Variant position: 153 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 391 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human MALLNFFFPDEKPYSEEESR RVRRNKRSKSNEGADGPVKNK
Mouse MALLNFFFPDEKAYSEEESR RVRRNKRSKSGEGADGPVKNK
Bovine MALVNFFIPKEKSYSEEESR RVRRNKRSKSSEGADGPVKNK
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 391 Ectodysplasin-A, membrane form
63 – 391 Extracellular
136 – 391 Missing. In isoform 2.
143 – 391 Missing. In isoform 5.
148 – 391 Missing. In isoform 4, isoform 6 and isoform 7.
159 – 159 R -> A. Abolishes proteolytic processing.
Ectodysplasin is released by proteolytic shedding and binds to the EDAR protein.
Elomaa O.; Pulkkinen K.; Hannelius U.; Mikkola M.; Saarialho-Kere U.; Kere J.;
Hum. Mol. Genet. 10:953-962(2001)
Cited for: PROTEOLYTIC PROCESSING; CHARACTERIZATION OF VARIANT XHED CYS-153; CHARACTERIZATION OF VARIANT HIS-156;
Mutations within a furin consensus sequence block proteolytic release of ectodysplasin-A and cause X-linked hypohidrotic ectodermal dysplasia.
Chen Y.; Molloy S.S.; Thomas L.; Gambee J.; Baechinger H.P.; Ferguson B.M.; Zonana J.; Thomas G.; Morris N.P.;
Proc. Natl. Acad. Sci. U.S.A. 98:7218-7223(2001)
Cited for: CHARACTERIZATION OF VARIANTS XHED CYS-153; CYS-155; CYS-156; HIS-156 AND ASN-158; MUTAGENESIS OF ARG-159; CLEAVAGE SITE;
Mutations leading to X-linked hypohidrotic ectodermal dysplasia affect three major functional domains in the tumor necrosis factor family member ectodysplasin-A.
Schneider P.; Street S.L.; Gaide O.; Hertig S.; Tardivel A.; Tschopp J.; Runkel L.; Alevizopoulos K.; Ferguson B.M.; Zonana J.;
J. Biol. Chem. 276:18819-18827(2001)
Cited for: VARIANTS XHED 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;
Identification of mutations in the EDA and EDAR genes in Pakistani families with hypohidrotic ectodermal dysplasia.
Shimomura Y.; Wajid M.; Weiser J.; Kraemer L.; Ishii Y.; Lombillo V.; Bale S.J.; Christiano A.M.;
Clin. Genet. 75:582-584(2009)
Cited for: VARIANTS XHED CYS-153; CYS-155 AND THR-349;
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