E1BBQ2 · MGLYR_BOVIN
- ProteinMetabotropic glycine receptor
- GeneGPR158
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1216 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Metabotropic receptor for glycine that controls synapse formation and function in the brain. Acts as an atypical G-protein coupled receptor that recruits and regulates the RGS7-GNB5 complex instead of activating G proteins. In absence of glycine ligand, promotes the GTPase activator activity of RGS7, increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Glycine-binding changes the conformation of the intracellular surface, inhibiting the GTPase activator activity of the RGS7-GNB5 complex, promoting G protein alpha subunits into their active GTP-bound form and regulating cAMP levels. Also able to bind taurine, a compound closely related to glycine, but with a two-fold lower affinity. Glycine receptor-dependent regulation of cAMP controls key ion channels, kinases and neurotrophic factors involved in neuronal excitability and synaptic transmission (By similarity).
Plays a pivotal role in regulating mood and cognition via its ability to regulate neuronal excitability in L2/L3 pyramidal neurons of the prefrontal cortex. Also involved in spatial learning by regulating hippocampal CA1 neuronal excitability. Acts as a synaptic organizer in the hippocampus, required for proper mossy fiber-CA3 neurocircuitry establishment, structure and function: induces presynaptic differentiation in contacting axons via its interaction with GPC4. In addition to glycine, may also act as a receptor for osteocalcin (BGLAP) hormone: osteocalcin-binding initiates a signaling response that prevents neuronal apoptosis in the hippocampus and regulates the synthesis of neurotransmitters (By similarity).
Plays a pivotal role in regulating mood and cognition via its ability to regulate neuronal excitability in L2/L3 pyramidal neurons of the prefrontal cortex. Also involved in spatial learning by regulating hippocampal CA1 neuronal excitability. Acts as a synaptic organizer in the hippocampus, required for proper mossy fiber-CA3 neurocircuitry establishment, structure and function: induces presynaptic differentiation in contacting axons via its interaction with GPC4. In addition to glycine, may also act as a receptor for osteocalcin (BGLAP) hormone: osteocalcin-binding initiates a signaling response that prevents neuronal apoptosis in the hippocampus and regulates the synthesis of neurotransmitters (By similarity).
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell projection | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic membrane | |
Cellular Component | presynaptic membrane | |
Molecular Function | enzyme activator activity | |
Molecular Function | G protein-coupled glycine receptor activity | |
Molecular Function | transmembrane signaling receptor activity | |
Biological Process | cognition | |
Biological Process | G protein-coupled receptor signaling pathway | |
Biological Process | protein localization to plasma membrane | |
Biological Process | regulation of G protein-coupled receptor signaling pathway | |
Biological Process | regulation of synapse organization |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameMetabotropic glycine receptor
- Short namesmGlyR
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionE1BBQ2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Postsynaptic cell membrane ; Multi-pass membrane protein
Presynaptic cell membrane ; Multi-pass membrane protein
Note: Mainly localizes to the postsynaptic membrane, with a small portion to the presynaptic membrane (By similarity).
Trafficks between the nucleus and the cell membrane; it is unclear how a multi-pass membrane protein can traffick between the nucleus and the cell membrane (By similarity).
