Q6F3F9 · AGRG6_MOUSE
- ProteinAdhesion G-protein coupled receptor G6
- GeneAdgrg6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1165 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
G-protein coupled receptor which is activated by type IV collagen, a major constituent of the basement membrane. Essential for normal differentiation of promyelinating Schwann cells and for normal myelination of axons these functions are mediated via G-protein-signaling pathways (PubMed:21613327, PubMed:24227709).
Regulates also neural, cardiac and ear development via G-protein- and/or N-terminus-dependent signaling. May act as a receptor for PRNP which may promote myelin homeostasis (PubMed:27501152).
Regulates also neural, cardiac and ear development via G-protein- and/or N-terminus-dependent signaling. May act as a receptor for PRNP which may promote myelin homeostasis (PubMed:27501152).
ADGRG6 N-terminal fragment
Plays an important role in heart developmention (PubMed:24082093).
Necessary and sufficient for axon sorting by Schwann cells independently of the ADGRG6-CTF (PubMed:25695270).
Necessary and sufficient for axon sorting by Schwann cells independently of the ADGRG6-CTF (PubMed:25695270).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 440-441 | Cleavage; by furin like-convertase | ||||
Sequence: RD | ||||||
Site | 810-811 | Cleavage | ||||
Sequence: FT |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | collagen binding | |
Molecular Function | extracellular matrix binding | |
Molecular Function | G protein-coupled receptor activity | |
Molecular Function | laminin binding | |
Biological Process | adenylate cyclase-activating G protein-coupled receptor signaling pathway | |
Biological Process | cAMP-mediated signaling | |
Biological Process | cell surface receptor signaling pathway | |
Biological Process | G protein-coupled receptor signaling pathway | |
Biological Process | heart trabecula formation | |
Biological Process | mitochondrion organization | |
Biological Process | myelination | |
Biological Process | myelination in peripheral nervous system |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdhesion G-protein coupled receptor G6
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ6F3F9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 31-832 | Extracellular | ||||
Sequence: VPLSVCGCGSCRLVLSNPSGTFTSPCYPNDYPNTQSCSWTLRAPAGYIIQITFNDFDIEEAPNCIYDSLSLDNGESQTKFCGATAKGLSFNSSVNEMHVSFSSDFSIQKKGFNASYIRVAVSLRNQKVILPQTLDAYQVSVAKSISIPELKAFTLCFEASKVGNEGGDWTAFSYSDESLTQLLSLEKASNGYFLSISGSRCLLNNALPVKDKEDIFTENLEQLCLVWNNSWGSIGINFKKNYETVPCDSTISAVVPGDGTLLLGSDRDEVASLRGSIYNFRLWNFTMDLKALSNLSCSVSGNVIDWHNDFWSISTQALKAEGNLSCGSYLIQLPAAELTNCSELGTLCQDGIMYRISVVIHNDFNHPEVKVQTKVAEWLNSTFQNWNYTVYVVNISFHQKVGEDRMKVKRDIMDDDKRLVLWALLVYNATNNVSLNEEKIKQKLMTNNASLEDGLRLCEVDVNQLGMCSALEDPDGFSWPATLPSVYKQPCPNKPGFFMTRACLSNGTSTFWGPVDTSNCSRQSNEVANEILNQTGDGQNLTSANINSIVEKVKRIVNKEENIDITLGSTLMNIFSNILSSSDSDLLESSTEALKTIDELAFKIDLNSTPHVNIETQNLALGVSSLIPGTNAPSNFSIGLPSNNESYFQMDFGNGQTDPLASVILPPNLLENLSPEDSVLVRRAQFTFFNKTGLFQDVGSQRKVLVSYVMACSIGNITIQNLKDPVQIKIKHTRTQEVHHPICAFWDMNKNKSFGGWNTSGCVAHSDLDAGETICLCSHFTHFGVLMDLPRSASQIDGRNTK | ||||||
