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UniProtKB/Swiss-Prot entry Q92838

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name EDA_HUMAN
Primary accession number Q92838
Secondary accession numbers A0AUZ2 A2A337 O75910 Q5JS00 Q5JUM7 Q9UP77 Q9Y6L0 Q9Y6L1 Q9Y6L2 Q9Y6L3 Q9Y6L4
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on July 15, 1999 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 99)
Name and origin of the protein
Protein name Ectodysplasin-A
Synonyms Ectodermal dysplasia protein
EDA protein
Contains Ectodysplasin-A, membrane form
Ectodysplasin-A, secreted form
Gene name
Name: EDA
Synonyms: ED1, EDA2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM I), AND VARIANTS ED1 HIS-61 AND LEU-69.
TISSUE=Sweat gland;
DOI=10.1038/ng0895-409; PubMed=8696334 [NCBI, ExPASy, EBI, Israel, Japan]
Kere J., Srivastava A.K., Montonen O., Zonana J., Thomas N.S.T., Ferguson B.M., Munoz F., Morgan D., Clarke A., Baybayan P., Chen E.Y., Ezer S., Saarialho-Kere U., la Chapelle A., Schlessinger D.;
"X-linked anhidrotic (hypohidrotic) ectodermal dysplasia is caused by mutation in a novel transmembrane protein.";
Nat. Genet. 13:409-416(1996).
[2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1), AND VARIANTS ED1.
TISSUE=Liver;
DOI=10.1086/301984; PubMed=9683615 [NCBI, ExPASy, EBI, Israel, Japan]
Monreal A.W., Zonana J., Ferguson B.M.;
"Identification of a new splice form of the EDA1 gene permits detection of nearly all X-linked hypohidrotic ectodermal dysplasia mutations.";
Am. J. Hum. Genet. 63:380-389(1998).
[3]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A1; A2; B; C; D; E AND F), AND VARIANTS ED1.
DOI=10.1093/hmg/7.11.1661; PubMed=9736768 [NCBI, ExPASy, EBI, Israel, Japan]
Bayes M., Hartung A.J., Ezer S., Pispa J., Thesleff I., Srivastava A.K., Kere J.;
"The anhidrotic ectodermal dysplasia gene (EDA) undergoes alternative splicing and encodes ectodysplasin-A with deletion mutations in collagenous repeats.";
Hum. Mol. Genet. 7:1661-1669(1998).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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]
 TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
Kobielak K., Kobielak A., Trzciak W.H.;
"Expression of a novel transcript isoform of the EDA gene in human umbilical cord.";
Eur. J. Hum. Genet. Suppl. 7:104-104(1999).
[7]
 RECEPTOR INTERACTION (ISOFORMS A1 AND A2).
DOI=10.1126/science.290.5491.523; PubMed=11039935 [NCBI, ExPASy, EBI, Israel, Japan]
Yan M., Wang L.-C., Hymowitz S.G., Schilbach S., Lee J., Goddard A., de Vos A.M., Gao W.-Q., Dixit V.M.;
"Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors.";
Science 290:523-527(2000).
[8]
 PROTEOLYTIC PROCESSING, MUTAGENESIS OF ARG-153, AND CHARACTERIZATION OF VARIANT HIS-156.
DOI=10.1093/hmg/10.9.953; PubMed=11309369 [NCBI, ExPASy, EBI, Israel, Japan]
Elomaa O., Pulkkinen K., Hannelius U., Mikkola M., Saarialho-Kere U., Kere J.;
"Ectodysplasin is released by proteolytic shedding and binds to the EDAR protein.";
Hum. Mol. Genet. 10:953-962(2001).
[9]
 CHARACTERIZATION OF VARIANTS ED1 CYS-155; CYS-156 AND HIS-156, MUTAGENESIS OF ARG-153; LYS-158 AND ARG-159, AND CLEAVAGE SITE.
