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GBRR2_RAT
ID   GBRR2_RAT               Reviewed;         465 AA.
AC   P47742;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 3.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit rho-2;
DE   AltName: Full=GABA(A) receptor subunit rho-2;
DE   AltName: Full=GABA(C) receptor;
DE   Flags: Precursor;
GN   Name=Gabrr2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Sprague-Dawley; TISSUE=Retina;
RX   PubMed=7643126; DOI=10.1046/j.1471-4159.1995.65030964.x;
RA   Ogurusu T., Taira H., Shingai R.;
RT   "Identification of GABAA receptor subunits in rat retina: cloning of the
RT   rat GABAA receptor rho 2-subunit cDNA.";
RL   J. Neurochem. 65:964-968(1995).
RN   [2]
RP   INTERACTION WITH SQSTM1.
RX   PubMed=12431995; DOI=10.1074/jbc.m205162200;
RA   Croci C., Brandstaetter J.H., Enz R.;
RT   "ZIP3, a new splice variant of the PKC-zeta-interacting protein family,
RT   binds to GABAC receptors, PKC-zeta, and Kv beta 2.";
RL   J. Biol. Chem. 278:6128-6135(2003).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate
CC       brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride channel.
CC       Rho-2 GABA receptor could play a role in retinal neurotransmission.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC       chains: alpha, beta, gamma, delta, and rho. Interacts with SQSTM1.
CC       {ECO:0000269|PubMed:12431995}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1;
CC         IsoId=P47742-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P47742-2; Sequence=VSP_044375;
CC   -!- TISSUE SPECIFICITY: Retina.
CC   -!- MISCELLANEOUS: [Isoform 2]: Isoform 2 could be translated from an
CC       upstream initiator ATG located in frame within the first coding exon.
CC       The probability of a signal peptide within this isoform is very low.
CC       {ECO:0000305}.
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. GABRR2 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; D38494; BAA07506.1; -; mRNA.
DR   PIR; I56523; I56523.
DR   RefSeq; NP_058988.1; NM_017292.2. [P47742-1]
DR   AlphaFoldDB; P47742; -.
DR   SMR; P47742; -.
DR   STRING; 10116.ENSRNOP00000009973; -.
DR   GlyGen; P47742; 2 sites.
DR   iPTMnet; P47742; -.
DR   PhosphoSitePlus; P47742; -.
DR   PaxDb; P47742; -.
DR   PRIDE; P47742; -.
DR   Ensembl; ENSRNOT00000009973; ENSRNOP00000009973; ENSRNOG00000007490. [P47742-2]
DR   GeneID; 29695; -.
DR   KEGG; rno:29695; -.
DR   UCSC; RGD:61902; rat. [P47742-1]
DR   CTD; 2570; -.
DR   RGD; 61902; Gabrr2.
DR   VEuPathDB; HostDB:ENSRNOG00000007490; -.
DR   eggNOG; KOG3643; Eukaryota.
DR   GeneTree; ENSGT00940000156864; -.
DR   InParanoid; P47742; -.
DR   OMA; KFPCVCG; -.
DR   OrthoDB; 640805at2759; -.
DR   TreeFam; TF315453; -.
DR   Reactome; R-RNO-977443; GABA receptor activation.
DR   PRO; PR:P47742; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000007490; Expressed in skeletal muscle tissue and 16 other tissues.
DR   ExpressionAtlas; P47742; baseline and differential.
DR   Genevisible; P47742; RN.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:1902711; C:GABA-A receptor complex; IBA:GO_Central.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
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; TAS:RGD.
DR   GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0004890; F:GABA-A receptor activity; IDA:RGD.
DR   GO; GO:0005237; F:inhibitory extracellular ligand-gated ion channel activity; TAS:RGD.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR   GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
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; ISO:RGD.
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   GO; GO:0007601; P:visual perception; ISO:RGD.
DR   Gene3D; 1.20.58.390; -; 1.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
DR   InterPro; IPR008059; GABAAa_rho2_rcpt.
DR   InterPro; IPR008057; GABAAa_rho_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; PR01670; GABAARRHO.
DR   PRINTS; PR01672; GABAARRHO2.
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   Alternative initiation; Cell membrane; Chloride; Chloride channel;
KW   Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Postsynaptic cell membrane; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..465
FT                   /note="Gamma-aminobutyric acid receptor subunit rho-2"
FT                   /id="PRO_0000000490"
FT   TOPO_DOM        21..260
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        347..443
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        444..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        178..192
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1
FT                   /note="M -> MVKSQGIFPCSCCSPVPACCVIDVCRM (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_044375"
SQ   SEQUENCE   465 AA;  54296 MW;  3A182C429C750028 CRC64;
     MPYFMRLALF LFCLMALVES RKPRRKRWTG HLETSKPSHL YKKNLDVTKI RTGKPRPLLR
     VEDHDFTMRP AFGGPAIPVG VDVQVESLDS ISEVDMDFTM TLYLRHYWRD ERLAFPSSSN
     RSMTFDGRLV KKIWVPDVFF VHSKRSFTHD TTTDNIMLRV FPDGHVLYSM RITVTAMCNM
     DFSHFPLDSQ TCSLELESYA YTDEDLMLYW KNGDESLKTD EKISLSQFLI QKFHTTSRLA
     FYSSTGWYNR LYINFTLRRH IFFFLLQTYF PATLMVMLSW VSFWIDHRAV PARVSLGIMT
     VLTMSTIITG VNASMPRVSY IRAVDIYLWV SFVFVFLSVL EYAAVNYLTT VQEQKERKLR
     DKFPCTCGML HSRTMTLDGS YSESEANSLA GYPRSHILPE EERQDKIVVH LALNSELTSS
     RKKGLLKGQM GLYIFQNTHA IDKYSRLIFP AFYIVFNLIY WSVFS
 
 
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