Transmembrane | 833-853 | Helical; Name=1 | ||||
Sequence: VLTFITYIGCGISAIFSAATL | ||||||
Topological domain | 854-873 | Cytoplasmic | ||||
Sequence: LTYVAFEKLRRDYPSKILMN | ||||||
Transmembrane | 874-894 | Helical; Name=2 | ||||
Sequence: LSSALLFLNLIFLLDGWVTSF | ||||||
Topological domain | 895-899 | Extracellular | ||||
Sequence: GVAGL | ||||||
Transmembrane | 900-920 | Helical; Name=3 | ||||
Sequence: CTAVAALLHFFLLATFTWMGL | ||||||
Topological domain | 921-940 | Cytoplasmic | ||||
Sequence: EAIHMYIALVKVFNTYIHRY | ||||||
Transmembrane | 941-961 | Helical; Name=4 | ||||
Sequence: ILKFCIIGWGLPALVVSIILV | ||||||
Topological domain | 962-994 | Extracellular | ||||
Sequence: SRRQNEVYGKESYGKDQDDEFCWIQDPVVFYVS | ||||||
Transmembrane | 995-1015 | Helical; Name=5 | ||||
Sequence: CAGYFGVMFFLNVAMFIVVMV | ||||||
Topological domain | 1016-1039 | Cytoplasmic | ||||
Sequence: QICGRNGKRSNRTLREEVLRNLRS | ||||||
Transmembrane | 1040-1060 | Helical; Name=6 | ||||
Sequence: VVSLTFLLGMTWGFAFFAWGP | ||||||
Topological domain | 1061-1062 | Extracellular | ||||
Sequence: LN | ||||||
Transmembrane | 1063-1083 | Helical; Name=7 | ||||
Sequence: IPFMYLFSIFNSLQGLFIFIF | ||||||
Topological domain | 1084-1165 | Cytoplasmic | ||||
Sequence: HCAMKENVQKQWRRHLCCGRFRLADNSDWSKTATNIIKKSSDNLGKSLSSSSIGSNSTYLTSKSKSSSTTYFKRNSHSDNFS |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Deficient mice die during organogenesis. Mutant embryos show signs of myocardial wall thinning, hypotrabeculation, defective mitochondrial and circulatory failure.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 55 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MMFDTLGKRCCPWRLKPSALLFLFVLCVTC | ||||||
Chain | PRO_0000438598 | 31-440 | ADGRG6 N-terminal fragment | |||
Sequence: VPLSVCGCGSCRLVLSNPSGTFTSPCYPNDYPNTQSCSWTLRAPAGYIIQITFNDFDIEEAPNCIYDSLSLDNGESQTKFCGATAKGLSFNSSVNEMHVSFSSDFSIQKKGFNASYIRVAVSLRNQKVILPQTLDAYQVSVAKSISIPELKAFTLCFEASKVGNEGGDWTAFSYSDESLTQLLSLEKASNGYFLSISGSRCLLNNALPVKDKEDIFTENLEQLCLVWNNSWGSIGINFKKNYETVPCDSTISAVVPGDGTLLLGSDRDEVASLRGSIYNFRLWNFTMDLKALSNLSCSVSGNVIDWHNDFWSISTQALKAEGNLSCGSYLIQLPAAELTNCSELGTLCQDGIMYRISVVIHNDFNHPEVKVQTKVAEWLNSTFQNWNYTVYVVNISFHQKVGEDRMKVKR | ||||||
Chain | PRO_0000303888 | 31-1165 | Adhesion G-protein coupled receptor G6 | |||