Trafficks between the nucleus and the cell membrane; it is unclear how a multi-pass membrane protein can traffick between the nucleus and the cell membrane (By similarity).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 24-417 | Extracellular | ||||
Sequence: ASREAPSRPDPPRERTLRAKQHAQQPARASASDPSAPWSRSTDGTILAQKLAEEVPMDVASYLYTGDSHKLKRANCSSRYELAGLPGKSPALASSHPSLHGALDTLTHATNFLNMMLQSNKSREQNLQDDLEWYQALVRSLLEGEPSISRAAITFSTESLSAPAPQVFLQATREESRILLQDLSSSAHHLANATLETEWFHGLRRKWRTHLHRRGSNQGPRGLGHSWRRRDGLSGDKSHVKWSPPYLECENGSYKPGWLVTLSAAFYGLQPNLVPEFRGVMKVDINLQKVDIDQCSSDGWFSGTHKCHLNNSECMPIKGLGFVLGAYQCICKAGFYHPRDFSFNNFQRRGPDHHFVESAKDVSEEVHVCLPCSEGCPYCADDSPCFVQEDKYLR | ||||||
Transmembrane | 418-439 | Helical; Name=1 | ||||
Sequence: LAIISFQALCMLLDFLSMLVVY | ||||||
Topological domain | 440-451 | Cytoplasmic | ||||
Sequence: RFRKAKSIRASG | ||||||
Transmembrane | 452-474 | Helical; Name=2 | ||||
Sequence: LILLETILFGSLLLYFPVVILYF | ||||||
Topological domain | 475-478 | Extracellular | ||||
Sequence: EPST | ||||||
Transmembrane | 479-501 | Helical; Name=3 | ||||
Sequence: FRCILLRWVRLLGFATVYGTVTL | ||||||
Topological domain | 502-525 | Cytoplasmic | ||||
Sequence: KLHRVLKVFLSRTAQRIPYMTGGR | ||||||
Transmembrane | 526-547 | Helical; Name=4 | ||||
Sequence: VMRMLAVILLVVFWFLVGWTSS | ||||||
Topological domain | 548-576 | Extracellular | ||||
Sequence: VCQNLERHISLIGQGRTSDHLIFSMCLVE | ||||||
Transmembrane | 577-597 | Helical; Name=5 | ||||
Sequence: RWDYMTAAAEFLFLLWGVYLC | ||||||
Topological domain | 598-611 | Cytoplasmic | ||||
Sequence: YAVRTVPSAFHEPR | ||||||
Transmembrane | 612-633 | Helical; Name=6 | ||||
Sequence: YMAVAVHNELIISAIFHTIRFV | ||||||
Topological domain | 634-642 | Extracellular | ||||
Sequence: LASRLQSDW | ||||||
Transmembrane | 643-664 | Helical; Name=7 | ||||
Sequence: MLMLYFAHTHLTVTVTIGLLLI | ||||||
Topological domain | 665-1216 | Cytoplasmic | ||||
Sequence: PKFSHSSNNPRDDIATEAYEDELDMGRSGSYLNSSINSAWSEHSLDPEDIRDELKKLYAQLEIYKRKKMITNNPHLQKKRCSKKGLGRSIMRRITEIPETVSRQCSKEDKDGGEHGSAKGSSAGRKNPQETAGGSGKPKEESLRSRVFSLKKSHSTYEHVREQPGGPGSPPAQSREEEEATDNSVLGSPVGANRPRPLQEDSQAVSTESVPLVCKSASAHNLSSEKKPGPTRTSVLQKSLSVIASAKEKTLGLAGKTQAACVEERAKAQKALPRERETNRKYSNSDNAETQDSAPPNSSHSEEPRKPQKLGIMKQQRANPTTANSDLSPGATHMKDNFDIGEVCPWEIYDLAPGPGPLESKVQKHVSIAASEMERNPTFSLKEKSHPKPKAADLCQQSNPKSVDKAEVCPWESQGQSLFEEEKYLMSKTQVPLGRAQGENSGQHCATGVCAGQCEELPPKAVASKVENENLNQLGEQEKKTSSSERNVPDSHNSSNNFQPPLMSRAEVCPWEFETPDKPNAERSVAFPASSALSANKIAGPRNEEVRLARKV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MGVMAYPFLFCLLLVHFGLGAIG | ||||||
Chain | PRO_0000418361 | 24-1216 | Metabotropic glycine receptor | |||