DOI=10.1073/pnas.131076098; PubMed=11416205 [NCBI, ExPASy, EBI, Israel, Japan]
Chen Y., Molloy S.S., Thomas L., Gambee J., Baechinger H.P., Ferguson B.M., Zonana J., Thomas G., Morris N.P.;
"Mutations within a furin consensus sequence block proteolytic release of ectodysplasin-A and cause X-linked hypohidrotic ectodermal dysplasia.";
Proc. Natl. Acad. Sci. U.S.A. 98:7218-7223(2001).
[10]
 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 230-391, AND SUBUNIT.
DOI=10.1016/j.str.2003.11.009; PubMed=14656435 [NCBI, ExPASy, EBI, Israel, Japan]
Hymowitz S.G., Compaan D.M., Yan M., Wallweber H.J., Dixit V.M., Starovasnik M.A., de Vos A.M.;
"The crystal structures of EDA-A1 and EDA-A2: splice variants with distinct receptor specificity.";
Structure 11:1513-1520(2003).
[11]
 VARIANT ED1 TYR-54.
PubMed=9630076 [NCBI, ExPASy, EBI, Israel, Japan]
Hertz J.M., Noergaard Hansen K., Juncker I., Kjeldsen M., Gregersen N.;
"A novel missense mutation (402C-->T) in exon 1 in the EDA gene in a family with X-linked hypohidrotic ectodermal dysplasia.";
Clin. Genet. 53:205-209(1998).
[12]
 VARIANT ED1 LYS-63.
PubMed=9507389 [NCBI, ExPASy, EBI, Israel, Japan]
Ferguson B.M., Thomas N.S.T., Munoz F., Morgan D., Clarke A., Zonana J.;
"Scarcity of mutations detected in families with X linked hypohidrotic ectodermal dysplasia: diagnostic implications.";
J. Med. Genet. 35:112-115(1998).
[13]
 VARIANT ED1 ARG-55.
DOI=10.1046/j.1523-1747.1999.00656.x; PubMed=10469321 [NCBI, ExPASy, EBI, Israel, Japan]
Martinez F., Millan J.M., Orellana C., Prieto F.;
"X-linked anhidrotic (hypohidrotic) ectodermal dysplasia caused by a novel mutation in EDA1 gene: 406T > G (Leu55Arg).";
J. Invest. Dermatol. 113:285-286(1999).
[14]
 VARIANT ED1 SER-156.
DOI=10.1046/j.1523-1747.2000.00065-1.x; PubMed=10951256 [NCBI, ExPASy, EBI, Israel, Japan]
Aoki N., Ito K., Tachibana T., Ito M.;
"A novel arginine-->Serine mutation in EDA1 in a Japanese family with X-linked anhidrotic ectodermal dysplasia.";
J. Invest. Dermatol. 115:329-330(2000).
[15]
 VARIANTS ED1 THR-349 AND ASN-360.
DOI=10.1002/ajmg.1225; PubMed=11343303 [NCBI, ExPASy, EBI, Israel, Japan]
Kobielak K., Kobielak A., Roszkiewicz J., Wierzba J., Limon J., Trzeciak W.H.;
"Mutations in the EDA gene in three unrelated families reveal no apparent correlation between phenotype and genotype in the patients with an X-linked anhidrotic ectodermal dysplasia.";
Am. J. Med. Genet. 100:191-197(2001).
[16]
 VARIANTS ED1 ARG-60; TYR-252; VAL-269; SER-302 AND MET-378.
DOI=10.1038/sj.ejhg.5200635; PubMed=11378824 [NCBI, ExPASy, EBI, Israel, Japan]
Vincent M.-C., Biancalana V., Ginisty D., Mandel J.-L., Calvas P.;
"Mutational spectrum of the ED1 gene in X-linked hypohidrotic ectodermal dysplasia.";
Eur. J. Hum. Genet. 9:355-363(2001).
[17]
 VARIANTS ED1 CYS-156; HIS-156; CYS-255; ASP-255; GLY-274; TYR-332 AND THR-349.