Sequence: VPLSVCGCGSCRLVLSNPSGTFTSPCYPNDYPNTQSCSWTLRAPAGYIIQITFNDFDIEEAPNCIYDSLSLDNGESQTKFCGATAKGLSFNSSVNEMHVSFSSDFSIQKKGFNASYIRVAVSLRNQKVILPQTLDAYQVSVAKSISIPELKAFTLCFEASKVGNEGGDWTAFSYSDESLTQLLSLEKASNGYFLSISGSRCLLNNALPVKDKEDIFTENLEQLCLVWNNSWGSIGINFKKNYETVPCDSTISAVVPGDGTLLLGSDRDEVASLRGSIYNFRLWNFTMDLKALSNLSCSVSGNVIDWHNDFWSISTQALKAEGNLSCGSYLIQLPAAELTNCSELGTLCQDGIMYRISVVIHNDFNHPEVKVQTKVAEWLNSTFQNWNYTVYVVNISFHQKVGEDRMKVKRDIMDDDKRLVLWALLVYNATNNVSLNEEKIKQKLMTNNASLEDGLRLCEVDVNQLGMCSALEDPDGFSWPATLPSVYKQPCPNKPGFFMTRACLSNGTSTFWGPVDTSNCSRQSNEVANEILNQTGDGQNLTSANINSIVEKVKRIVNKEENIDITLGSTLMNIFSNILSSSDSDLLESSTEALKTIDELAFKIDLNSTPHVNIETQNLALGVSSLIPGTNAPSNFSIGLPSNNESYFQMDFGNGQTDPLASVILPPNLLENLSPEDSVLVRRAQFTFFNKTGLFQDVGSQRKVLVSYVMACSIGNITIQNLKDPVQIKIKHTRTQEVHHPICAFWDMNKNKSFGGWNTSGCVAHSDLDAGETICLCSHFTHFGVLMDLPRSASQIDGRNTKVLTFITYIGCGISAIFSAATLLTYVAFEKLRRDYPSKILMNLSSALLFLNLIFLLDGWVTSFGVAGLCTAVAALLHFFLLATFTWMGLEAIHMYIALVKVFNTYIHRYILKFCIIGWGLPALVVSIILVSRRQNEVYGKESYGKDQDDEFCWIQDPVVFYVSCAGYFGVMFFLNVAMFIVVMVQICGRNGKRSNRTLREEVLRNLRSVVSLTFLLGMTWGFAFFAWGPLNIPFMYLFSIFNSLQGLFIFIFHCAMKENVQKQWRRHLCCGRFRLADNSDWSKTATNIIKKSSDNLGKSLSSSSIGSNSTYLTSKSKSSSTTYFKRNSHSDNFS | ||||||
Disulfide bond | 41↔67 | |||||
Sequence: CRLVLSNPSGTFTSPCYPNDYPNTQSC | ||||||
Disulfide bond | 94↔111 | |||||
Sequence: CIYDSLSLDNGESQTKFC | ||||||
Glycosylation | 121 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 143 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 186↔254 | |||||
Sequence: CFEASKVGNEGGDWTAFSYSDESLTQLLSLEKASNGYFLSISGSRCLLNNALPVKDKEDIFTENLEQLC | ||||||
Glycosylation | 258 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 314 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 324 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 353 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 370 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 410 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 417 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 424 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000438599 | 441-1165 | ADGRG6 C-terminal fragment | |||
Sequence: DIMDDDKRLVLWALLVYNATNNVSLNEEKIKQKLMTNNASLEDGLRLCEVDVNQLGMCSALEDPDGFSWPATLPSVYKQPCPNKPGFFMTRACLSNGTSTFWGPVDTSNCSRQSNEVANEILNQTGDGQNLTSANINSIVEKVKRIVNKEENIDITLGSTLMNIFSNILSSSDSDLLESSTEALKTIDELAFKIDLNSTPHVNIETQNLALGVSSLIPGTNAPSNFSIGLPSNNESYFQMDFGNGQTDPLASVILPPNLLENLSPEDSVLVRRAQFTFFNKTGLFQDVGSQRKVLVSYVMACSIGNITIQNLKDPVQIKIKHTRTQEVHHPICAFWDMNKNKSFGGWNTSGCVAHSDLDAGETICLCSHFTHFGVLMDLPRSASQIDGRNTKVLTFITYIGCGISAIFSAATLLTYVAFEKLRRDYPSKILMNLSSALLFLNLIFLLDGWVTSFGVAGLCTAVAALLHFFLLATFTWMGLEAIHMYIALVKVFNTYIHRYILKFCIIGWGLPALVVSIILVSRRQNEVYGKESYGKDQDDEFCWIQDPVVFYVSCAGYFGVMFFLNVAMFIVVMVQICGRNGKRSNRTLREEVLRNLRSVVSLTFLLGMTWGFAFFAWGPLNIPFMYLFSIFNSLQGLFIFIFHCAMKENVQKQWRRHLCCGRFRLADNSDWSKTATNIIKKSSDNLGKSLSSSSIGSNSTYLTSKSKSSSTTYFKRNSHSDNFS | ||||||
