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GBRD_RAT
ID   GBRD_RAT                Reviewed;         449 AA.
AC   P18506;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit delta;
DE   AltName: Full=GABA(A) receptor subunit delta;
DE   Flags: Precursor;
GN   Name=Gabrd;
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.
RC   TISSUE=Brain;
RX   PubMed=2561970; DOI=10.1016/0896-6273(89)90257-2;
RA   Shivers B.D., Killisch I., Sprengel R., Sontheimer H., Koehler M.,
RA   Schofield P.R., Seeburg P.H.;
RT   "Two novel GABAA receptor subunits exist in distinct neuronal
RT   subpopulations.";
RL   Neuron 3:327-337(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=1690000; DOI=10.1016/0006-291x(90)91747-g;
RA   Zhao Z.Y., Joho R.H.;
RT   "Isolation of distantly related members in a multigene family using the
RT   polymerase chain reaction technique.";
RL   Biochem. Biophys. Res. Commun. 167:174-182(1990).
RN   [3]
RP   ERRATUM OF PUBMED:1690000.
RA   Zhao Z.Y., Joho R.H.;
RL   Biochem. Biophys. Res. Commun. 168:887-887(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 1-22.
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   PubMed=8195163; DOI=10.1016/s0021-9258(17)36601-2;
RA   Motejlek K., Hauselmann R., Leitgeb S., Luescher B.;
RT   "BSF1, a novel brain-specific DNA-binding protein recognizing a tandemly
RT   repeated purine DNA element in the GABAA receptor delta subunit gene.";
RL   J. Biol. Chem. 269:15265-15273(1994).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC       chains: alpha, beta, gamma, delta, and rho.
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       Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRD sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L08496; AAC42035.1; -; Genomic_DNA.
DR   EMBL; BC087714; AAH87714.1; -; mRNA.
DR   EMBL; M35162; AAA41182.1; -; mRNA.
DR   PIR; A34625; A34625.
DR   RefSeq; NP_058985.1; NM_017289.1.
DR   AlphaFoldDB; P18506; -.
DR   SMR; P18506; -.
DR   ComplexPortal; CPX-280; GABA-A receptor, alpha-4/beta-3/delta.
DR   ComplexPortal; CPX-406; GABA-A receptor, alpha-6/beta-3/delta.
DR   ComplexPortal; CPX-407; GABA-A receptor, alpha-6/beta-2/delta.
DR   ComplexPortal; CPX-408; GABA-A receptor, alpha-4/beta-2/delta.
DR   CORUM; P18506; -.
DR   IntAct; P18506; 1.
DR   STRING; 10116.ENSRNOP00000022246; -.
DR   BindingDB; P18506; -.
DR   ChEMBL; CHEMBL4296050; -.
DR   ChEMBL; CHEMBL4296053; -.
DR   ChEMBL; CHEMBL4296056; -.
DR   ChEMBL; CHEMBL4296061; -.
DR   DrugCentral; P18506; -.
DR   GlyGen; P18506; 2 sites.
DR   iPTMnet; P18506; -.
DR   PhosphoSitePlus; P18506; -.
DR   PaxDb; P18506; -.
DR   ABCD; P18506; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000022246; ENSRNOP00000022246; ENSRNOG00000016385.
DR   GeneID; 29689; -.
DR   KEGG; rno:29689; -.
DR   CTD; 2563; -.
DR   RGD; 61901; Gabrd.
DR   eggNOG; KOG3643; Eukaryota.
DR   GeneTree; ENSGT00940000160122; -.
DR   HOGENOM; CLU_010920_0_1_1; -.
DR   InParanoid; P18506; -.
DR   OMA; YRCVEME; -.
DR   OrthoDB; 480926at2759; -.
DR   PhylomeDB; P18506; -.
DR   TreeFam; TF315453; -.
DR   PRO; PR:P18506; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000016385; Expressed in frontal cortex and 4 other tissues.
DR   Genevisible; P18506; RN.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; ISO:RGD.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; ISO:RGD.
DR   GO; GO:1902711; C:GABA-A receptor complex; IPI:ComplexPortal.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; ISO:RGD.
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; IDA:RGD.
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; ISO:RGD.
DR   GO; GO:0007268; P:chemical synaptic transmission; IDA:RGD.
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; IPR008098; GABAAd_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   PANTHER; PTHR18945:SF34; PTHR18945:SF34; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR01722; GABAARDELTA.
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   1: Evidence at protein level;
KW   Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..16
FT   CHAIN           17..449
FT                   /note="Gamma-aminobutyric acid receptor subunit delta"
FT                   /id="PRO_0000000470"
FT   TOPO_DOM        17..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        249..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        275..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        309..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        332..426
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        427..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         390
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        164..178
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  50566 MW;  64BDBCDEEB2C70AF CRC64;
     MDVLGWLLLP LLLLCTQPHH GARAMNDIGD YVGSNLEISW LPNLDGLMEG YARNFRPGIG
     GPPVNVALAL EVASIDHISE ANMEYTMTVF LHQSWRDSRL SYNHTNETLG LDSRFVDKLW
     LPDTFIVNAK SAWFHDVTVE NKLIRLQPDG VILYSIRITS TVACDMDLAK YPMDEQECML
     DLESYGYSSE DIVYYWSENQ EQIHGLDRLQ LAQFTITSYR FTTELMNFKS AGQFPRLSLH
     FQLRRNRGVY IIQSYMPSVL LVAMSWVSFW ISQAAVPARV SLGITTVLTM TTLMVSARSS
     LPRASAIKAL DVYFWICYVF VFAALVEYAF AHFNADYRKK RKAKVKVTKP RAEMDVRNAI
     VLFSLSAAGV SQELAISRRQ GRVPGNLMGS YRSVEVEAKK EGGSRPGGPG GIRSRLKPID
     ADTIDIYARA VFPAAFAAVN IIYWAAYTM
 
 
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