P56476 · GBRR2_MOUSE
- ProteinGamma-aminobutyric acid receptor subunit rho-2
- GeneGabrr2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids465 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Rho subunit of the pentameric ligand-gated chloride channels responsible for mediating the effects of gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the brain (By similarity).
Rho-containing GABA-gated chloride channels are a subclass of GABA(A) receptors (GABAARs) entirely composed of rho subunits, where GABA molecules bind at the rho intersubunit interfaces (By similarity).
When activated by GABA, rho-GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (By similarity).
Rho-2 GABAARs may contribute to the regulation of glial development in the cerebellum by controlling extrasynaptic transmission (PubMed:25422464).
Rho-2 GABAARs are also involved in neuronal tonic (extrasynaptic) and phasic (synaptic) transmission in the Purkinje neurons of the cerebellum (PubMed:16945976).
Rho-2 GABAARs expressed in retina may play a role in retinal neurotransmission (By similarity).
Rho-containing GABA-gated chloride channels are a subclass of GABA(A) receptors (GABAARs) entirely composed of rho subunits, where GABA molecules bind at the rho intersubunit interfaces (By similarity).
When activated by GABA, rho-GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (By similarity).
Rho-2 GABAARs may contribute to the regulation of glial development in the cerebellum by controlling extrasynaptic transmission (PubMed:25422464).
Rho-2 GABAARs are also involved in neuronal tonic (extrasynaptic) and phasic (synaptic) transmission in the Purkinje neurons of the cerebellum (PubMed:16945976).
Rho-2 GABAARs expressed in retina may play a role in retinal neurotransmission (By similarity).
Catalytic activity
- chloride(in) = chloride(out)
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 105 | 4-aminobutanoate (UniProtKB | ChEBI); ligand shared between two neighboring rho subunits; in chain A | ||||
Sequence: R | ||||||
Binding site | 169 | 4-aminobutanoate (UniProtKB | ChEBI); ligand shared between two neighboring rho subunits; in chain A | ||||
Sequence: S | ||||||
Binding site | 197 | 4-aminobutanoate (UniProtKB | ChEBI); ligand shared between two neighboring rho subunits; in chain B | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | chloride channel complex | |
Cellular Component | GABA-A receptor complex | |
Cellular Component | GABA-ergic synapse | |
Cellular Component | neuron projection | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic membrane | |
Cellular Component | synapse | |
Cellular Component | transmembrane transporter complex | |
Molecular Function | GABA-A receptor activity | |
Molecular Function | GABA-gated chloride ion channel activity | |
Molecular Function | neurotransmitter receptor activity | |
Molecular Function | protein domain specific binding | |
Molecular Function | transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential | |
Biological Process | chloride transmembrane transport | |
Biological Process | chloride transport | |
Biological Process | gamma-aminobutyric acid signaling pathway | |
Biological Process | visual perception |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGamma-aminobutyric acid receptor subunit rho-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP56476
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Postsynaptic cell membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Note: Located at the plasma membrane of astrocytes, in soma and to some extent in distal processes.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 21-260 | Extracellular | ||||
Sequence: RKPRRKRWTGLLETSKPSHLYKKNLDVTKMRPGKPRPLLRVEDHDFTMRPAFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWRDERLAFPSSSNKSMTFDGRLVKKIWVPDVFFVHSKRSFIHDTTTDNIMLRVFPDGHVLYSMRITVTAMCNMDFSHFPLDSQTCSLELESYAYTDEDLMLYWKNGDESLKTDEKISLSQFLIQKFHTTSRLAFYSSTGWYNRLYINFTLRRH | ||||||
Transmembrane | 261-281 | Helical | ||||
Sequence: IFFFLLQTYFPATLMVMLSWV | ||||||
Topological domain | 282-293 | Cytoplasmic | ||||
Sequence: SFWIDHRAVPAR | ||||||
Transmembrane | 294-314 | Helical | ||||
Sequence: VSLGIMTVLTMSTIITGVNAS | ||||||
Topological domain | 315-325 | Extracellular | ||||
Sequence: MPRVSYIRAVD | ||||||
Transmembrane | 326-346 | Helical | ||||
Sequence: IYLWVSFVFVFLSVLEYAAVN | ||||||
Topological domain | 347-443 | Cytoplasmic | ||||
Sequence: YLTTLQEQKERKFREKLPCMCGMLHSRTMMLDGSYSESEANSLAGYPRSHILPEEERPDNIVVHLALNSELTSSRKKGLLKGQMGLYIFQNTHAIDK | ||||||
Transmembrane | 444-464 | Helical | ||||
Sequence: YSRLIFPAFYIVFNLIYWSVF | ||||||
Topological domain | 465 | Extracellular | ||||
Sequence: S |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MPYLMRLALVLFCLMALVES | ||||||
Chain | PRO_0000000489 | 21-465 | Gamma-aminobutyric acid receptor subunit rho-2 | |||
Sequence: RKPRRKRWTGLLETSKPSHLYKKNLDVTKMRPGKPRPLLRVEDHDFTMRPAFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWRDERLAFPSSSNKSMTFDGRLVKKIWVPDVFFVHSKRSFIHDTTTDNIMLRVFPDGHVLYSMRITVTAMCNMDFSHFPLDSQTCSLELESYAYTDEDLMLYWKNGDESLKTDEKISLSQFLIQKFHTTSRLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDHRAVPARVSLGIMTVLTMSTIITGVNASMPRVSYIRAVDIYLWVSFVFVFLSVLEYAAVNYLTTLQEQKERKFREKLPCMCGMLHSRTMMLDGSYSESEANSLAGYPRSHILPEEERPDNIVVHLALNSELTSSRKKGLLKGQMGLYIFQNTHAIDKYSRLIFPAFYIVFNLIYWSVFS | ||||||
Glycosylation | 120 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 178↔192 | |||||
Sequence: CNMDFSHFPLDSQTC | ||||||
Glycosylation | 254 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the cerebellum.
