G5E8Q8 · AGRF5_MOUSE
- ProteinAdhesion G protein-coupled receptor F5
- GeneAdgrf5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1348 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor that plays a critical role in lung surfactant homeostasis (PubMed:23590306, PubMed:23684610, PubMed:23922714).
May play a role in controlling adipocyte function (PubMed:22971422).
May play a role in controlling adipocyte function (PubMed:22971422).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 51-52 | Cleavage; by furin | ||||
Sequence: RA | ||||||
Site | 223-224 | Cleavage | ||||
Sequence: GS | ||||||
Site | 992-993 | Cleavage; by autolysis | ||||
Sequence: LT |
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 | apical part of cell | |
Cellular Component | cell surface | |
Cellular Component | cytoplasmic vesicle | |
Cellular Component | plasma membrane | |
Molecular Function | G protein-coupled receptor activity | |
Biological Process | adenylate cyclase-activating G protein-coupled receptor signaling pathway | |
Biological Process | cell surface receptor signaling pathway | |
Biological Process | energy reserve metabolic process | |
Biological Process | erythrocyte development | |
Biological Process | fat cell differentiation | |
Biological Process | glomerular filtration | |
Biological Process | glucose homeostasis | |
Biological Process | macrophage activation | |
Biological Process | negative regulation of macrophage activation | |
Biological Process | pharyngeal arch artery morphogenesis | |
Biological Process | phospholipid biosynthetic process | |
Biological Process | positive regulation of phospholipid biosynthetic process | |
Biological Process | regulation of lipid metabolic process | |
Biological Process | surfactant homeostasis |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAdhesion G protein-coupled receptor F5
- Alternative names
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 accessionG5E8Q8
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 | 22-1019 | Extracellular | ||||
Sequence: ALSTPTEPIVQPSILQEHELAGEELLRPKRAAAAGDRVAEEYMVDIEISFENVSFLESIRAHLNNLSFPIRGTEADILNIAMTTVCTPAGNDLLCFCEKGYQWSEERCLHSLTCQDYDSALPGGYCSCLKGLPPQGPFCQLPEAFITLKLKVRLNIGFQEDLKNTSSALYRSYKTDLERAFRAGYRTLPGFRSVTVTQFTKGSVVVNYVVRVTSAPLPGSIHKANEQVIQNLNHTYKMDYNSFQGTPSNETKFTVIPEFIFEGDNVTLECETEFVTSNTSWYYGEKRSDIQNSDKYSIHTTVINNISLITRLTIYNFTQHDAGMYGCNVTLDIFEYGTVRKLDVTPIRILAKEERKVVCDNHPISLNCCSENIANWSSIEWKQEGKISILGNPESDLESSCSTYTLKADGTQCPSGSSGTTVIYTCEFVSAYGARGSKNIAVTFTSVANLTITRDPISVSEGQSFSITCLSDVSSFDEVYWNTSAGIKIHPRFYTMRRYQDGAESVLMVKTSTREWNGTYHCIFRYKNSYSIATKDVTVHPLPLVSDIMMDPLEASGLCTSSHQFKCCVEEDAGEEYAVTFHVDSSSFPAEREVIGKQACYTYSLPANLPRCPKDIAVFCHFTNAANSSVRSPSMKLKLIPRENVTCQDPIIGIGDPGKVIQKLCQFSGVYGSPGQAIGGTVTYKCVGTQWKEESRACISAPINGLLQVAKALIKSPTQDQKLPTYLRDLSVSAGKEEQDIRSSPGSLGAIISILDLLSTVPTQVNSEMMRDILATINVILDKSALNSWEKLLQQQSNQSSQFLHSVERFSQALQLGDSTPPFLAHPNVQMKSMVIKRGHPQIYQQQFIFKDSDLWGDVAIDECQLGNLQPDSSIVTVAFPTLKAILAQDVQRKTSSNSLVMTTTVSHNIVKPFRISMTFKNNHRSGGKPQCVFWNFSLANNTGGWDSSGCSVEDDGRDNRDRVFCKCNHLTSFSILMSPDSPDPGSLLKILLDIISY | ||||||
