca G., Plauchu H., Coulet F., Lefebvre S., Plessis G., Odent S., RA Riviere S., Leheup B., Goizet C., Carette M.-F., Cordier J.-F., Pinson S., RA Soubrier F., Calender A., Giraud S.; RT "Molecular screening of ALK1/ACVRL1 and ENG genes in hereditary hemorrhagic RT telangiectasia in France."; RL Hum. Mutat. 23:289-299(2004). RN [21] RP VARIANTS HHT1 PRO-221 AND ILE-263 DEL, AND VARIANT LEU-615. RX PubMed=15712270; DOI=10.1002/humu.9311; RA Kuehl H.K.A., Caselitz M., Hasenkamp S., Wagner S., El-Harith E.-H.A., RA Manns M.P., Stuhrmann M.; RT "Hepatic manifestation is associated with ALK1 in hereditary hemorrhagic RT telangiectasia: identification of five novel ALK1 and one novel ENG RT mutations."; RL Hum. Mutat. 25:320-320(2005). RN [22] RP VARIANTS HHT1 ASP-11; ASP-105; GLU-175; THR-220; ASP-308; SER-363; TRP-437; RP SER-490; HIS-529; PRO-547 AND ASP-604. RX PubMed=16752392; DOI=10.1002/humu.20342; RA Bossler A.D., Richards J., George C., Godmilow L., Ganguly A.; RT "Novel mutations in ENG and ACVRL1 identified in a series of 200 RT individuals undergoing clinical genetic testing for hereditary hemorrhagic RT telangiectasia (HHT): correlation of genotype with phenotype."; RL Hum. Mutat. 27:667-675(2006). RN [23] RP VARIANTS HHT1 193-THR-LEU-194 DELINS VAL-LEU-GLN AND ASP-545. RX PubMed=16525724; RA Argyriou L., Twelkemeyer S., Panchulidze I., Wehner L.E., Teske U., RA Engel W., Nayernia K.; RT "Novel mutations in the ENG and ACVRL1 genes causing hereditary hemorrhagic RT teleangiectasia."; RL Int. J. Mol. Med. 17:655-659(2006). RN [24] RP VARIANTS PRO-150; PRO-205; MET-236; MET-315; GLU-374; ARG-414; SER-545; RP TYR-549 AND ALA-561, AND VARIANTS HHT1 GLN-221; GLU-238; SER-263; ARG-269; RP TYR-394; PRO-529 AND ARG-603. RX PubMed=20414677; DOI=10.1007/s00439-010-0825-4; RA Richards-Yutz J., Grant K., Chao E.C., Walther S.E., Ganguly A.; RT "Update on molecular diagnosis of hereditary hemorrhagic telangiectasia."; RL Hum. Genet. 128:61-77(2010). CC -!- FUNCTION: Vascular endothelium glycoprotein that plays an important CC role in the regulation of angiogenesis (PubMed:21737454, CC PubMed:23300529). Required for normal structure and integrity of adult CC vasculature (PubMed:7894484). Regulates the migration of vascular CC endothelial cells (PubMed:17540773). Required for normal extraembryonic CC angiogenesis and for embryonic heart development (By similarity). May CC regulate endothelial cell shape changes in response to blood flow, CC which drive vascular remodeling and establishment of normal vascular CC morphology during angiogenesis (By similarity). May play a critical CC role in the binding of endothelial cells to integrins and/or other RGD CC receptors (PubMed:1692830). Acts as a TGF-beta coreceptor and is CC involved in the TGF-beta/BMP signaling cascade that ultimately leads to CC the activation of SMAD transcription factors (PubMed:8370410, CC PubMed:21737454, PubMed:22347366, PubMed:23300529). Required for CC GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates CC TGFB1 signaling through SMAD3 (PubMed:21737454, PubMed:22347366, CC PubMed:23300529). {ECO:0000250|UniProtKB:Q63961, CC ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:21737454, CC ECO:0000269|PubMed:23300529, ECO:0000269|PubMed:7894484, CC ECO:0000269|PubMed:8370410, ECO:0000305|PubMed:1692830}. CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:8370410, PubMed:1326540, CC PubMed:21737454, PubMed:22347366, PubMed:28564608). Forms a heteromeric CC complex with the signaling receptors for transforming growth factor- CC beta: TGFBR1 and/or TGFBR2 (PubMed:1326540). It is able to bind TGFB1 CC and TGFB2 with high affinity, but not TGFB3 (PubMed:8370410, CC PubMed:1326540). Interacts with GDF2, forming a heterotetramer with a CC 2:2 stoichiometry (PubMed:21737454, PubMed:22347366, PubMed:28564608). CC Interacts with ACVRL1 (PubMed:22347366, PubMed:28564608). Can form a CC heteromeric complex with GDF2 and ACVRL1 (PubMed:28564608). Interacts CC with BMP10 (PubMed:21737454). Interacts with DYNLT4 (PubMed:16982625). CC Interacts with ARRB2 (PubMed:17540773). {ECO:0000269|PubMed:1326540, CC ECO:0000269|PubMed:16982625, ECO:0000269|PubMed:17540773, CC ECO:0000269|PubMed:21737454, ECO:0000269|PubMed:22347366, CC ECO:0000269|PubMed:28564608, ECO:0000269|PubMed:8370410}. CC -!- INTERACTION: CC P17813; P17813: ENG; NbExp=2; IntAct=EBI-2834630, EBI-2834630; CC P17813; PRO_0000033903 [Q9UK05]: GDF2; NbExp=10; IntAct=EBI-2834630, EBI-16227344; CC P17813; P08648: ITGA5; NbExp=4; IntAct=EBI-2834630, EBI-1382311; CC P17813; P05556: ITGB1; NbExp=3; IntAct=EBI-2834630, EBI-703066; CC P17813; P17931: LGALS3; NbExp=5; IntAct=EBI-2834630, EBI-1170392; CC P17813; P01137: TGFB1; NbExp=2; IntAct=EBI-2834630, EBI-779636; CC P17813; P19474: TRIM21; NbExp=6; IntAct=EBI-2834630, EBI-81290; CC P17813-1; P02750: LRG1; NbExp=4; IntAct=EBI-16065304, EBI-9083443; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10545596, CC ECO:0000269|PubMed:1326540, ECO:0000269|PubMed:1692830, CC ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:8370410}; Single-pass CC type I membrane protein {ECO:0000305|PubMed:1692830, CC ECO:0000305|PubMed:8370410}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P17813-1; Sequence=Displayed; CC Name=Short; CC IsoId=P17813-2; Sequence=VSP_004233; CC -!- TISSUE SPECIFICITY: Detected on umbilical veil endothelial cells CC (PubMed:10625079). Detected in placenta (at protein level) CC (PubMed:1692830). Detected on endothelial cells (PubMed:1692830). CC {ECO:0000269|PubMed:10625079, ECO:0000269|PubMed:1692830}. CC -!- DOMAIN: The ZP domain mediates dimerization. CC {ECO:0000269|PubMed:28564608}. CC -!- DOMAIN: The N-terminal OR region is composed of two intertwined domains CC (OR1 and OR2) with a common, novel fold. Each contains 12 beta-strands CC that form a parallel beta-helix-like structure, plus a single alpha- CC helix. The OR1 region mediates interaction with GDF2. CC {ECO:0000269|PubMed:28564608}. CC -!- DISEASE: Telangiectasia, hereditary hemorrhagic, 1 (HHT1) [MIM:187300]: CC A multisystemic vascular dysplasia leading to dilation of permanent CC blood vessels and arteriovenous malformations of skin, mucosa, and CC viscera. The disease is characterized by recurrent epistaxis and CC gastro-intestinal hemorrhage. Visceral involvement includes CC arteriovenous malformations of the lung, liver, and brain. CC {ECO:0000269|PubMed:10545596, ECO:0000269|PubMed:10625079, CC ECO:0000269|PubMed:10982033, ECO:0000269|PubMed:15024723, CC ECO:0000269|PubMed:15712270, ECO:0000269|PubMed:16525724, CC ECO:0000269|PubMed:16752392, ECO:0000269|PubMed:20414677, CC ECO:0000269|PubMed:7894484, ECO:0000269|PubMed:9157574, CC ECO:0000269|PubMed:9245986, ECO:0000269|PubMed:9554745}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40452/ENG"; CC -!