ID   EDA_BOVIN               Reviewed;         391 AA.
AC   Q9BEG5; Q9BEG6;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Ectodysplasin-A;
DE   AltName: Full=Ectodermal dysplasia protein;
DE   AltName: Full=Ectodysplasin-1;
DE   Contains:
DE     RecName: Full=Ectodysplasin-A, membrane form;
DE   Contains:
DE     RecName: Full=Ectodysplasin-A, secreted form;
GN   Name=EDA; Synonyms=ED1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A1 AND A2).
RC   STRAIN=Holstein;
RX   PubMed=11167539; DOI=10.1046/j.1365-2052.2000.00693.x;
RA   Droegemueller C., Distl O., Leeb T.;
RT   "Identification of a highly polymorphic microsatellite within the bovine
RT   ectodysplasin A (ED1) gene on BTA Xq22-24.";
RL   Anim. Genet. 31:416-416(2000).
CC   -!- FUNCTION: Cytokine which is involved in epithelial-mesenchymal
CC       signaling during morphogenesis of ectodermal organs. Functions as a
CC       ligand activating the DEATH-domain containing receptors EDAR and EDA2R.
CC       Isoform A1 binds only to the receptor EDAR, while isoform A2 binds
CC       exclusively to the receptor EDA2R. May also play a role in cell
CC       adhesion. {ECO:0000250|UniProtKB:O54693, ECO:0000250|UniProtKB:Q92838}.
CC   -!- FUNCTION: Isoform A1 binds only to the receptor EDAR, while isoform A2
CC       binds exclusively to the receptor EDA2R.
CC       {ECO:0000250|UniProtKB:Q92838}.
CC   -!- FUNCTION: Isoform A2 binds exclusively to the receptor EDA2R.
CC       {ECO:0000250|UniProtKB:Q92838}.
CC   -!- SUBUNIT: Homotrimer. The homotrimers may then dimerize and form higher-
CC       order oligomers. {ECO:0000250|UniProtKB:Q92838}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O54693};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:O54693}.
CC   -!- SUBCELLULAR LOCATION: [Ectodysplasin-A, secreted form]: Secreted
CC       {ECO:0000250|UniProtKB:Q92838}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=A1;
CC         IsoId=Q9BEG5-1; Sequence=Displayed;
CC       Name=A2;
CC         IsoId=Q9BEG5-2; Sequence=VSP_006453;
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O54693}.
CC   -!- PTM: Processing by furin produces a secreted form.
CC       {ECO:0000250|UniProtKB:Q92838}.
CC   -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR   EMBL; AJ300468; CAC29151.1; -; Genomic_DNA.
DR   EMBL; AJ300469; CAC29151.1; JOINED; Genomic_DNA.
DR   EMBL; AJ278907; CAC29151.1; JOINED; Genomic_DNA.
DR   EMBL; AJ300468; CAC29152.1; -; Genomic_DNA.
DR   EMBL; AJ300469; CAC29152.1; JOINED; Genomic_DNA.
DR   EMBL; AJ278907; CAC29152.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_001075212.1; NM_001081743.2. [Q9BEG5-1]
DR   RefSeq; XP_005228089.1; XM_005228032.3. [Q9BEG5-2]
DR   AlphaFoldDB; Q9BEG5; -.
DR   SMR; Q9BEG5; -.
DR   STRING; 9913.ENSBTAP00000016649; -.
DR   PaxDb; Q9BEG5; -.
DR   GeneID; 616179; -.
DR   KEGG; bta:616179; -.
DR   CTD; 1896; -.
DR   eggNOG; ENOG502QUAV; Eukaryota.
DR   HOGENOM; CLU_062448_0_0_1; -.
DR   InParanoid; Q9BEG5; -.
DR   OrthoDB; 1183050at2759; -.
DR   TreeFam; TF332099; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0038177; F:death receptor agonist activity; ISS:UniProtKB.
DR   GO; GO:0005123; F:death receptor binding; ISS:UniProtKB.
DR   GO; GO:0048018; F:receptor ligand activity; IBA:GO_Central.
DR   GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR   GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISS:UniProtKB.
DR   GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR   CDD; cd00184; TNF; 1.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR006052; TNF_dom.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   Pfam; PF00229; TNF; 1.
DR   SUPFAM; SSF49842; SSF49842; 1.
DR   PROSITE; PS50049; TNF_2; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Cell membrane; Cleavage on pair of basic residues;
KW   Collagen; Developmental protein; Differentiation; Glycoprotein; Membrane;
KW   Reference proteome; Secreted; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..391
FT                   /note="Ectodysplasin-A, membrane form"
FT                   /id="PRO_0000034536"
FT   CHAIN           160..391
FT                   /note="Ectodysplasin-A, secreted form"
FT                   /evidence="ECO:0000250|UniProtKB:Q92838"
FT                   /id="PRO_0000034537"
FT   TOPO_DOM        1..41
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        63..391
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          180..229
FT                   /note="Collagen-like"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..230
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            159..160
FT                   /note="Cleavage; by furin"
FT                   /evidence="ECO:0000250|UniProtKB:Q92838"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         307..308
FT                   /note="Missing (in isoform A2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006453"
SQ   SEQUENCE   391 AA;  41567 MW;  1F87AD67A04EB7AA CRC64;
     MGYPEVERRE PLPAAAPRER GSQGCGCRGA PARAGEGNSC RLFLGFFGLS LALHLLTLCC
     YLELRSELRR ERGAESRFSG PGTPGTSGTL SSPGGLDPNG PITRHFGQRS PQQQPLEPGE
     TTLPPDSQDG HQMALVNFFI PKEKSYSEEE SRRVRRNKRS KSSEGADGPV KNKKKGKKAG
     PPGPNGPPGP PGPPGPQGPP GIPGIPGIPG TTVMGPPGPP GPPGPQGPPG LQGPSGAADK
     AGTRENQPAV VHLQGQGSAI QVKNDLSGGV LNDWSRITMN PKVFKLHPRS GELEVLVDGT
     YFIYSQVEVY YINFTDFASY EVVVDEKPFL QCTRSIETGK TNYNTCYTAG VCLLKARQKI
     AVKMVHADIS INMSKHTTFF GAIRLGEAPA S