Sequence: ASREAPSRPDPPRERTLRAKQHAQQPARASASDPSAPWSRSTDGTILAQKLAEEVPMDVASYLYTGDSHKLKRANCSSRYELAGLPGKSPALASSHPSLHGALDTLTHATNFLNMMLQSNKSREQNLQDDLEWYQALVRSLLEGEPSISRAAITFSTESLSAPAPQVFLQATREESRILLQDLSSSAHHLANATLETEWFHGLRRKWRTHLHRRGSNQGPRGLGHSWRRRDGLSGDKSHVKWSPPYLECENGSYKPGWLVTLSAAFYGLQPNLVPEFRGVMKVDINLQKVDIDQCSSDGWFSGTHKCHLNNSECMPIKGLGFVLGAYQCICKAGFYHPRDFSFNNFQRRGPDHHFVESAKDVSEEVHVCLPCSEGCPYCADDSPCFVQEDKYLRLAIISFQALCMLLDFLSMLVVYRFRKAKSIRASGLILLETILFGSLLLYFPVVILYFEPSTFRCILLRWVRLLGFATVYGTVTLKLHRVLKVFLSRTAQRIPYMTGGRVMRMLAVILLVVFWFLVGWTSSVCQNLERHISLIGQGRTSDHLIFSMCLVERWDYMTAAAEFLFLLWGVYLCYAVRTVPSAFHEPRYMAVAVHNELIISAIFHTIRFVLASRLQSDWMLMLYFAHTHLTVTVTIGLLLIPKFSHSSNNPRDDIATEAYEDELDMGRSGSYLNSSINSAWSEHSLDPEDIRDELKKLYAQLEIYKRKKMITNNPHLQKKRCSKKGLGRSIMRRITEIPETVSRQCSKEDKDGGEHGSAKGSSAGRKNPQETAGGSGKPKEESLRSRVFSLKKSHSTYEHVREQPGGPGSPPAQSREEEEATDNSVLGSPVGANRPRPLQEDSQAVSTESVPLVCKSASAHNLSSEKKPGPTRTSVLQKSLSVIASAKEKTLGLAGKTQAACVEERAKAQKALPRERETNRKYSNSDNAETQDSAPPNSSHSEEPRKPQKLGIMKQQRANPTTANSDLSPGATHMKDNFDIGEVCPWEIYDLAPGPGPLESKVQKHVSIAASEMERNPTFSLKEKSHPKPKAADLCQQSNPKSVDKAEVCPWESQGQSLFEEEKYLMSKTQVPLGRAQGENSGQHCATGVCAGQCEELPPKAVASKVENENLNQLGEQEKKTSSSERNVPDSHNSSNNFQPPLMSRAEVCPWEFETPDKPNAERSVAFPASSALSANKIAGPRNEEVRLARKV | ||||||
Glycosylation | 98 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 99↔272 | |||||
Sequence: CSSRYELAGLPGKSPALASSHPSLHGALDTLTHATNFLNMMLQSNKSREQNLQDDLEWYQALVRSLLEGEPSISRAAITFSTESLSAPAPQVFLQATREESRILLQDLSSSAHHLANATLETEWFHGLRRKWRTHLHRRGSNQGPRGLGHSWRRRDGLSGDKSHVKWSPPYLEC | ||||||
Glycosylation | 143 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 215 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 274 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 333 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 481↔573 | |||||
Sequence: CILLRWVRLLGFATVYGTVTLKLHRVLKVFLSRTAQRIPYMTGGRVMRMLAVILLVVFWFLVGWTSSVCQNLERHISLIGQGRTSDHLIFSMC | ||||||
Modified residue | 694 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 705 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 708 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 774 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 866 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 947 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1066 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1081 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer. Associates with the RGS7-GNB5 complex, promoting its localization to the cell membrane and regulating its GTPase activator activity. Interacts (via VCPWE motifs) with GNAO1 (By similarity).
Interacts with GPC4 (By similarity).
Interacts with EGFLAM (By similarity).
Interacts with GPC4 (By similarity).