- WEB RESOURCE: Name=Hereditary Hemorrhagic Telangiectasia and ENG; CC URL="http://arup.utah.edu/database/ENG/ENG_welcome.php"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X72012; CAA50891.1; -; mRNA. DR EMBL; AL157935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL162586; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87702.1; -; Genomic_DNA. DR EMBL; J05481; AAA35800.1; -; mRNA. DR EMBL; U37439; AAC63386.1; -; Genomic_DNA. DR EMBL; AF036969; AAC63386.1; JOINED; Genomic_DNA. DR EMBL; U37447; AAC63386.1; JOINED; Genomic_DNA. DR EMBL; AF036970; AAC63386.1; JOINED; Genomic_DNA. DR EMBL; U37446; AAC63386.1; JOINED; Genomic_DNA. DR EMBL; U37445; AAC63386.1; JOINED; Genomic_DNA. DR EMBL; AF036971; AAC63386.1; JOINED; Genomic_DNA. DR EMBL; U37442; AAC63386.1; JOINED; Genomic_DNA. DR EMBL; U37441; AAC63386.1; JOINED; Genomic_DNA. DR CCDS; CCDS48029.1; -. [P17813-1] DR CCDS; CCDS6880.1; -. [P17813-2] DR PIR; S50831; S50831. DR RefSeq; NP_000109.1; NM_000118.3. [P17813-2] DR RefSeq; NP_001108225.1; NM_001114753.2. [P17813-1] DR RefSeq; NP_001265067.1; NM_001278138.1. DR PDB; 5HZV; X-ray; 2.70 A; A=338-581. DR PDB; 5HZW; X-ray; 4.45 A; A=26-337. DR PDB; 5I04; X-ray; 2.42 A; A=26-337. DR PDBsum; 5HZV; -. DR PDBsum; 5HZW; -. DR PDBsum; 5I04; -. DR AlphaFoldDB; P17813; -. DR SASBDB; P17813; -. DR SMR; P17813; -. DR BioGRID; 108337; 204. DR CORUM; P17813; -. DR DIP; DIP-6246N; -. DR IntAct; P17813; 225. DR MINT; P17813; -. DR STRING; 9606.ENSP00000362299; -. DR ChEMBL; CHEMBL3712885; -. DR DrugBank; DB06322; Carotuximab. DR GuidetoPHARMACOLOGY; 2895; -. DR GlyCosmos; P17813; 9 sites, 2 glycans. DR GlyGen; P17813; 10 sites, 3 O-linked glycans (5 sites). DR iPTMnet; P17813; -. DR PhosphoSitePlus; P17813; -. DR SwissPalm; P17813; -. DR BioMuta; ENG; -. DR DMDM; 3041681; -. DR EPD; P17813; -. DR jPOST; P17813; -. DR MassIVE; P17813; -. DR MaxQB; P17813; -. DR PaxDb; 9606-ENSP00000362299; -. DR PeptideAtlas; P17813; -. DR ProteomicsDB; 53517; -. [P17813-1] DR ProteomicsDB; 53518; -. [P17813-2] DR Pumba; P17813; -. DR ABCD; P17813; 2 sequenced antibodies. DR Antibodypedia; 2321; 2718 antibodies from 53 providers. DR DNASU; 2022; -. DR Ensembl; ENST00000344849.4; ENSP00000341917.3; ENSG00000106991.14. [P17813-2] DR Ensembl; ENST00000373203.9; ENSP00000362299.4; ENSG00000106991.14. [P17813-1] DR GeneID; 2022; -. DR KEGG; hsa:2022; -. DR MANE-Select; ENST00000373203.9; ENSP00000362299.4; NM_001114753.3; NP_001108225.1. DR UCSC; uc004bsj.6; human. [P17813-1] DR AGR; HGNC:3349; -. DR CTD; 2022; -. DR DisGeNET; 2022; -. DR GeneCards; ENG; -. DR GeneReviews; ENG; -. DR HGNC; HGNC:3349; ENG. DR HPA; ENSG00000106991; Tissue enhanced (heart). DR MalaCards; ENG; -. DR MIM; 131195; gene. DR MIM; 187300; phenotype. DR neXtProt; NX_P17813; -. DR OpenTargets; ENSG00000106991; -. DR Orphanet; 231160; Familial cerebral saccular aneurysm. DR Orphanet; 329971; Generalized juvenile polyposis/juvenile polyposis coli. DR Orphanet; 774; Hereditary hemorrhagic telangiectasia. DR Orphanet; 275777; Heritable pulmonary arterial hypertension. DR PharmGKB; PA27785; -. DR VEuPathDB; HostDB:ENSG00000106991; -. DR eggNOG; ENOG502RZQ9; Eukaryota. DR GeneTree; ENSGT00530000063861; -. DR InParanoid; P17813; -. DR OMA; QCEIPRE; -. DR OrthoDB; 5320235at2759; -. DR PhylomeDB; P17813; -. DR TreeFam; TF337375; -. DR PathwayCommons; P17813; -. DR SignaLink; P17813; -. DR SIGNOR; P17813; -. DR BioGRID-ORCS; 2022; 14 hits in 1157 CRISPR screens. DR ChiTaRS; ENG; human. DR GeneWiki; Endoglin; -. DR GenomeRNAi; 2022; -. DR Pharos; P17813; Tbio. DR PRO; PR:P17813; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P17813; Protein. DR Bgee; ENSG00000106991; Expressed in right lung and 187 other cell types or tissues. DR ExpressionAtlas; P17813; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0072563; C:endothelial microparticle; IEA:Ensembl. DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0043235; C:receptor