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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   03-AUG-2022, entry version 154.
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   -!- 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.ENSGALP00000012809; -.
DR   PaxDb; P02717; -.
DR   PRIDE; P02717; -.
DR   VEuPathDB; HostDB:geneid_424940; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   InParanoid; P02717; -.
DR   OrthoDB; 588360at2759; -.
DR   PhylomeDB; P02717; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IC:ComplexPortal.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 cation-selective channel activity; IBA:GO_Central.
DR   GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0095500; P:acetylcholine receptor signaling pathway; IC:ComplexPortal.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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   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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