Interacts with EGFLAM (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 25-65 | Disordered | ||||
Sequence: SREAPSRPDPPRERTLRAKQHAQQPARASASDPSAPWSRST | ||||||
Compositional bias | 30-44 | Basic and acidic residues | ||||
Sequence: SRPDPPRERTLRAKQ | ||||||
Compositional bias | 46-65 | Polar residues | ||||
Sequence: AQQPARASASDPSAPWSRST | ||||||
Region | 85-281 | Cache-like region | ||||
Sequence: YLYTGDSHKLKRANCSSRYELAGLPGKSPALASSHPSLHGALDTLTHATNFLNMMLQSNKSREQNLQDDLEWYQALVRSLLEGEPSISRAAITFSTESLSAPAPQVFLQATREESRILLQDLSSSAHHLANATLETEWFHGLRRKWRTHLHRRGSNQGPRGLGHSWRRRDGLSGDKSHVKWSPPYLECENGSYKPGW | ||||||
Region | 757-875 | Disordered | ||||
Sequence: RITEIPETVSRQCSKEDKDGGEHGSAKGSSAGRKNPQETAGGSGKPKEESLRSRVFSLKKSHSTYEHVREQPGGPGSPPAQSREEEEATDNSVLGSPVGANRPRPLQEDSQAVSTESVP | ||||||
Compositional bias | 766-780 | Basic and acidic residues | ||||
Sequence: SRQCSKEDKDGGEHG | ||||||
Compositional bias | 801-823 | Basic and acidic residues | ||||
Sequence: KPKEESLRSRVFSLKKSHSTYEH | ||||||
Region | 911-1000 | Disordered | ||||
Sequence: KEKTLGLAGKTQAACVEERAKAQKALPRERETNRKYSNSDNAETQDSAPPNSSHSEEPRKPQKLGIMKQQRANPTTANSDLSPGATHMKD | ||||||
Compositional bias | 931-947 | Basic and acidic residues | ||||
Sequence: KAQKALPRERETNRKYS | ||||||
Compositional bias | 948-965 | Polar residues | ||||
Sequence: NSDNAETQDSAPPNSSHS | ||||||
Compositional bias | 978-995 | Polar residues | ||||
Sequence: KQQRANPTTANSDLSPGA | ||||||
Motif | 1007-1011 | VCPWE motif 1 | ||||
Sequence: VCPWE | ||||||
Region | 1038-1072 | Disordered | ||||
Sequence: ERNPTFSLKEKSHPKPKAADLCQQSNPKSVDKAEV | ||||||
Motif | 1072-1076 | VCPWE motif 2 | ||||
Sequence: VCPWE | ||||||
Region | 1128-1167 | Disordered | ||||
Sequence: SKVENENLNQLGEQEKKTSSSERNVPDSHNSSNNFQPPLM | ||||||
Compositional bias | 1151-1166 | Polar residues | ||||
Sequence: NVPDSHNSSNNFQPPL | ||||||
Motif | 1172-1176 | VCPWE motif 3 | ||||
Sequence: VCPWE |
Domain
The Cache-like region shares similarity with the Cache domain, a well-known receptor for amino acids. It acts as a ligand-binding module that recognizes and binds glycine and taurine.
Sequence similarities
Belongs to the G-protein coupled receptor 3 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,216
- Mass (Da)135,363
- Last updated2011-11-16 v2
- Checksum5B83D2CCA66D6ED1
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 30-44 | Basic and acidic residues | ||||
Sequence: SRPDPPRERTLRAKQ | ||||||
Compositional bias | 46-65 | Polar residues | ||||
Sequence: AQQPARASASDPSAPWSRST | ||||||
Compositional bias | 766-780 | Basic and acidic residues | ||||
Sequence: SRQCSKEDKDGGEHG | ||||||
Compositional bias | 801-823 | Basic and acidic residues | ||||
Sequence: KPKEESLRSRVFSLKKSHSTYEH | ||||||
Compositional bias | 931-947 | Basic and acidic residues | ||||
Sequence: KAQKALPRERETNRKYS | ||||||
Compositional bias | 948-965 | Polar residues | ||||
Sequence: NSDNAETQDSAPPNSSHS | ||||||
Compositional bias | 978-995 | Polar residues | ||||
Sequence: KQQRANPTTANSDLSPGA | ||||||
Compositional bias | 1151-1166 | Polar residues | ||||
Sequence: NVPDSHNSSNNFQPPL |
Keywords
- Technical term