DOI=10.1002/humu.33; PubMed=11295832 [NCBI, ExPASy, EBI, Israel, Japan]
Paeaekkoenen K., Cambiaghi S., Novelli G., Ouzts L.V., Penttinen M., Kere J., Srivastava A.K.;
"The mutation spectrum of the EDA gene in X-linked anhidrotic ectodermal dysplasia.";
Hum. Mutat. 17:349-349(2001).
[18]
 VARIANTS ED1 CYS-153; CYS-155; CYS-156; HIS-156; ASN-158; 183-GLY--PRO-194 DEL; 185-ASN--PRO-196 DEL; GLU-189; 191-PRO--PRO-196 DEL; ARG-207; ASP-218; 218-GLY--PRO-223 DEL; ARG-291; SER-299; CYS-320; CYS-343; ARG-374; PRO-378 AND MET-378.
DOI=10.1074/jbc.M101280200; PubMed=11279189 [NCBI, ExPASy, EBI, Israel, Japan]
Schneider P., Street S.L., Gaide O., Hertig S., Tardivel A., Tschopp J., Runkel L., Alevizopoulos K., Ferguson B.M., Zonana J.;
"Mutations leading to X-linked hypohidrotic ectodermal dysplasia affect three major functional domains in the tumor necrosis factor family member ectodysplasin-A.";
J. Biol. Chem. 276:18819-18827(2001).
[19]
 VARIANTS ED1 ALA-198 AND MET-378.
DOI=10.1001/archderm.138.9.1256; PubMed=12225002 [NCBI, ExPASy, EBI, Israel, Japan]
Vincent M.-C., Cossee M., Vabres P., Stewart F., Bonneau D., Calvas P.;
"Pitfalls in clinical diagnosis of female carriers of X-linked hypohidrotic ectodermal dysplasia.";
Arch. Dermatol. 138:1256-1258(2002).
[20]
 VARIANT ED1 HIS-306.
DOI=10.1046/j.1365-2133.2003.05480.x; PubMed=12932274 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu M.M.L., Chao S.C., Lu A.C.H.;
"A novel missense mutation (Gln306His) in exon 7 of the ED1 gene causing anhidrotic ectodermal dysplasia with prominent milia-like facial sebaceous papules.";
Br. J. Dermatol. 149:443-445(2003).
[21]
 VARIANT HYPODONTIA GLY-65.
DOI=10.1007/s10038-006-0389-2; PubMed=16583127 [NCBI, ExPASy, EBI, Israel, Japan]
Tao R., Jin B., Guo S.Z., Qing W., Feng G.Y., Brooks D.G., Liu L., Xu J., Li T., Yan Y., He L.;
"A novel missense mutation of the EDA gene in a Mongolian family with congenital hypodontia.";
J. Hum. Genet. 51:498-502(2006).
[22]
 VARIANT [LARGE SCALE ANALYSIS] LEU-118.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
[23]
 VARIANT ED1 GLU-358.
DOI=10.1002/ajmg.a.31567; PubMed=17256800 [NCBI, ExPASy, EBI, Israel, Japan]
Tarpey P., Pemberton T.J., Stockton D.W., Das P., Ninis V., Edkins S., Andrew Futreal P., Wooster R., Kamath S., Nayak R., Stratton M.R., Patel P.I.;
"A novel Gln358Glu mutation in ectodysplasin A associated with X-linked dominant incisor hypodontia.";
Am. J. Med. Genet. A 143:390-394(2007).
[24]
 VARIANTS ED1 CYS-155; CYS-156; HIS-156; 183-GLY--PRO-194 DEL; 184-PRO--GLY-189 DEL; 185-ASN--PRO-196 DEL; ARG-291; TYR-298; GLY-307; ASP-372 AND ILE-373.
DOI=10.1038/sj.ejhg.5202012; PubMed=18231121 [NCBI, ExPASy, EBI, Israel, Japan]
van der Hout A.H., Oudesluijs G.G., Venema A., Verheij J.B.G.M., Mol B.G.J., Rump P., Brunner H.G., Vos Y.J., van Essen A.J.;
"Mutation screening of the ectodysplasin-A receptor gene EDAR in hypohidrotic ectodermal dysplasia.";
Eur. J. Hum. Genet. 16:673-679(2008).
