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Database: UniProt
Entry: ACHD_CHICK
LinkDB: ACHD_CHICK
Original site: ACHD_CHICK 
ID   ACHD_CHICK              Reviewed;         513 AA.
AC   P02717;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Acetylcholine receptor subunit delta;
DE   Flags: Precursor;
GN   Name=CHRND;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6096871; DOI=10.1073/pnas.81.24.7975;
RA   Nef P., Mauron A., Stalder R., Alliod C., Ballivet M.;
RT   "Structure linkage, and sequence of the two genes encoding the delta and
RT   gamma subunits of the nicotinic acetylcholine receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:7975-7979(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX   PubMed=2311580; DOI=10.1002/j.1460-2075.1990.tb08174.x;
RA   Wang X.M., Tsay H.J., Schmidt J.;
RT   "Expression of the acetylcholine receptor delta-subunit gene in
RT   differentiating chick muscle cells is activated by an element that contains
RT   two 16 bp copies of a segment of the alpha-subunit enhancer.";
RL   EMBO J. 9:783-790(1990).
CC   -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and leads to
CC       opening of an ion-conducting channel across the plasma membrane.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:P04759};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P04759};
CC   -!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta,
CC       and gamma chains.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. {ECO:0000305}.
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DR   EMBL; K02903; AAB59944.1; -; Genomic_DNA.
DR   EMBL; X52010; CAA36259.1; -; Genomic_DNA.
DR   PIR; A03176; ACCHD1.
DR   AlphaFoldDB; P02717; -.
DR   SMR; P02717; -.
DR   ComplexPortal; CPX-254; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma.
DR   STRING; 9031.ENSGALP00000054388; -.
DR   GlyCosmos; P02717; 2 sites, No reported glycans.
DR   PaxDb; 9031-ENSGALP00000012809; -.
DR   VEuPathDB; HostDB:geneid_424940; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   InParanoid; P02717; -.
DR   PhylomeDB; P02717; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   CDD; cd19028; LGIC_ECD_nAChR_D; 1.
DR   CDD; cd19064; LGIC_TM_nAChR; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 2.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF61; ACETYLCHOLINE RECEPTOR SUBUNIT DELTA; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..18
FT   CHAIN           19..513
FT                   /note="Acetylcholine receptor subunit delta"
FT                   /id="PRO_0000000325"
FT   TOPO_DOM        19..244
FT                   /note="Extracellular"
FT   TRANSMEM        245..269
FT                   /note="Helical"
FT   TRANSMEM        277..295
FT                   /note="Helical"
FT   TRANSMEM        311..332
FT                   /note="Helical"
FT   TOPO_DOM        333..467
FT                   /note="Cytoplasmic"
FT   TRANSMEM        468..490
FT                   /note="Helical"
FT   MOD_RES         388
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        148..162
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   513 AA;  59011 MW;  0C35772CC57E12CF CRC64;
     MAVLLALFGA LVLSGGLCVN QEERLIHHLF EERGYNKEVR PVASADEVVD VYLALTLSNL
     ISLKEVDETL TTNVWVEQSW TDYRLQWNTS EFGGVDVLRL LPEMLWLPEI VLENNNDGLF
     EVAYYCNVLV YNTGYVYWLP PAIFRSACPI NVNFFPFDWQ NCTLKFSSLA YNAQEINMHL
     KEESDPETEK NYRVEWIIID PEGFTENGEW EIIHRPARKN IHPSYPTESS EHQDITFYLI
     IKRKPLFYVI NIVTPCVLIA FMAILVFYLP ADSGEKMTLV ISVLLAQSVF LLLVSQRLPA
     TSHAIPLIGK YLLFIMLLVT AVVVICVVVL NFHFRTPSTH VMSDWVRGVF LEILPRLLHM
     SHPAESPAGA PCIRRCSSAG YIAKAEEYYS VKSRSELMFE KQSERHGLAS RVTPARFAPA
     ATSEEQLYDH LKPTLDEANF IVKHMREKNS YNEEKDNWNR VARTLDRLCL FLITPMLVVG
     TLWIFLMGIY NHPPPLPFSG DPFDYREENK RYI
//
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