Primary Information
BoMiProt ID	Bomi5408
Protein Name	Ectodysplasin-A/Ectodermal dysplasia protein Ectodysplasin-1/Ectodermal dysplasia protein Ectodysplasin-1
Organism	Bos taurus
Uniprot ID	Q9BEG5
Milk Fraction	Whey
Ref Sequence ID	NP_001075212.1
Aminoacid Length	391
Molecular Weight	41567
FASTA Sequence	Download
Gene Name	EDA
Gene ID	616179
Protein Existence Status	reviewed
Secondary Information
Protein Function	induction, morphogenesis and/or maintenance of skin-derived structures such as teeth, hair, sweat glands and several other glands.Deficiencies in the EDA - EDA receptor (EDAR) signalling pathway cause hypohidrotic ectodermal dysplasia (HED).
Biochemical Properties	EDA is a 391 amino acid residues-long membrane protein with a short intracellular domain, a transmembrane domain, a stalk region of uncharacterized function, a consensus furin cleavage sequence responsible for proteolytic processing of EDA, a short positively-charged sequence required for interactions with heparan-sulfate proteoglycans, a bi-partite collagen-like domain and a 150 amino acid residues-long C-terminal TNF homology domain (THD) responsible for receptor binding.EDA isoforms (up to nine in mouse keratinocytes), of which only the longest two, EDA1 and EDA2, contain the THD, interact with receptors and are known to be biologically active. EDA1 and EDA2 differ by two amino acid residues in the THD (Glu308 and Val309) as a result of differential usage of a splice donor site at the end of exon 7.
Significance in milk	role in the development of skin,hair,teeth and sweat glands
PTMs	N-glycosylated on Arg
Additional Comments	EDAR agonists may serve to treat certain forms of ectodermal dysplasia.
Linking IDs	Bomi5408
Bibliography	Kowalczyk-Quintas C, Schneider P. Ectodysplasin A (EDA) - EDA receptor signalling and its pharmacological modulation. Cytokine Growth Factor Rev. 2014 Apr;25(2):195-203. doi: 10.1016/j.cytogfr.2014.01.004. Epub 2014 Jan 23. PMID: 24508088.
Protein Function	induction, morphogenesis and/or maintenance of skin-derived structures such as teeth, hair, sweat glands and several other glands.Deficiencies in the EDA - EDA receptor (EDAR) signalling pathway cause hypohidrotic ectodermal dysplasia (HED).
Biochemical Properties	EDA is a 391 amino acid residues-long membrane protein with a short intracellular domain, a transmembrane domain, a stalk region of uncharacterized function, a consensus furin cleavage sequence responsible for proteolytic processing of EDA, a short positively-charged sequence required for interactions with heparan-sulfate proteoglycans, a bi-partite collagen-like domain and a 150 amino acid residues-long C-terminal TNF homology domain (THD) responsible for receptor binding.EDA isoforms (up to nine in mouse keratinocytes), of which only the longest two, EDA1 and EDA2, contain the THD, interact with receptors and are known to be biologically active. EDA1 and EDA2 differ by two amino acid residues in the THD (Glu308 and Val309) as a result of differential usage of a splice donor site at the end of exon 7.
Significance in milk	role in the development of skin,hair,teeth and sweat glands
PTMs	N-glycosylated on Arg
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation	>sp|Q9BEG5|EDA_BOVIN Ectodysplasin-A OS=Bos taurus OX=9913 GN=EDA PE=3 SV=2 MGYPEVERREPLPAAAPRERGSQGCGCRGAPARAGEGNSCRLFLGFFGLSLALHLLTLCC YLELRSELRRERGAESRFSGPGTPGTSGTLSSPGGLDPNGPITRHFGQRSPQQQPLEPGE TTLPPDSQDGHQMALVNFFIPKEKSYSEEESRRVRRNKRSKSSEGADGPVKNKKKGKKAG PPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADK AGTRENQPAVVHLQGQGSAIQVKNDLSGGVLNDWSRITMNPKVFKLHPRSGELEVLVDGT YFIYSQVEVYYIN*313FTDFASYEVVVDEKPFLQCTRSIETGKTNYNTCYTAGVCLLKARQKI AVKMVHADISIN*372MSKHTTFFGAIRLGEAPAS
Predicted Disorder Regions	2 disordered segments; (1-35), (71-248)
DisProt Annotation
TM Helix Prediction	1TMH; (42-64)
Additional Comments	EDAR agonists may serve to treat certain forms of ectodermal dysplasia.
Linking IDs
Bibliography	Kowalczyk-Quintas C, Schneider P. Ectodysplasin A (EDA) - EDA receptor signalling and its pharmacological modulation. Cytokine Growth Factor Rev. 2014 Apr;25(2):195-203. doi: 10.1016/j.cytogfr.2014.01.004. Epub 2014 Jan 23. PMID: 24508088.