Glycosylation | 458 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 462 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 478 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 536 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 549 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 563 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 570 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 665 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 674 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 720 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 746 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 773↔805 | |||||
Sequence: CAFWDMNKNKSFGGWNTSGCVAHSDLDAGETIC | ||||||
Glycosylation | 781 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 788 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 792↔807 | |||||
Sequence: CVAHSDLDAGETICLC | ||||||
Modified residue | 1135 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1138 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Proteolytically cleaved into 2 conserved sites: one in the GPS region of the GAIN-B domain (S1 site) and the other in the middle of the extracellular domain (S2 site). The proteolytic cleavage at S1 site generates an N-terminal fragment (NTF) and a seven-transmembrane-containing C-terminal fragment (CTF). The membrane-bound CTF can act as an independent receptor and the soluble NTF can act as a ligand or coreceptor. Furin is involved in the cleavage of the S2 site generating a soluble fragment. Processing at the GPS region occurred independent of and probably prior to the cleavage at the S2 site. Proteolytic cleavage is required for activation of the receptor (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at high levels in the heart, somite and otic vesicle during embryogenesis and in adult lung.
Gene expression databases
Interaction
Subunit
Interacts with Laminin-2; this interaction stabilizes the receptor in an inactive state (PubMed:25695270).
Laminin-2 polymerization could facilitate ADGRG6-NTF removal, thereby exposing the tethered agonist to drive myelination (PubMed:25695270).
Interacts with PRNP (PubMed:27501152).
Laminin-2 polymerization could facilitate ADGRG6-NTF removal, thereby exposing the tethered agonist to drive myelination (PubMed:25695270).
Interacts with PRNP (PubMed:27501152).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 41-149 | CUB | ||||
Sequence: CRLVLSNPSGTFTSPCYPNDYPNTQSCSWTLRAPAGYIIQITFNDFDIEEAPNCIYDSLSLDNGESQTKFCGATAKGLSFNSSVNEMHVSFSSDFSIQKKGFNASYIRV | ||||||
Region | 41-355 | Mediates interaction with type IV collagen | ||||
Sequence: CRLVLSNPSGTFTSPCYPNDYPNTQSCSWTLRAPAGYIIQITFNDFDIEEAPNCIYDSLSLDNGESQTKFCGATAKGLSFNSSVNEMHVSFSSDFSIQKKGFNASYIRVAVSLRNQKVILPQTLDAYQVSVAKSISIPELKAFTLCFEASKVGNEGGDWTAFSYSDESLTQLLSLEKASNGYFLSISGSRCLLNNALPVKDKEDIFTENLEQLCLVWNNSWGSIGINFKKNYETVPCDSTISAVVPGDGTLLLGSDRDEVASLRGSIYNFRLWNFTMDLKALSNLSCSVSGNVIDWHNDFWSISTQALKAEGNLS | ||||||