complex; IPI:BHF-UCL. DR GO; GO:0048185; F:activin binding; TAS:BHF-UCL. DR GO; GO:0015026; F:coreceptor activity; IDA:BHF-UCL. DR GO; GO:0005534; F:galactose binding; IDA:BHF-UCL. DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL. DR GO; GO:0030546; F:signaling receptor activator activity; IDA:BHF-UCL. DR GO; GO:0050431; F:transforming growth factor beta binding; IPI:BHF-UCL. DR GO; GO:0005024; F:transforming growth factor beta receptor activity; IBA:GO_Central. DR GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:BHF-UCL. DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IPI:BHF-UCL. DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IPI:BHF-UCL. DR GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL. DR GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; ISS:BHF-UCL. DR GO; GO:1905222; P:atrioventricular canal morphogenesis; ISS:BHF-UCL. DR GO; GO:0030509; P:BMP signaling pathway; TAS:BHF-UCL. DR GO; GO:0060348; P:bone development; IEA:Ensembl. DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISS:BHF-UCL. DR GO; GO:0003209; P:cardiac atrium morphogenesis; ISS:BHF-UCL. DR GO; GO:0003208; P:cardiac ventricle morphogenesis; ISS:BHF-UCL. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0060326; P:cell chemotaxis; IMP:BHF-UCL. DR GO; GO:0016477; P:cell migration; IMP:BHF-UCL. DR GO; GO:0003273; P:cell migration involved in endocardial cushion formation; IEA:Ensembl. DR GO; GO:0048870; P:cell motility; IMP:BHF-UCL. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0022009; P:central nervous system vasculogenesis; IMP:BHF-UCL. DR GO; GO:0070483; P:detection of hypoxia; IDA:BHF-UCL. DR GO; GO:0035912; P:dorsal aorta morphogenesis; ISS:BHF-UCL. DR GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:BHF-UCL. DR GO; GO:0001837; P:epithelial to mesenchymal transition; IBA:GO_Central. DR GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL. DR GO; GO:0070278; P:extracellular matrix constituent secretion; IEA:Ensembl. DR GO; GO:0022617; P:extracellular matrix disassembly; IMP:BHF-UCL. DR GO; GO:0001947; P:heart looping; ISS:BHF-UCL. DR GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL. DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:BHF-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; ISS:BHF-UCL. DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IMP:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:BHF-UCL. DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL. DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl. DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:BHF-UCL. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl. DR GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IGI:BHF-UCL. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:BHF-UCL. DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:1905065; P:positive regulation of vascular associated smooth muscle cell differentiation; ISS:BHF-UCL. DR GO; GO:0030155; P:regulation of cell adhesion; TAS:BHF-UCL. DR GO; GO:0042127; P:regulation of cell population proliferation; TAS:BHF-UCL. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:HGNC-UCL. DR GO; GO:0042325; P:regulation of phosphorylation; TAS:BHF-UCL. DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:HGNC-UCL. DR GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0048745; P:smooth muscle tissue development; ISS:BHF-UCL. