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ACHA4_CHICK
ID   ACHA4_CHICK             Reviewed;         622 AA.
AC   P09482;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-4;
DE   Flags: Precursor;
GN   Name=CHRNA4;
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 / MRNA].
RC   STRAIN=White leghorn; TISSUE=Brain;
RX   PubMed=3267226; DOI=10.1002/j.1460-2075.1988.tb02852.x;
RA   Nef P., Oneyser C., Alliod C., Couturier S., Ballivet M.;
RT   "Genes expressed in the brain define three distinct neuronal nicotinic
RT   acetylcholine receptors.";
RL   EMBO J. 7:595-601(1988).
RN   [2]
RP   MUTAGENESIS OF GLU-289, AND SUBUNIT.
RX   PubMed=2005979; DOI=10.1038/350235a0;
RA   Cooper E., Couturier S., Ballivet M.;
RT   "Pentameric structure and subunit stoichiometry of a neuronal nicotinic
RT   acetylcholine receptor.";
RL   Nature 350:235-238(1991).
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: Neuronal AChR seems to be composed of two different type of
CC       subunits: alpha and non-alpha (also called beta). A functional receptor
CC       seems to consist of two alpha-chains and three non-alpha chains.
CC       {ECO:0000269|PubMed:2005979}.
CC   -!- INTERACTION:
CC       P09482; P09484: CHRNB2; NbExp=7; IntAct=EBI-10686088, EBI-10686072;
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein. Cell membrane
CC       {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-4/CHRNA4 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X07348; CAA30285.1; -; Genomic_DNA.
DR   EMBL; X07349; CAA30285.1; JOINED; Genomic_DNA.
DR   EMBL; X07350; CAA30285.1; JOINED; Genomic_DNA.
DR   EMBL; X07351; CAA30285.1; JOINED; Genomic_DNA.
DR   EMBL; X07352; CAA30285.1; JOINED; Genomic_DNA.
DR   EMBL; X07399; CAA30285.1; JOINED; Genomic_DNA.
DR   EMBL; AJ250361; CAB59626.1; -; mRNA.
DR   PIR; S00379; ACCH4N.
DR   RefSeq; NP_990145.1; NM_204814.1.
DR   AlphaFoldDB; P09482; -.
DR   SMR; P09482; -.
DR   ComplexPortal; CPX-172; Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2.
DR   ComplexPortal; CPX-173; Neuronal nicotinic acetylcholine receptor complex, 2xalpha4-3xbeta2.
DR   ComplexPortal; CPX-217; Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2.
DR   ComplexPortal; CPX-221; Neuronal nicotinic acetylcholine receptor complex, alpha4-beta4.
DR   IntAct; P09482; 1.
DR   STRING; 9031.ENSGALP00000009302; -.
DR   BindingDB; P09482; -.
DR   ChEMBL; CHEMBL5569; -.
DR   DrugCentral; P09482; -.
DR   PaxDb; P09482; -.
DR   Ensembl; ENSGALT00000009316; ENSGALP00000009302; ENSGALG00000005801.
DR   GeneID; 395606; -.
DR   KEGG; gga:395606; -.
DR   CTD; 1137; -.
DR   VEuPathDB; HostDB:geneid_395606; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000159329; -.
DR   HOGENOM; CLU_018074_1_1_1; -.
DR   InParanoid; P09482; -.
DR   OMA; IFPAFGH; -.
DR   OrthoDB; 381858at2759; -.
DR   PhylomeDB; P09482; -.
DR   TreeFam; TF315605; -.
DR   PRO; PR:P09482; -.
DR   Proteomes; UP000000539; Chromosome 20.
DR   Bgee; ENSGALG00000005801; Expressed in brain and 3 other tissues.
DR   ExpressionAtlas; P09482; baseline and differential.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IPI: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:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
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:0035094; P:response to nicotine; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; 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   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..23
FT   CHAIN           24..622
FT                   /note="Neuronal acetylcholine receptor subunit alpha-4"
FT                   /id="PRO_0000000355"
FT   TOPO_DOM        24..237
FT                   /note="Extracellular"
FT   TRANSMEM        238..262
FT                   /note="Helical"
FT   TRANSMEM        270..288
FT                   /note="Helical"
FT   TRANSMEM        304..325
FT                   /note="Helical"
FT   TOPO_DOM        326..595
FT                   /note="Cytoplasmic"
FT   TRANSMEM        596..614
FT                   /note="Helical"
FT   REGION          380..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           266
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        156..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        220..221
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         289
FT                   /note="E->K: Reduces channel conductance by 50%."
FT                   /evidence="ECO:0000269|PubMed:2005979"
SQ   SEQUENCE   622 AA;  70838 MW;  290B035893D6485A CRC64;
     MGFLVSKGNL LLLLCASIFP AFGHVETRAH AEERLLKKLF SGYNKWSRPV ANISDVVLVR
     FGLSIAQLID VDEKNQMMTT NVWVKQEWHD YKLRWDPQEY ENVTSIRIPS ELIWRPDIVL
     YNNADGDFAV THLTKAHLFY DGRIKWMPPA IYKSSCSIDV TFFPFDQQNC KMKFGSWTYD
     KAKIDLVSMH SHVDQLDYWE SGEWVIINAV GNYNSKKYEC CTEIYPDITY SFIIRRLPLF
     YTINLIIPCL LISCLTVLVF YLPSECGEKI TLCISVLLSL TVFLLLITEI IPSTSLVIPL
     IGEYLLFTMI FVTLSIIITV FVLNVHHRSP RTHTMPDWVR RVFLDIVPRL LFMKRPSTVK
     DNCKKLIESM HKLTNSPRLW SETDMEPNFT TSSSPSPQSN EPSPTSSFCA HLEEPAKPMC
     KSPSGQYSML HPEPPQVTCS SPKPSCHPLS DTQTTSISKG RSLSVQQMYS PNKTEEGSIR
     CRSRSIQYCY LQEDSSQTNG HSSASPASQR CHLNEEQPQH KPHQCKCKCR KGEAAGTPTQ
     GSKSHSNKGE HLVLMSPALK LAVEGVHYIA DHLRAEDADF SVKEDWKYVA MVIDRIFLWM
     FIIVCLLGTV GLFLPPWLAG MI
 
 
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