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ACHA_RAT
ID   ACHA_RAT                Reviewed;         457 AA.
AC   P25108;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Acetylcholine receptor subunit alpha;
DE   Flags: Precursor;
GN   Name=Chrna1; Synonyms=Acra;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=1702709; DOI=10.1111/j.1432-1033.1990.tb15637.x;
RA   Witzemann V., Stein E., Barg B., Konno T., Koenen M., Kues W., Criado M.,
RA   Hofmann M., Sakmann B.;
RT   "Primary structure and functional expression of the alpha-, beta-, gamma-,
RT   delta- and epsilon-subunits of the acetylcholine receptor from rat
RT   muscle.";
RL   Eur. J. Biochem. 194:437-448(1990).
CC   -!- FUNCTION: Upon acetylcholine binding, the AChR responds by an extensive
CC       change in conformation that affects all subunits and leads to opening
CC       of an ion-conducting channel across the plasma membrane.
CC       {ECO:0000250|UniProtKB:P02708}.
CC   -!- SUBUNIT: One of the alpha chains that assemble within the acetylcholine
CC       receptor, a pentamer of two alpha chains, a beta, a delta, and a gamma
CC       (in immature muscle) or epsilon (in mature muscle) chains. The muscle
CC       heteropentamer composed of alpha-1, beta-1, delta, epsilon subunits
CC       interacts with the alpha-conotoxin ImII.
CC       {ECO:0000250|UniProtKB:P02708}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-1/CHRNA1 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X74832; CAA52826.1; -; mRNA.
DR   PIR; S13872; S13872.
DR   RefSeq; NP_077811.1; NM_024485.1.
DR   AlphaFoldDB; P25108; -.
DR   SMR; P25108; -.
DR   ComplexPortal; CPX-253; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma.
DR   ComplexPortal; CPX-258; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon.
DR   STRING; 10116.ENSRNOP00000024706; -.
DR   BindingDB; P25108; -.
DR   ChEMBL; CHEMBL3885509; -.
DR   ChEMBL; CHEMBL4523658; -.
DR   DrugCentral; P25108; -.
DR   GlyGen; P25108; 1 site.
DR   PhosphoSitePlus; P25108; -.
DR   PaxDb; P25108; -.
DR   PRIDE; P25108; -.
DR   ABCD; P25108; 3 sequenced antibodies.
DR   Ensembl; ENSRNOT00000024706; ENSRNOP00000024706; ENSRNOG00000018286.
DR   GeneID; 79557; -.
DR   KEGG; rno:79557; -.
DR   UCSC; RGD:69277; rat.
DR   CTD; 1134; -.
DR   RGD; 69277; Chrna1.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000156851; -.
DR   HOGENOM; CLU_018074_1_0_1; -.
DR   InParanoid; P25108; -.
DR   OMA; STHIMPE; -.
DR   OrthoDB; 381858at2759; -.
DR   PhylomeDB; P25108; -.
DR   TreeFam; TF315605; -.
DR   Reactome; R-RNO-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   Reactome; R-RNO-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR   PRO; PR:P25108; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000018286; Expressed in esophagus and 5 other tissues.
DR   Genevisible; P25108; RN.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:RGD.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0042166; F:acetylcholine binding; IEA:Ensembl.
DR   GO; GO:0015464; F:acetylcholine receptor activity; IEA:Ensembl.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:RGD.
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:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
DR   GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISO:RGD.
DR   GO; GO:0006812; P:cation transport; IDA:RGD.
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:0046716; P:muscle cell cellular homeostasis; ISO:RGD.
DR   GO; GO:0050881; P:musculoskeletal movement; ISO:RGD.
DR   GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR   GO; GO:0007528; P:neuromuscular junction development; ISO:RGD.
DR   GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; ISO:RGD.
DR   GO; GO:0070050; P:neuron cellular homeostasis; ISO:RGD.
DR   GO; GO:0019228; P:neuronal action potential; ISO:RGD.
DR   GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0003009; P:skeletal muscle contraction; IDA:RGD.
DR   GO; GO:0048630; P:skeletal muscle tissue growth; ISO:RGD.
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; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..457
FT                   /note="Acetylcholine receptor subunit alpha"
FT                   /id="PRO_0000000307"
FT   TOPO_DOM        21..230
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317..428
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..447
FT                   /note="Helical"
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"
FT   DISULFID        212..213
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   457 AA;  51867 MW;  776AE3B8DF8F68F3 CRC64;
     MELTAVLLLL GLCSAGTVLG SEHETRLVAK LFKDYSSVVR PVGDHREIVQ VTVGLQLIQL
     INVDEVNQIV TTNVRLKQQW VDYNLKWNPD DYGGVKKIHI PSEKIWRPDV VLYNNADGDF
     AIVKFTKVLL DYTGHITWTP PAIFKSYCEI IVTHFPFDEQ NCSMKLGTWT YDGSVVAINP
     ESDQPDLSNF MESGEWVIKE ARGWKHWVFY SCCPNTPYLD ITYHFVMQRL PLYFIVNVII
     PCLLFSFLTS LVFYLPTDSG EKMTLSISVL LSLTVFLLVI VELIPSTSSA VPLIGKYMLF
     TMVFVIASII ITVIVINTHH RSPSTHIMPE WVRKVFIDTI PNIMFFSTMK RPSRDKQEKR
     IFTEDIDISD ISGKPGPPPM GFHSPLIKHP EVKSAIEGVK YIAETMKSDQ ESNNASEEWK
     YVAMVMDHIL LGVFMLVCLI GTLAVFAGRL IELHQQG
 
 
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