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0097084; P:vascular associated smooth muscle cell development; ISS:BHF-UCL. DR GO; GO:0001570; P:vasculogenesis; IMP:BHF-UCL. DR GO; GO:0048845; P:venous blood vessel morphogenesis; ISS:BHF-UCL. DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL. DR GO; GO:0042060; P:wound healing; IMP:BHF-UCL. DR PANTHER; PTHR14002:SF1; ENDOGLIN; 1. DR PANTHER; PTHR14002; ENDOGLIN/TGF-BETA RECEPTOR TYPE III; 1. DR Genevisible; P17813; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Angiogenesis; Cell adhesion; KW Cell membrane; Direct protein sequencing; Disease variant; Disulfide bond; KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..25 FT /evidence="ECO:0000269|PubMed:1692830" FT CHAIN 26..658 FT /note="Endoglin" FT /id="PRO_0000021156" FT TOPO_DOM 26..586 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 587..611 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 612..658 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 363..533 FT /note="ZP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375, FT ECO:0000305|PubMed:28564608" FT REGION 26..337 FT /note="Required for interaction with GDF2" FT /evidence="ECO:0000269|PubMed:21737454, FT ECO:0000269|PubMed:22347366, ECO:0000269|PubMed:28564608" FT REGION 26..46 FT /note="OR1, N-terminal part" FT /evidence="ECO:0000269|PubMed:28564608" FT REGION 47..199 FT /note="OR2" FT /evidence="ECO:0000269|PubMed:28564608" FT REGION 200..330 FT /note="OR1, C-terminal part" FT /evidence="ECO:0000269|PubMed:28564608" FT REGION 270..282 FT /note="Essential for interaction with GDF2" FT /evidence="ECO:0000269|PubMed:28564608" FT REGION 626..658 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 399..401 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 632..658 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 646 FT /note="Phosphoserine; by TGFBR1" FT /evidence="ECO:0000250|UniProtKB:Q63961" FT MOD_RES 649 FT /note="Phosphoserine; by TGFBR1" FT /evidence="ECO:0000250|UniProtKB:Q63961" FT CARBOHYD 88 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 102 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 121 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 134 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 307 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 30..207 FT /evidence="ECO:0000269|PubMed:28564608, FT ECO:0007744|PDB:5HZW, ECO:0007744|PDB:5I04" FT DISULFID 53..182 FT /evidence="ECO:0000269|PubMed:28564608, FT ECO:0007744|PDB:5HZW, ECO:0007744|PDB:5I04" FT DISULFID 242..330 FT /evidence="ECO:0000269|PubMed:28564608, FT ECO:0007744|PDB:5HZW" FT DISULFID 350..382 FT /evidence="ECO:0000269|PubMed:28564608, FT ECO:0007744|PDB:5HZV" FT DISULFID 363..442 FT /evidence="ECO:0000269|PubMed:28564608, FT ECO:0007744|PDB:5HZV" FT DISULFID 394..412 FT /evidence="ECO:0000269|PubMed:28564608, FT ECO:0007744|PDB:5HZV" FT DISULFID 493..549 FT /evidence="ECO:0000269|PubMed:28564608, FT ECO:0007744|PDB:5HZV" FT DISULFID 516 FT /note="Interchain" FT /evidence="ECO:0000305|PubMed:28564608" FT VAR_SEQ 619..658 FT /note="SPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA -> EYPRPPQ FT (in isoform Short)" FT /evidence="ECO:0000303|PubMed:8370410" FT /id="VSP_004233" FT VARIANT 5 FT /note="T -> M (in dbSNP:rs35400405)" FT /evidence="ECO:0000269|PubMed:9245986" FT /id="VAR_005192" FT VARIANT 8 FT /note="L -> P (in HHT1; dbSNP:rs1564466414)" FT /evidence="ECO:0000269|PubMed:15024723" FT /id="VAR_026774" FT VARIANT 11 FT /note="A -> D (in HHT1)" FT /evidence="ECO:0000269|PubMed:16752392" FT /id="VAR_070279" FT VARIANT 49 FT /note="V -> F (in HHT1; dbSNP:rs1252348200)" FT /evidence="ECO:0000269|PubMed:15024723" FT /id="VAR_026775" FT VARIANT 52 FT /note="G -> V (in HHT1; impairs protein folding; abolishes FT