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GBRR2_BOVIN
ID   GBRR2_BOVIN             Reviewed;         465 AA.
AC   Q0II76;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 4.
DT   03-AUG-2022, entry version 105.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC       chains: alpha, beta, gamma, delta, and rho. Interacts with SQSTM1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q0II76-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0II76-2; Sequence=VSP_044372;
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; BC122770; AAI22771.1; -; mRNA.
DR   RefSeq; NP_001071414.2; NM_001077946.1. [Q0II76-1]
DR   AlphaFoldDB; Q0II76; -.
DR   SMR; Q0II76; -.
DR   STRING; 9913.ENSBTAP00000047201; -.
DR   PaxDb; Q0II76; -.
DR   Ensembl; ENSBTAT00000024526; ENSBTAP00000024526; ENSBTAG00000011672. [Q0II76-2]
DR   GeneID; 522099; -.
DR   KEGG; bta:522099; -.
DR   CTD; 2570; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011672; -.
DR   eggNOG; KOG3643; Eukaryota.
DR   GeneTree; ENSGT00940000156864; -.
DR   HOGENOM; CLU_010920_0_1_1; -.
DR   InParanoid; Q0II76; -.
DR   OrthoDB; 640805at2759; -.
DR   Proteomes; UP000009136; Chromosome 9.
DR   Bgee; ENSBTAG00000011672; Expressed in retina and 53 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:1902711; C:GABA-A receptor complex; IBA:GO_Central.
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:0004890; F:GABA-A receptor activity; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
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   2: Evidence at transcript 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_0000282336"
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..444
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        445..465
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 -> MVKPGGICPAAGPWKAACSIADIHRM (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_044372"
SQ   SEQUENCE   465 AA;  54122 MW;  4A86931A8C7160F6 CRC64;
     MPYFSRLILF LFCLVVLVES RKPKKRRWTG QLETSKPSHL YKKNPDMTKI RHGKPQPLLR
     VDDHDFTMRP AFGGPAIPVG VDVQVESLDS ISEVDMDFTM TLYLRHYWKD ERLAFPSASN
     KSMTFDGRLV KKIWVPDVFF VHSKRSFIHD TTTDNIMLRV FPDGQVLYSM RITVTAMCNM
     DFSHFPLDSQ TCSLELESYA YTDEDLMLYW KNGDESLKTD EKISLSQFLI QKFHTTSRLA
     FYSSTGWYNR LYINFTLRRH IFFFLLQTYF PATLMVMLSW VSFWIDRRAV PARVSLGITT
     VLTMSTIITG VNASMPRVSY IKAVDIYLWV SFVFVFLSVL EYAAVNYLTT VQERKERKLQ
     EKFPCMCGML HSRTMMLDGS YSESEANSLA GYPRSHILPE EERQDKIVVH LALSNESSSS
     RKKGLLKGQV GLRIFQNTHA IDKYSRLIFP ASYIFFNLIY WSVFA
 
 
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