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GLRB4_CAEEL
ID   GLRB4_CAEEL             Reviewed;         473 AA.
AC   Q09453;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Glycine receptor subunit beta-type 4;
DE   Flags: Precursor;
GN   Name=ggr-1; Synonyms=gbr-4; ORFNames=C09G5.1/C09G5.9;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel
CC       opening is triggered by extracellular glycine. Contributes to the
CC       generation of inhibitory postsynaptic currents.
CC       {ECO:0000250|UniProtKB:P48168}.
CC   -!- SUBUNIT: Pentamer. {ECO:0000250|UniProtKB:P48167}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:P48168}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P48167}. Synapse {ECO:0000250|UniProtKB:P48168}.
CC       Cell membrane {ECO:0000250|UniProtKB:P48168}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P23415}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Glycine receptor (TC 1.A.9.3) subfamily. {ECO:0000305}.
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DR   EMBL; Z46791; CAA86760.2; -; Genomic_DNA.
DR   PIR; T19145; T19145.
DR   RefSeq; NP_496306.2; NM_063905.3.
DR   AlphaFoldDB; Q09453; -.
DR   SMR; Q09453; -.
DR   STRING; 6239.C09G5.1; -.
DR   PaxDb; Q09453; -.
DR   PRIDE; Q09453; -.
DR   EnsemblMetazoa; C09G5.1.1; C09G5.1.1; WBGene00001586.
DR   GeneID; 191636; -.
DR   KEGG; cel:CELE_C09G5.1; -.
DR   UCSC; C09G5.1; c. elegans.
DR   CTD; 191636; -.
DR   WormBase; C09G5.1; CE36915; WBGene00001586; ggr-1.
DR   eggNOG; KOG3644; Eukaryota.
DR   HOGENOM; CLU_010920_0_1_1; -.
DR   InParanoid; Q09453; -.
DR   OMA; EITHHII; -.
DR   OrthoDB; 614790at2759; -.
DR   PhylomeDB; Q09453; -.
DR   Reactome; R-CEL-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR   PRO; PR:Q09453; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00001586; Expressed in larva and 3 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: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:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
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:1902476; P:chloride transmembrane transport; 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:0007165; P:signal transduction; 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; 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; 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   3: Inferred from homology;
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..473
FT                   /note="Glycine receptor subunit beta-type 4"
FT                   /id="PRO_0000000426"
FT   TOPO_DOM        20..249
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P23415"
FT   TRANSMEM        250..271
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P23415"
FT   TOPO_DOM        272..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P23415"
FT   TRANSMEM        277..297
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P23415"
FT   TOPO_DOM        298..308
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P23415"
FT   TRANSMEM        309..329
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P23415"
FT   TOPO_DOM        330..439
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P23415"
FT   TRANSMEM        440..460
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P23415"
FT   TOPO_DOM        461..473
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P23415"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        166..180
FT                   /evidence="ECO:0000250|UniProtKB:P23415"
SQ   SEQUENCE   473 AA;  55540 MW;  0290671D994F7307 CRC64;
     MHSLFLKILI YSLMQCVLGQ AEFWDYDENV TQIEEDFKID DVTRILKRVG NYNRNAYPLL
     DQDLATHVDI QMYIEGMSSF HAQSMDFQVD IYFQEKWVDH RLQHNNTKRI LVKDPKLFGL
     LWHPDLYFAN ARTASFHDVT QPNFLVWIYP NGTVWYDCRI SLTVLCMQDL ARYPLDSQNC
     GLRILSYAYD EEQLIIRWNG GNPVEVNRGI RMPDMHLKHI KFYTKRDKYA TGIWSSAVAE
     FHVDREITHH IIQSYIPTSL IVIISWFSFW LDVEAVPGRV SLSITTLLTL ATQSSAARMA
     LPQASDVKAI DVWMGTCMAF VFSAMIEFTV VNYCVRRKVR TKIKPRGLSE QVHDMVAQYR
     EKKDKFNNGN CEISYEMALQ PNEDNATVQR NFEKKEVREM NQASLFVRRS LLPTSKRKTI
     EDRINRVEEN RKNAQKIDRY SRALFPLAFI IFNIFYWIYY LKYAGSNSPE LLL
 
 
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