expression at the cell surface)" FT /evidence="ECO:0000269|PubMed:10545596, FT ECO:0000269|PubMed:9554745" FT /id="VAR_005193" FT VARIANT 53 FT /note="C -> R (in HHT1; impairs protein folding; abolishes FT expression at the cell surface)" FT /evidence="ECO:0000269|PubMed:10545596, FT ECO:0000269|PubMed:10625079, ECO:0000269|PubMed:9554745" FT /id="VAR_005194" FT VARIANT 105 FT /note="V -> D (in HHT1; dbSNP:rs1588585880)" FT /evidence="ECO:0000269|PubMed:16752392" FT /id="VAR_070280" FT VARIANT 107 FT /note="L -> R (in HHT1)" FT /evidence="ECO:0000269|PubMed:15024723" FT /id="VAR_026776" FT VARIANT 149 FT /note="W -> C (in HHT1; impairs protein folding; nearly FT abolishes expression at the cell surface; FT dbSNP:rs878853657)" FT /evidence="ECO:0000269|PubMed:10545596, FT ECO:0000269|PubMed:9554745" FT /id="VAR_005195" FT VARIANT 150 FT /note="A -> P (found in a family with hereditary FT hemorrhagic talagiectasia; uncertain significance)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070281" FT VARIANT 160 FT /note="A -> D (in HHT1)" FT /evidence="ECO:0000269|PubMed:9157574" FT /id="VAR_009120" FT VARIANT 175 FT /note="A -> E (in HHT1)" FT /evidence="ECO:0000269|PubMed:16752392" FT /id="VAR_070282" FT VARIANT 192..198 FT /note="Missing (in HHT1)" FT /evidence="ECO:0000269|PubMed:9245986" FT /id="VAR_005196" FT VARIANT 193..194 FT /note="TL -> VLQ (in HHT1)" FT /evidence="ECO:0000269|PubMed:16525724" FT /id="VAR_070283" FT VARIANT 205 FT /note="R -> P" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070284" FT VARIANT 207 FT /note="Missing (in HHT1)" FT /evidence="ECO:0000269|PubMed:15024723" FT /id="VAR_026777" FT VARIANT 220 FT /note="I -> T (in HHT1; dbSNP:rs1588582695)" FT /evidence="ECO:0000269|PubMed:16752392" FT /id="VAR_070285" FT VARIANT 221 FT /note="L -> P (in HHT1; impairs protein folding; strongly FT reduces expression at the cell surface; FT dbSNP:rs1554810378)" FT /evidence="ECO:0000269|PubMed:10545596, FT ECO:0000269|PubMed:15712270" FT /id="VAR_009121" FT VARIANT 221 FT /note="L -> Q (in HHT1)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070286" FT VARIANT 232..233 FT /note="Missing (in HHT1)" FT /id="VAR_026778" FT VARIANT 236 FT /note="V -> M (found in a patient with hereditary FT hemorrhagic talagiectasia; uncertain significance; FT dbSNP:rs754136153)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070287" FT VARIANT 238 FT /note="V -> E (in HHT1; dbSNP:rs1060501415)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070288" FT VARIANT 263 FT /note="I -> S (in HHT1)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070289" FT VARIANT 263 FT /note="I -> T (in HHT1)" FT /evidence="ECO:0000269|PubMed:15024723" FT /id="VAR_026780" FT VARIANT 263 FT /note="Missing (in HHT1)" FT /evidence="ECO:0000269|PubMed:15024723, FT ECO:0000269|PubMed:15712270" FT /id="VAR_026779" FT VARIANT 269 FT /note="M -> R (in HHT1)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070290" FT VARIANT 306 FT /note="L -> P (in HHT1)" FT /evidence="ECO:0000269|PubMed:9554745" FT /id="VAR_005197" FT VARIANT 308 FT /note="A -> D (in HHT1)" FT /evidence="ECO:0000269|PubMed:16752392" FT /id="VAR_070291" FT VARIANT 315 FT /note="V -> M (found in a family with hereditary FT hemorrhagic talagiectasia; uncertain significance; FT dbSNP:rs763508329)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070292" FT VARIANT 363 FT /note="C -> S (in HHT1; dbSNP:rs1588580782)" FT /evidence="ECO:0000269|PubMed:16752392" FT /id="VAR_070293" FT VARIANT 366 FT /note="D -> H (in dbSNP:rs1800956)" FT /id="VAR_014764" FT VARIANT 374 FT /note="K -> E (found in a patient with hereditary FT hemorrhagic talagiectasia; uncertain significance)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070294" FT VARIANT 394 FT /note="C -> Y (in HHT1; dbSNP:rs1830434129)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070295" FT VARIANT 412 FT /note="C -> S (in HHT1)" FT /evidence="ECO:0000269|PubMed:15024723" FT /id="VAR_026781" FT VARIANT 413 FT /note="G -> V (in HHT1; dbSNP:rs121918401)" FT /evidence="ECO:0000269|PubMed:10982033" FT /id="VAR_037140" FT VARIANT 414 FT /note="M -> R (found in a patient with hereditary FT hemorrhagic talagiectasia; uncertain significance)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070296" FT VARIANT 437 FT /note="R -> W (in HHT1; dbSNP:rs1434169817)" FT /evidence="ECO:0000269|PubMed:16752392" FT /id="VAR_070297" FT VARIANT 490 FT /note="L -> S (in HHT1; dbSNP:rs763475207)" FT /evidence="ECO:0000269|PubMed:16752392" FT /id="VAR_070298" FT VARIANT 504 FT /note="V -> M (in HHT1; dbSNP:rs116330805)" FT /evidence="ECO:0000269|PubMed:15024723" FT /id="VAR_026782" FT VARIANT 529 FT /note="R -> H (in HHT1; dbSNP:rs863223538)" FT /evidence="ECO:0000269|PubMed:16752392" FT /id="VAR_070299" FT VARIANT 529 FT /note="R -> P (in HHT1)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070300" FT VARIANT 545 FT /note="G -> D (in HHT1)" FT /evidence="ECO:0000269|PubMed:16525724" FT /id="VAR_070301" FT VARIANT 545 FT /note="G -> S (in dbSNP:rs142896669)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070302" FT VARIANT 547 FT /note="L -> P (in HHT1)" FT /evidence="ECO:0000269|PubMed:16752392" FT /id="VAR_070303" FT VARIANT 549 FT /note="C -> Y (found in a patient with hereditary FT hemorrhagic talagiectasia; uncertain significance; FT dbSNP:rs1060501421)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070304" FT VARIANT 561 FT /note="D -> A (in dbSNP:rs375965489)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070305" FT VARIANT 603 FT /note="G -> R (in HHT1; dbSNP:rs1830302008)" FT /evidence="ECO:0000269|PubMed:20414677" FT /id="VAR_070306" FT VARIANT 604 FT /note="A -> D (in HHT1)" FT /evidence="ECO:0000269|PubMed:16752392" FT /id="VAR_070307" FT VARIANT 615 FT /note="S -> L (in dbSNP:rs148002300)" FT /evidence="ECO:0000269|PubMed:15712270" FT /id="VAR_026783" FT MUTAGEN 246 FT /note="D->A: No effect on interaction with GDF2." FT /evidence="ECO:0000269|PubMed:28564608" FT MUTAGEN 269 FT /note="M->A: Impairs protein folding, but does not abolish FT interaction with GDF2." FT /evidence="ECO:0000269|PubMed:28564608" FT MUTAGEN 270..271 FT /note="QI->AA: Loss of interaction with GDF2." FT /evidence="ECO:0000269|PubMed:28564608" FT MUTAGEN 277 FT /note="Y->A: No effect on interaction with GDF2." FT /evidence="ECO:0000269|PubMed:28564608" FT MUTAGEN 278 FT /note="S->P: Loss of interaction with GDF2." FT /evidence="ECO:0000269|PubMed:28564608" FT MUTAGEN 282 FT /note="F->V: Loss of interaction with GDF2." FT /evidence="ECO:0000269|PubMed:28564608" FT MUTAGEN 290 FT /note="F->A: No effect on interaction with GDF2." FT /evidence="ECO:0000269|PubMed:28564608" FT MUTAGEN 350 FT /note="C->S: Impairs protein folding. Impairs protein FT folding; when associated with C-382." FT /evidence="ECO:0000269|PubMed:28564608" FT MUTAGEN 382 FT /note="C->S: Impairs protein folding. Impairs protein FT folding; when associated with C-350." FT /evidence="ECO:0000269|PubMed:28564608" FT MUTAGEN 516 FT /note="C->S: Loss of dimerization via ZP domain." FT /evidence="ECO:0000269|PubMed:28564608" FT MUTAGEN 650 FT /note="T->A: Loss of interaction with ARRB2." FT /evidence="ECO:0000269|PubMed:17540773" FT CONFLICT 14 FT /note="L -> G (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 122..130 FT /note="SSLVTFQEP -> FQPGHLPRA (in Ref. 5)" FT /evidence="ECO:0000305" FT TURN 37..39 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 40..54 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 61..70 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 76..83 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 94..103 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 105..111 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 116..120 FT /evidence="ECO:0007829|PDB:5I04" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 125..129 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:5I04" FT HELIX 143..151 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 156..171 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 185..189 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 193..200 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 217..224 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 232..240 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 249..254 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 259..267 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 270..279 FT /evidence="ECO:0007829|PDB:5I04" FT HELIX 296..305 FT /evidence="ECO:0007829|PDB:5I04" FT STRAND 309..327 FT /evidence="ECO:0007829|PDB:5I04" FT HELIX 352..358 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 360..363 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 365..373 FT /evidence="ECO:0007829|PDB:5HZV" FT HELIX 374..379 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 384..388 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 400..408 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 415..417 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 420..431 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 436..443 FT /evidence="ECO:0007829|PDB:5HZV" FT TURN 445..447 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 448..459 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 465..467 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 473..481 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 484..496 FT /evidence="ECO:0007829|PDB:5HZV" FT TURN 499..501 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 503..508 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 517..519 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 524..526 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 529..532 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 538..540 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 543..555 FT /evidence="ECO:0007829|PDB:5HZV" FT HELIX 560..562 FT /evidence="ECO:0007829|PDB:5HZV" FT STRAND 564..574 FT /evidence="ECO:0007829|PDB:5HZV" SQ SEQUENCE 658 AA; 70578 MW; 49CA2CE013298D17 CRC64; MDRGTLPLAV ALLLASCSLS PTSLAETVHC DLQPVGPERG EVTYTTSQVS KGCVAQAPNA ILEVHVLFLE FPTGPSQLEL TLQASKQNGT WPREVLLVLS VNSSVFLHLQ ALGIPLHLAY NSSLVTFQEP PGVNTTELPS FPKTQILEWA AERGPITSAA ELNDPQSILL RLGQAQGSLS FCMLEASQDM GRTLEWRPRT PALVRGCHLE GVAGHKEAHI LRVLPGHSAG PRTVTVKVEL SCAPGDLDAV LILQGPPYVS WLIDANHNMQ IWTTGEYSFK IFPEKNIRGF KLPDTPQGLL GEARMLNASI VASFVELPLA SIVSLHASSC GGRLQTSPAP IQTTPPKDTC SPELLMSLIQ TKCADDAMTL VLKKELVAHL KCTITGLTFW DPSCEAEDRG DKFVLRSAYS SCGMQVSASM ISNEAVVNIL SSSSPQRKKV HCLNMDSLSF QLGLYLSPHF LQASNTIEPG QQSFVQVRVS PSVSEFLLQL DSCHLDLGPE GGTVELIQGR AAKGNCVSLL SPSPEGDPRF SFLLHFYTVP IPKTGTLSCT VALRPKTGSQ DQEVHRTVFM RLNIISPDLS GCTSKGLVLP AVLGITFGAF LIGALLTAAL WYIYSHTRSP SKREPVVAVA APASSESSST NHSIGSTQST PCSTSSMA //