Developmental stage
Expressed during early postnatal development of cerebellar ependymal glial cells. The expression is down-regulated in young mice, but limited to Purkinje neurons and a small fraction of glial cells in adults.
Gene expression databases
Interaction
Subunit
Three rho subunits (rho-1/GBRR1, rho-2/GBRR2 and rho-3/GBRR3) coassemble either to form functional homopentamers or heteropentamers (PubMed:25422464).
Rho-2 is unable to form a functional homopentamer (By similarity).
Interacts with SQSTM1 (By similarity).
Rho-2 is unable to form a functional homopentamer (By similarity).
Interacts with SQSTM1 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Domain
GABAARs subunits share a common topological structure: a peptide sequence made up of a long extracellular N-terminal, four transmembrane domains, intracellular or cytoplasmic domain located between the third and the fourth transmembrane domains.
Sequence similarities
Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRR2 sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative initiation.
P56476-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length465
- Mass (Da)54,231
- Last updated2012-10-31 v4
- ChecksumB44B51B572468A20
P56476-2
- Name2
- NoteIsoform 2 could be translated from an upstream initiator ATG located in frame within the first coding exon. The probability of a signal peptide within this isoform is very low.
- Differences from canonical
- 1-1: M → MVKPGGILPIKSPCTAACCIIDMCRM
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_044374 | 1 | in isoform 2 | |||
Sequence: M → MVKPGGILPIKSPCTAACCIIDMCRM | ||||||
Sequence conflict | 33 | in Ref. 1; AAB81965 | ||||
Sequence: E → D | ||||||
Sequence conflict | 52 | in Ref. 1; AAB81965 | ||||
Sequence: P → A | ||||||
Sequence conflict | 59 | in Ref. 1; AAB81965 | ||||
Sequence: L → F | ||||||
Sequence conflict | 88 | in Ref. 1; AAB81965 | ||||
Sequence: L → V | ||||||
Sequence conflict | 105 | in Ref. 1; AAB81965 | ||||
Sequence: R → K | ||||||
Sequence conflict | 109 | in Ref. 1; AAB81965 | ||||
Sequence: R → K | ||||||
Sequence conflict | 149 | in Ref. 1; AAB81965 | ||||
Sequence: H → Q | ||||||
Sequence conflict | 357 | in Ref. 1; AAB81965 | ||||
Sequence: R → L | ||||||
Sequence conflict | 366 | in Ref. 1; AAB81965 | ||||
Sequence: M → V | ||||||
Sequence conflict | 372 | in Ref. 1; AAB81965 | ||||
Sequence: S → A | ||||||
Sequence conflict | 394 | in Ref. 1; AAB81965 | ||||
Sequence: R → T | ||||||
Sequence conflict | 400 | in Ref. 1; AAB81965 | ||||
Sequence: E → K | ||||||
Sequence conflict | 421 | in Ref. 1; AAB81965 | ||||
Sequence: R → K | ||||||
Sequence conflict | 429 | in Ref. 1; AAB81965 | ||||
Sequence: Q → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF024621 EMBL· GenBank· DDBJ | AAB81965.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466538 EMBL· GenBank· DDBJ | EDL05492.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC057957 EMBL· GenBank· DDBJ | AAH57957.2 EMBL· GenBank· DDBJ | mRNA |