Comments
  • FUNCTION: Seems to be involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Isoform A1 binds only to the receptor EDAR, while isoform A2 binds exclusively to the receptor XEDAR.
  • SUBUNIT: Homotrimer. The homotrimers may then dimerize and form higher order oligomers.
  • INTERACTION:
    Q9UNE0:EDAR; NbExp=1; IntAct=EBI-529425, EBI-529289;
  • SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.
  • SUBCELLULAR LOCATION: Ectodysplasin-A, secreted form: Secreted.
  • ALTERNATIVE PRODUCTS: 8 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.
    NameA1
    SynonymsII
    Isoform IDQ92838-1
    This is the isoform sequence displayed in this entry.
    NameI
    Isoform IDQ92838-2
    Features which should be applied to build the isoform sequence: VSP_006454, VSP_006455.
    NameA2
    Isoform IDQ92838-3
    Features which should be applied to build the isoform sequence: VSP_006464.
    NameB
    Isoform IDQ92838-4
    Features which should be applied to build the isoform sequence: VSP_006462, VSP_006463.
    NameC
    Isoform IDQ92838-5
    Features which should be applied to build the isoform sequence: VSP_006458, VSP_006461.
    NameD
    Isoform IDQ92838-6
    Features which should be applied to build the isoform sequence: VSP_006456, VSP_006457.
    NameE
    Isoform IDQ92838-7
    Features which should be applied to build the isoform sequence: VSP_006459, VSP_006461.
    NameF
    Isoform IDQ92838-8
    Features which should be applied to build the isoform sequence: VSP_006460, VSP_006461.
  • TISSUE SPECIFICITY: Not abundant; expressed in specific cell types of ectodermal (but not mesodermal) origin of keratinocytes, hair follicles, sweat glands. Also in adult heart, liver, muscle, pancreas, prostate, fetal liver, uterus, small intestine and umbilical chord.
  • PTM: N-glycosylated.
  • PTM: Processing by furin produces a secreted form.
  • DISEASE: Defects in EDA are the cause of ectodermal dysplasia, type 1 (ED1) [MIM:305100]; also known as Christ-Siemens-Touraine syndrome or X-linked hypohidrotic ectodermal dysplasia (XLHED). Ectodermal dysplasia defines a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. ED1 is a disease characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands. ED1 is the most common form of over 150 clinically distinct ectodermal dysplasias.
  • DISEASE: Defects in EDA are a cause of hypodontia [MIM:300606]. Hypodontia is agenesis of two or more permanent teeth without associated systemic disorders. Hypodontia due to EDA defects is an X-linked recessive disorder. Affected individuals have normal hair, skin, and nails, but lack primary and permanent teeth.
  • SIMILARITY: Belongs to the tumor necrosis factor family.
  • SIMILARITY: Contains 1 collagen-like domain.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=EDA";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U59227; AAC50678.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U59228; AAC50679.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061189; AAC77371.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061190; AAC77372.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061191; AAC77373.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061192; AAC77374.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061193; AAC77375.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061194; AAC77376.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060999; AAC36302.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060998; AAC36303.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060992; AAC36303.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060993; AAC36303.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060994; AAC36303.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060995; AAC36303.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060996; AAC36303.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060997; AAC36303.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF040628; AAC77363.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158141; CAI40385.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL450449; CAI40385.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158069; CAI40385.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158141; CAM17680.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158069; CAM17680.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL450449; CAM17680.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL450449; CAI39805.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158069; CAI39805.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL450449; CAI39806.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158069; CAI39806.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158141; CAI39806.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL450449; CAM14498.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158069; CAM14498.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158141; CAM14498.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158069; CAI41611.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL450449; CAI41611.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158069; CAI41612.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158141; CAI41612.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL450449; CAI41612.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158069; CAM24742.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL158141; CAM24742.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL450449; CAM24742.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC126143; AAI26144.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00023765; -.
