位置:首页 > 蛋白库 > ACHA6_CHICK
ACHA6_CHICK
ID   ACHA6_CHICK             Reviewed;         494 AA.
AC   P49581; Q90709;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-6;
DE   Flags: Precursor;
GN   Name=CHRNA6;
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 [MRNA].
RC   STRAIN=White leghorn;
RA   Alliod C., Ballivet M.;
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9203638; DOI=10.1124/mol.51.2.320;
RA   Gerzanich V., Kuryatov A., Anand R., Lindstrom J.;
RT   "'Orphan' alpha6 nicotinic AChR subunit can form a functional heteromeric
RT   acetylcholine receptor.";
RL   Mol. Pharmacol. 51:320-327(1997).
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   -!- 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. Alpha-6/CHRNA6 sub-
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X83889; CAA58766.1; -; mRNA.
DR   EMBL; U48860; AAA92122.1; -; mRNA.
DR   PIR; T09289; T09289.
DR   RefSeq; NP_990695.1; NM_205364.1.
DR   AlphaFoldDB; P49581; -.
DR   SMR; P49581; -.
DR   ComplexPortal; CPX-201; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR   ComplexPortal; CPX-214; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4.
DR   STRING; 9031.ENSGALP00000036997; -.
DR   BindingDB; P49581; -.
DR   PaxDb; P49581; -.
DR   GeneID; 396321; -.
DR   KEGG; gga:396321; -.
DR   CTD; 8973; -.
DR   VEuPathDB; HostDB:geneid_396321; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   InParanoid; P49581; -.
DR   OrthoDB; 381858at2759; -.
DR   PhylomeDB; P49581; -.
DR   PRO; PR:P49581; -.
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: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; IC: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: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   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..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..494
FT                   /note="Neuronal acetylcholine receptor subunit alpha-6"
FT                   /id="PRO_0000000364"
FT   TOPO_DOM        32..240
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        328..468
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          364..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..390
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        158..172
FT                   /evidence="ECO:0000250"
FT   CONFLICT        97
FT                   /note="R -> W (in Ref. 2; CAA58766/AAA92122)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   494 AA;  57495 MW;  195C9B2D27B86025 CRC64;
     MHPKRRLCWC LPASGAWAFM LTSLIADTTA CESEERLFHK LFSRYNQFIR PVENVSDPVT
     VHFELAITQL TNVDEVNQIM ETNLWLRHIW NDYKLRRDPR EYDGIEFVRV PADKIWKPDI
     VLYNNAVGDF QVEGKTKALL RYDGMITWTP PAIFKSSCPM DITFFPFDHQ NCSLKFGSWT
     YDKAKIDLLI IGSKVDMNEF WENSEWEIVD ASGYKHDIKY NCCEEIYTDI TYSFYIRRLP
     MFYTINLIIP CLFISFLTVL VFYLPSDCGE KVTLCISVLL SLTVFLLVIT ETIPSTSLVI
     PLVGEYLLFT MIFVTLSIVI TVFVLNIHYR TPTTHTMPKW VKTVFLSLLP KVLLMQRPLE
     QEKKNISKKT KKGSAKTSGK SKHSKHKDNK LHKEQRCCHC DKADDLTSTR RSRLSHQSLK
     WMAEHTEYSP EVKDVINNVQ FIAENMKSQN ETKEVEDDWK YVAMVIDRVF LWVFIILCVF
     GTAGLFIQPL IADT
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024