ID   ACHD_XENLA              Reviewed;         521 AA.
AC   P09628;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Acetylcholine receptor subunit delta;
DE   Flags: Precursor;
GN   Name=chrnd;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=3339098; DOI=10.1083/jcb.106.2.469;
RA   Baldwin T.J., Yoshihara C.M., Blackmer K., Kintner C.R., Burden S.J.;
RT   "Regulation of acetylcholine receptor transcript expression during
RT   development in Xenopus laevis.";
RL   J. Cell Biol. 106:469-478(1988).
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   -!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta,
CC       and gamma (in immature muscle) or epsilon (in mature muscle) 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; X07069; CAA30105.1; -; mRNA.
DR   PIR; C28529; C28529.
DR   RefSeq; NP_001095267.1; NM_001101797.1.
DR   AlphaFoldDB; P09628; -.
DR   SMR; P09628; -.
DR   GeneID; 444847; -.
DR   KEGG; xla:444847; -.
DR   CTD; 444847; -.
DR   Xenbase; XB-GENE-989980; chrnd.L.
DR   OrthoDB; 588360at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 444847; Expressed in muscle tissue and 3 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   Gene3D; 1.20.58.390; -; 2.
DR   Gene3D; 2.70.170.10; -; 1.
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   PANTHER; PTHR18945; PTHR18945; 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; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   2: Evidence at transcript level;
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..21
FT   CHAIN           22..521
FT                   /note="Acetylcholine receptor subunit delta"
FT                   /id="PRO_0000000327"
FT   TOPO_DOM        22..247
FT                   /note="Extracellular"
FT   TRANSMEM        248..272
FT                   /note="Helical"
FT   TRANSMEM        280..297
FT                   /note="Helical"
FT   TRANSMEM        314..335
FT                   /note="Helical"
FT   TOPO_DOM        336..475
FT                   /note="Cytoplasmic"
FT   TRANSMEM        476..494
FT                   /note="Helical"
FT   MOD_RES         394
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        151..165
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   521 AA;  60256 MW;  5D6FA9DB407791B2 CRC64;
     MAWIWISLLL PILIYFPGCF SESEEERLLN HIFVERGYRK ELRPVEHTGE TVNVSLALTL
     SNLISLKEAD ETLTTNVWVE LAWYDKRLAW DMETYNNIDI LRVPPDMVWQ PQLILENNNN
     GVFEVAYYSN VLISSDGFMY WLPPAIFQTS CSINVNYFPF DWQNCSLKFS SLTYNAKEIN
     LQLRQDLDEA SQRYYPVEWI IIDPEGFTEN GEWEIVHIPA KKNIDRSLSP ESTKYQDITF
     YLIIERKPLF YIINILAPCV LIALMANLVF YLPADSGEKM TLAISVLLAQ SVFLLLISQR
     LPETSFAIPL ISKYLMFIMV LVTIVVVSCV IVLNLHFRTP STHAISERMK EIFLNKLPRI
     LHMSQPAEPE PEPWSGVLLR RSSSVGYIVK AEEYYSVKSR SELMFEKQSE RHGLTSRATP
     ARVNPLNANN SQDQLYGEIK PAIDGANFIV KHIRDKNDYN EEKDNWYRIA RTVDRLCLFL
     VTPVMIIGTL WIFLGGAYNL PPSLPFPGDP FIYTKEHRRL I