IPI00216144; -.
IPI00216145; -.
IPI00216146; -.
IPI00216147; -.
IPI00216148; -.
IPI00216149; -.
IPI00216150; -.
RefSeq NP_001005609.1; -.
NP_001005610.1; -.
NP_001005611.1; -.
NP_001005612.1; -.
NP_001005615.1; -.
NP_001390.1; -.
UniGene Hs.105407
3D structure databases
PDB
1RJ7; X-ray; 2.30 A; A/B/D/E/F/G/H/I/J/K/L/M=233-391.[ExPASy / RCSB / EBI]
1RJ8; X-ray; 2.23 A; A/B/D/E/F/G=230-391.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1RJ7; -.
1RJ8; -.
DisProt DP00460; -.
ModBase Q92838.
Protein-protein interaction databases
IntAct Q92838; 1.
PTM databases
PhosphoSite Q92838; -.
Organism-specific databases
GeneCards GC0XP068752; -.
H-InvDB HIX0056123; -.
HGNC HGNC:3157; EDA.
GenAtlas EDA.
HPA CAB012644; -.
MIM 300451; gene. [NCBI / EBI]
300606; phenotype. [NCBI / EBI]
305100; phenotype. [NCBI / EBI]
Orphanet 181; Christ-Siemens-Touraine syndrome.
2227; Hypodontia.
PharmGKB PA27601; -.
Gene expression databases
ArrayExpress Q92838; -.
Bgee Q92838; -.
GermOnline ENSG00000158813; Homo sapiens.
Ontologies
GO
GO:0005856; Cellular component: cytoskeleton (traceable author statement from ProtInc).
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0016021; Cellular component: integral to membrane (traceable author statement from ProtInc).
GO:0005624; Cellular component: membrane fraction (traceable author statement from ProtInc).
GO:0005886; Cellular component: plasma membrane (traceable author statement from ProtInc).
GO:0005164; Molecular function: tumor necrosis factor receptor binding (inferred from electronic annotation from InterPro).
GO:0030154; Biological process: cell differentiation (inferred from electronic annotation from UniProtKB-KW).
GO:0007398; Biological process: ectoderm development (traceable author statement from ProtInc).
GO:0006955; Biological process: immune response (inferred from electronic annotation from InterPro).
GO:0051092; Biological process: positive regulation of NF-kappaB transcription factor activity (inferred from direct assay from HGNC).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR008160; Collagen.
IPR006052; TNF_family.
IPR008983; Tumour_necrosis_fac-like.
Graphical view of domain structure.
Gene3D G3DSA:2.60.120.40; Tumour_necrosis_fac-like; 1.
Pfam PF01391; Collagen; 1.
PF00229; TNF; 1.
Pfam graphical view of domain structure.
SMART SM00207; TNF; 1.
SMART graphical view of domain structure.
PROSITE PS00251; TNF_1; FALSE_NEG.
PS50049; TNF_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q92838; -.
Genome annotation databases
Ensembl ENSG00000158813; Homo sapiens. [Contig view]
GeneID 1896; -.
KEGG hsa:1896; -.
Phylogenomic databases
HOVERGEN Q92838; -.
OMA Q92838; TLPPDSQ.
Other
NextBio 7729; -.
PMAP-CutDB Q92838; -.
SOURCE EDA; Homo sapiens.
ProtoNet Q92838.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cell membrane; Cleavage on pair of basic residues; Collagen; Developmental protein; Differentiation; Disease mutation; Ectodermal dysplasia; Glycoprotein; Membrane; Polymorphism; Secreted; Signal-anchor; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   391  391     Ectodysplasin-A, membrane form. PRO_0000034538
CHAIN   160   391  232     Ectodysplasin-A, secreted form. PRO_0000034539
TOPO_DOM   1    41  41     Cytoplasmic (Potential). 