Region | 41-822 | Inhibits receptor signaling in absence of type IV collagen | ||||
Sequence: CRLVLSNPSGTFTSPCYPNDYPNTQSCSWTLRAPAGYIIQITFNDFDIEEAPNCIYDSLSLDNGESQTKFCGATAKGLSFNSSVNEMHVSFSSDFSIQKKGFNASYIRVAVSLRNQKVILPQTLDAYQVSVAKSISIPELKAFTLCFEASKVGNEGGDWTAFSYSDESLTQLLSLEKASNGYFLSISGSRCLLNNALPVKDKEDIFTENLEQLCLVWNNSWGSIGINFKKNYETVPCDSTISAVVPGDGTLLLGSDRDEVASLRGSIYNFRLWNFTMDLKALSNLSCSVSGNVIDWHNDFWSISTQALKAEGNLSCGSYLIQLPAAELTNCSELGTLCQDGIMYRISVVIHNDFNHPEVKVQTKVAEWLNSTFQNWNYTVYVVNISFHQKVGEDRMKVKRDIMDDDKRLVLWALLVYNATNNVSLNEEKIKQKLMTNNASLEDGLRLCEVDVNQLGMCSALEDPDGFSWPATLPSVYKQPCPNKPGFFMTRACLSNGTSTFWGPVDTSNCSRQSNEVANEILNQTGDGQNLTSANINSIVEKVKRIVNKEENIDITLGSTLMNIFSNILSSSDSDLLESSTEALKTIDELAFKIDLNSTPHVNIETQNLALGVSSLIPGTNAPSNFSIGLPSNNESYFQMDFGNGQTDPLASVILPPNLLENLSPEDSVLVRRAQFTFFNKTGLFQDVGSQRKVLVSYVMACSIGNITIQNLKDPVQIKIKHTRTQEVHHPICAFWDMNKNKSFGGWNTSGCVAHSDLDAGETICLCSHFTHFGVLMDLPRS | ||||||
Domain | 154-356 | Pentraxin (PTX) | ||||
Sequence: RNQKVILPQTLDAYQVSVAKSISIPELKAFTLCFEASKVGNEGGDWTAFSYSDESLTQLLSLEKASNGYFLSISGSRCLLNNALPVKDKEDIFTENLEQLCLVWNNSWGSIGINFKKNYETVPCDSTISAVVPGDGTLLLGSDRDEVASLRGSIYNFRLWNFTMDLKALSNLSCSVSGNVIDWHNDFWSISTQALKAEGNLSC | ||||||
Region | 446-807 | Mediates interaction with laminin-2 | ||||
Sequence: DKRLVLWALLVYNATNNVSLNEEKIKQKLMTNNASLEDGLRLCEVDVNQLGMCSALEDPDGFSWPATLPSVYKQPCPNKPGFFMTRACLSNGTSTFWGPVDTSNCSRQSNEVANEILNQTGDGQNLTSANINSIVEKVKRIVNKEENIDITLGSTLMNIFSNILSSSDSDLLESSTEALKTIDELAFKIDLNSTPHVNIETQNLALGVSSLIPGTNAPSNFSIGLPSNNESYFQMDFGNGQTDPLASVILPPNLLENLSPEDSVLVRRAQFTFFNKTGLFQDVGSQRKVLVSYVMACSIGNITIQNLKDPVQIKIKHTRTQEVHHPICAFWDMNKNKSFGGWNTSGCVAHSDLDAGETICLC | ||||||
Domain | 640-823 | GAIN-B | ||||
Sequence: PHVNIETQNLALGVSSLIPGTNAPSNFSIGLPSNNESYFQMDFGNGQTDPLASVILPPNLLENLSPEDSVLVRRAQFTFFNKTGLFQDVGSQRKVLVSYVMACSIGNITIQNLKDPVQIKIKHTRTQEVHHPICAFWDMNKNKSFGGWNTSGCVAHSDLDAGETICLCSHFTHFGVLMDLPRSA | ||||||
Region | 773-823 | GPS | ||||
Sequence: CAFWDMNKNKSFGGWNTSGCVAHSDLDAGETICLCSHFTHFGVLMDLPRSA | ||||||
Motif | 812-820 | STACHEL | ||||
Sequence: HFGVLMDLP | ||||||
Region | 1126-1165 | Disordered | ||||
Sequence: NLGKSLSSSSIGSNSTYLTSKSKSSSTTYFKRNSHSDNFS |
Sequence similarities
Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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.
- Length1,165
- Mass (Da)129,721
- Last updated2004-08-16 v1
- ChecksumB5CC5CDEAA42CB50
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A571BEJ4 | A0A571BEJ4_MOUSE | Adgrg6 | 1220 | ||
A0A140LIH4 | A0A140LIH4_MOUSE | Adgrg6 | 1193 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB183545 EMBL· GenBank· DDBJ | BAD27570.1 EMBL· GenBank· DDBJ | mRNA | ||
BC046534 EMBL· GenBank· DDBJ | AAH46534.1 EMBL· GenBank· DDBJ | mRNA |