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GBRA1_CHICK
ID   GBRA1_CHICK             Reviewed;         455 AA.
AC   P19150;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-1;
DE   AltName: Full=GABA(A) receptor subunit alpha-1;
DE   Flags: Precursor;
GN   Name=GABRA1;
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], AND TISSUE SPECIFICITY.
RC   STRAIN=Commercial Rhode Island cross; TISSUE=Brain;
RX   PubMed=1710013; DOI=10.1016/0169-328x(91)90081-8;
RA   Bateson A.N., Harvey R.J., Wisden W., Glencorse T.A., Hicks A.A.,
RA   Hunt S.P., Barnard E.A., Darlison M.G.;
RT   "The chicken GABAA receptor alpha 1 subunit: cDNA sequence and localization
RT   of the corresponding mRNA.";
RL   Brain Res. Mol. Brain Res. 9:333-339(1991).
CC   -!- FUNCTION: Ligand-gated chloride channel which is a component of the
CC       heteropentameric receptor for GABA, the major inhibitory
CC       neurotransmitter in the brain (By similarity). Plays an important role
CC       in the formation of functional inhibitory GABAergic synapses in
CC       addition to mediating synaptic inhibition as a GABA-gated ion channel
CC       (By similarity). Functions also as histamine receptor and mediates
CC       cellular responses to histamine (By similarity).
CC       {ECO:0000250|UniProtKB:P62812, ECO:0000250|UniProtKB:P62813}.
CC   -!- ACTIVITY REGULATION: Allosterically activated by benzodiazepines, the
CC       neuroanesthetic alphaxalone and pentobarbital (By similarity).
CC       Inhibited by the antagonist bicuculline (By similarity).
CC       {ECO:0000250|UniProtKB:P14867, ECO:0000250|UniProtKB:P62813}.
CC   -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma,
CC       delta and rho chains. {ECO:0000250|UniProtKB:P14867}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:P08219}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P62812}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:1710013}.
CC   -!- DOMAIN: The extracellular domain contributes to synaptic contact
CC       formation. {ECO:0000250|UniProtKB:P62812}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRA1 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X54244; CAA38148.1; -; mRNA.
DR   PIR; A60033; CHCHA1.
DR   RefSeq; NP_989649.1; NM_204318.2.
DR   RefSeq; XP_015149123.1; XM_015293637.1.
DR   AlphaFoldDB; P19150; -.
DR   SMR; P19150; -.
DR   STRING; 9031.ENSGALP00000002606; -.
DR   PaxDb; P19150; -.
DR   Ensembl; ENSGALT00000002609; ENSGALP00000002606; ENSGALG00000001698.
DR   Ensembl; ENSGALT00000091190; ENSGALP00000066924; ENSGALG00000001698.
DR   Ensembl; ENSGALT00000092358; ENSGALP00000073963; ENSGALG00000001698.
DR   GeneID; 374214; -.
DR   KEGG; gga:374214; -.
DR   CTD; 2554; -.
DR   VEuPathDB; HostDB:geneid_374214; -.
DR   eggNOG; KOG3642; Eukaryota.
DR   GeneTree; ENSGT00940000159136; -.
DR   HOGENOM; CLU_010920_2_1_1; -.
DR   InParanoid; P19150; -.
DR   OMA; ELHKPAM; -.
DR   OrthoDB; 1057372at2759; -.
DR   PhylomeDB; P19150; -.
DR   TreeFam; TF315453; -.
DR   Reactome; R-GGA-977443; GABA receptor activation.
DR   PRO; PR:P19150; -.
DR   Proteomes; UP000000539; Chromosome 13.
DR   Bgee; ENSGALG00000001698; Expressed in cerebellum and 6 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR   GO; GO:1902711; C:GABA-A receptor complex; ISS:UniProtKB.
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:0098794; C:postsynapse; 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:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR   GO; GO:0022851; F:GABA-gated chloride ion channel activity; IBA:GO_Central.
DR   GO; GO:0005237; F:inhibitory 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; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
DR   GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
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:0060078; P:regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; IBA:GO_Central.
DR   Gene3D; 1.20.58.390; -; 1.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
DR   InterPro; IPR001390; GABAAa_rcpt.
DR   InterPro; IPR005431; GABBAa1_rcpt.
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   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR01079; GABAARALPHA.
DR   PRINTS; PR01614; GABAARALPHA1.
DR   PRINTS; PR00253; GABAARECEPTR.
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; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..455
FT                   /note="Gamma-aminobutyric acid receptor subunit alpha-1"
FT                   /id="PRO_0000000431"
FT   TOPO_DOM        28..251
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        252..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        279..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        313..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        335..420
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        166..180
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   455 AA;  51842 MW;  23AD620C56762E8D CRC64;
     MKRLLVLCDC LWAWSLLLNA LTERSYGQTS SQDELKDNTT VFTRILDRLL DGYDNRLRPG
     LGERVTEVKT DIFVTSFGPV SDHDMEYTID VFFRQSWKDE RLKFKGPMTV LRLNNLMASK
     IWTPDTFFHN GKKSVAHNMT MPNKLLRITE DGTLLYTMRL TVRAECPMHL EDFPMDVHAC
     PLKFGSYAYT RAEVVYEWTR EPARSVVVAE DGSRLNQYDL LGQTVDSGIV QSSTGEYVVM
     TTHFHLKRKI GYFVIQTYLP CIMTVILSQV SFWLNRESVP ARTVFGVTTV LTMTTLSISA
     RNSLPKVAYA TAMDWFIAVC YAFVFSALIE FATVNYFTKR GYAWDGKSVV PEKPKKVKDP
     LIKKNNTYTA AATSYTPNIA RDPGLATIAK SATIEPKEVK PETKPAEPKK TFNSVSKIDR
     LSRIAFPLLF GIFNLVYWAT YLNREPQLKA PTPHQ
 
 
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