TRANSMEM   42    62  21     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   63   391  329     Extracellular (Potential). 
DOMAIN   180   229  50     Collagen-like. 
SITE   159   160  2     Cleavage; by furin. 
CARBOHYD   313   313        N-linked (GlcNAc...) (Potential). 
CARBOHYD   372   372        N-linked (GlcNAc...) (Potential). 
VAR_SEQ   133   147        MALLNFFFPDEKPYS -> VSHLVGAAAAPSPRG (in isoform C). VSP_006458
VAR_SEQ   133   147        MALLNFFFPDEKPYS -> DFDYIISFSYGLQGFC (in isoform E). VSP_006459
VAR_SEQ   133   147        MALLNFFFPDEKPYS -> LHVSFSLRKKKAGHQ (in isoform F). VSP_006460
VAR_SEQ   133   142        MALLNFFFPD -> ACFPQVLLSL (in isoform D). VSP_006456
VAR_SEQ   133   135        MAL -> GHQ (in isoform I). VSP_006454
VAR_SEQ   136   391        Missing (in isoform I). VSP_006455
VAR_SEQ   143   391        Missing (in isoform D). VSP_006457
VAR_SEQ   148   391        Missing (in isoform C, isoform E and isoform F). VSP_006461
VAR_SEQ   169   178        PVKNKKKGKK -> KSTQLILYHF (in isoform B). VSP_006462
VAR_SEQ   179   391        Missing (in isoform B). VSP_006463
VAR_SEQ   307   308        Missing (in isoform A2). VSP_006464
VARIANT   54    54  1     H -> Y (in ED1). VAR_010611 
VARIANT   55    55  1     L -> R (in ED1). VAR_010612 
VARIANT   60    60  1     C -> R (in ED1). VAR_013484 
VARIANT   61    61  1     Y -> H (in ED1). VAR_005179 
VARIANT   63    63  1     E -> K (in ED1). VAR_005180 
VARIANT   65    65  1     R -> G (in hypodontia). VAR_029534 
VARIANT   69    69  1     R -> L (in ED1). VAR_005181 
VARIANT   118   118  1     P -> L (in a colorectal cancer sample; somatic mutation). VAR_036590 
VARIANT   153   153  1     R -> C (in ED1). VAR_054454 
VARIANT   155   155  1     R -> C (in ED1; abolishes proteolytic processing). VAR_005182 
VARIANT   156   156  1     R -> C (in ED1; abolishes proteolytic processing). VAR_005183 
VARIANT   156   156  1     R -> H (in ED1; abolishes proteolytic processing). VAR_005184 
VARIANT   156   156  1     R -> S (in ED1). VAR_054455 
VARIANT   158   158  1     K -> N (in ED1). VAR_054456 
VARIANT   183   194  12     Missing (in ED1). VAR_054457
VARIANT   184   189  6     Missing (in ED1). VAR_054458
VARIANT   185   196  12     Missing (in ED1). VAR_054459
VARIANT   189   189  1     G -> E (in ED1). VAR_054460 
VARIANT   191   196  6     Missing (in ED1). VAR_054461
VARIANT   198   198  1     G -> A (in ED1). VAR_054462 
VARIANT   207   207  1     G -> R (in ED1). VAR_054463 
VARIANT   209   209  1     P -> L (in ED1). VAR_005185 
VARIANT   218   223  6     Missing (in ED1). VAR_054465
VARIANT   218   218  1     G -> D (in ED1). VAR_054464 
VARIANT   224   224  1     G -> A (in ED1). VAR_005186 
VARIANT   252   252  1     H -> L (in ED1). VAR_005187 [3D]
VARIANT   252   252  1     H -> Y (in ED1). VAR_013485 [3D]
VARIANT   255   255  1     G -> C (in ED1). VAR_011077 [3D]
VARIANT   255   255  1     G -> D (in ED1; mild). VAR_011078 [3D]
VARIANT   269   269  1     G -> V (in ED1). VAR_013486 [3D]
VARIANT   274   274  1     W -> G (in ED1). VAR_011079 [3D]
