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ACHA5_CHICK
ID   ACHA5_CHICK             Reviewed;         454 AA.
AC   P26152;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-5;
DE   Flags: Precursor;
GN   Name=CHRNA5;
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; TISSUE=Brain;
RX   PubMed=1698777; DOI=10.1016/s0021-9258(18)38201-2;
RA   Couturier S., Erkman L., Valera S., Rungger D., Bertrand S., Boulter J.,
RA   Ballivet M., Bertrand D.;
RT   "Alpha 5, alpha 3, and non-alpha 3. Three clustered avian genes encoding
RT   neuronal nicotinic acetylcholine receptor-related subunits.";
RL   J. Biol. Chem. 265:17560-17567(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: 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   -!- INTERACTION:
CC       P26152; P09484: CHRNB2; NbExp=8; IntAct=EBI-10686157, EBI-10686072;
CC       P26152; P26153: CHRNB4; NbExp=4; IntAct=EBI-10686157, EBI-10686176;
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-5/CHRNA5 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; J05642; AAA48560.1; -; mRNA.
DR   PIR; B39218; B39218.
DR   RefSeq; NP_989746.1; NM_204415.1.
DR   AlphaFoldDB; P26152; -.
DR   SMR; P26152; -.
DR   ComplexPortal; CPX-192; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2.
DR   ComplexPortal; CPX-207; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4.
DR   ComplexPortal; CPX-217; Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2.
DR   IntAct; P26152; 4.
DR   STRING; 9031.ENSGALP00000004767; -.
DR   PaxDb; P26152; -.
DR   GeneID; 386577; -.
DR   KEGG; gga:386577; -.
DR   CTD; 1138; -.
DR   VEuPathDB; HostDB:geneid_386577; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   InParanoid; P26152; -.
DR   OrthoDB; 381858at2759; -.
DR   PhylomeDB; P26152; -.
DR   PRO; PR:P26152; -.
DR   Proteomes; UP000000539; Unplaced.
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: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; 2.
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; Membrane; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..454
FT                   /note="Neuronal acetylcholine receptor subunit alpha-5"
FT                   /id="PRO_0000000359"
FT   TOPO_DOM        30..240
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..416
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        438..454
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        215
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"
SQ   SEQUENCE   454 AA;  51957 MW;  A33D79ED1F799776 CRC64;
     MPLRARSRKP GAGPAARAPQ AGVSEPSFVA KSEDRLFKHL FEDYQRWVRP VEHLNDTIKI
     KFGLAISQLV DVDEKNQLMT TNVWLKQEWI HVKLRWNPED YAGITSIRVP SDSIWIPDIV
     LYDNADGRFE GTSTKTVVKY DGTIAWTPPV NYKSSCTIDV TFFPFDLQNC SMKFGSWTYD
     GSQVDIILED YEVDKRDFFD NGEWEIVTAT GSKGNRTDGC CWYPFVTYSF IIRRLPLFYT
     LFLIIPCIGL SFLTVLVFYL PSNEAEKISL CTSVLVSLTV FLLVIEEIIP SSSKVIPLIG
     EYLVFTMIFV TLSIVITVFA INIHHRSSST HNAMAPWVRK IFLHKLPKLL CMRSHVDRYF
     AQKEEKGNMS GSESSRNTLE AALDSIRYIT RHVMKENEVR EVVEDWKFIA QVLDRMFLWA
     FLLVSIIGSL VLFIPVIHKW ASIIVPVHIG STNT
 
 
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