VARIANT   291   291  1     G -> R (in ED1). VAR_010613 [3D]
VARIANT   291   291  1     G -> W (in ED1). VAR_010614 [3D]
VARIANT   298   298  1     D -> H (in ED1). VAR_010615 [3D]
VARIANT   298   298  1     D -> Y (in ED1). VAR_054466 [3D]
VARIANT   299   299  1     G -> S (in ED1). VAR_005188 [3D]
VARIANT   302   302  1     F -> S (in ED1). VAR_013487 [3D]
VARIANT   306   306  1     Q -> H (in ED1). VAR_054467 [3D]
VARIANT   307   307  1     V -> G (in ED1). VAR_054468 [3D]
VARIANT   320   320  1     Y -> C (in ED1). VAR_054469 [3D]
VARIANT   332   332  1     C -> Y (in ED1). VAR_011080 [3D]
VARIANT   343   343  1     Y -> C (in ED1). VAR_054470 [3D]
VARIANT   349   349  1     A -> T (in ED1). VAR_005189 [3D]
VARIANT   356   356  1     A -> D (in ED1). VAR_005190 [3D]
VARIANT   357   357  1     R -> P (in ED1). VAR_005191 [3D]
VARIANT   358   358  1     Q -> E (in ED1). VAR_054471 [3D]
VARIANT   360   360  1     I -> N (in ED1). VAR_054472 [3D]
VARIANT   372   372  1     N -> D (in ED1). VAR_054473 [3D]
VARIANT   373   373  1     M -> I (in ED1). VAR_054474 [3D]
VARIANT   374   374  1     S -> R (in ED1). VAR_054475 [3D]
VARIANT   378   378  1     T -> M (in ED1). VAR_013488 [3D]
VARIANT   378   378  1     T -> P (in ED1). VAR_054476 [3D]
MUTAGEN   153   153        R->C: Abolishes proteolytic processing. 
MUTAGEN   158   158        K->N: Abolishes proteolytic processing. 
MUTAGEN   159   159        R->A: Abolishes proteolytic processing. 
STRAND   249   255  7      
HELIX   262   265  4      
STRAND   274   279  6      
TURN   281   283  3      
STRAND   284   287  4      
TURN   288   291  4      
STRAND   292   297  6      
STRAND   299   314  16      
STRAND   318   324  7      
STRAND   327   334  8      
STRAND   338   340  3      
STRAND   344   354  11      
STRAND   359   364  6      
STRAND   366   372  7      
TURN   375   377  3      
STRAND   378   386  9      
Sequence information
Length: 391 AA [This is the length of the unprocessed precursor] Molecular weight: 41294 Da [This is the MW of the unprocessed precursor] CRC64: 15DB3F5053293CBA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGYPEVERRE LLPAAAPRER GSQGCGCGGA PARAGEGNSC LLFLGFFGLS LALHLLTLCC 

        70         80         90        100        110        120 
YLELRSELRR ERGAESRLGG SGTPGTSGTL SSLGGLDPDS PITSHLGQPS PKQQPLEPGE 

       130        140        150        160        170        180 
AALHSDSQDG HQMALLNFFF PDEKPYSEEE SRRVRRNKRS KSNEGADGPV KNKKKGKKAG 

       190        200        210        220        230        240 
PPGPNGPPGP PGPPGPQGPP GIPGIPGIPG TTVMGPPGPP GPPGPQGPPG LQGPSGAADK 

       250        260        270        280        290        300 
AGTRENQPAV VHLQGQGSAI QVKNDLSGGV LNDWSRITMN PKVFKLHPRS GELEVLVDGT 

       310        320        330        340        350        360 
YFIYSQVEVY YINFTDFASY EVVVDEKPFL QCTRSIETGK TNYNTCYTAG VCLLKARQKI 

       370        380        390 
AVKMVHADIS INMSKHTTFF GAIRLGEAPA S
Q92838 in FASTA format

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