Transmembrane | 1020-1040 | Helical | ||||
Sequence: IGLGFSIVSLAACLVVEAMVW | ||||||
Topological domain | 1041-1055 | Cytoplasmic | ||||
Sequence: KSVTKNRTSYMRHIC | ||||||
Transmembrane | 1056-1076 | Helical | ||||
Sequence: IVNIAFCLLIADIWFIVAGAI | ||||||
Topological domain | 1077-1092 | Extracellular | ||||
Sequence: HDGRYPLNETACVAAT | ||||||
Transmembrane | 1093-1113 | Helical | ||||
Sequence: FFIHFFYLSVFFWMLTLGLML | ||||||
Topological domain | 1114-1130 | Cytoplasmic | ||||
Sequence: FYRLIFILHDASKSTQK | ||||||
Transmembrane | 1131-1151 | Helical | ||||
Sequence: AIAFSLGYGCPLIISSITVGV | ||||||
Topological domain | 1152-1175 | Extracellular | ||||
Sequence: TQPQEVYMRKNACWLNWEDTRALL | ||||||
Transmembrane | 1176-1196 | Helical | ||||
Sequence: AFAIPALIIVVVNVSITVVVI | ||||||
Topological domain | 1197-1221 | Cytoplasmic | ||||
Sequence: TKILRPSIGDKPGKQEKSSLFQISK | ||||||
Transmembrane | 1222-1242 | Helical | ||||
Sequence: SIGVLTPLLGLTWGFGLATVI | ||||||
Topological domain | 1243-1250 | Extracellular | ||||
Sequence: QGSNAVFH | ||||||
Transmembrane | 1251-1271 | Helical | ||||
Sequence: IIFTLLNAFQGLFILLFGCLW | ||||||
Topological domain | 1272-1348 | Cytoplasmic | ||||
Sequence: DQKVQEALLHKFSLSRWSSQHSKSTSIGSSTPVFSMSSPISRRFNNLFGKTGTYNVSTPETTSSSLENSSSAYSLLN |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Deficient mice exhibit premature death, decreased body weight and respiratory distress associated with pulmonary alveolar proteinosis.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 81 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MRSPRTFTFYFLLLVICSSEA | ||||||
Chain | PRO_0000433564 | 22-1348 | Adhesion G protein-coupled receptor F5 | |||
Sequence: ALSTPTEPIVQPSILQEHELAGEELLRPKRAAAAGDRVAEEYMVDIEISFENVSFLESIRAHLNNLSFPIRGTEADILNIAMTTVCTPAGNDLLCFCEKGYQWSEERCLHSLTCQDYDSALPGGYCSCLKGLPPQGPFCQLPEAFITLKLKVRLNIGFQEDLKNTSSALYRSYKTDLERAFRAGYRTLPGFRSVTVTQFTKGSVVVNYVVRVTSAPLPGSIHKANEQVIQNLNHTYKMDYNSFQGTPSNETKFTVIPEFIFEGDNVTLECETEFVTSNTSWYYGEKRSDIQNSDKYSIHTTVINNISLITRLTIYNFTQHDAGMYGCNVTLDIFEYGTVRKLDVTPIRILAKEERKVVCDNHPISLNCCSENIANWSSIEWKQEGKISILGNPESDLESSCSTYTLKADGTQCPSGSSGTTVIYTCEFVSAYGARGSKNIAVTFTSVANLTITRDPISVSEGQSFSITCLSDVSSFDEVYWNTSAGIKIHPRFYTMRRYQDGAESVLMVKTSTREWNGTYHCIFRYKNSYSIATKDVTVHPLPLVSDIMMDPLEASGLCTSSHQFKCCVEEDAGEEYAVTFHVDSSSFPAEREVIGKQACYTYSLPANLPRCPKDIAVFCHFTNAANSSVRSPSMKLKLIPRENVTCQDPIIGIGDPGKVIQKLCQFSGVYGSPGQAIGGTVTYKCVGTQWKEESRACISAPINGLLQVAKALIKSPTQDQKLPTYLRDLSVSAGKEEQDIRSSPGSLGAIISILDLLSTVPTQVNSEMMRDILATINVILDKSALNSWEKLLQQQSNQSSQFLHSVERFSQALQLGDSTPPFLAHPNVQMKSMVIKRGHPQIYQQQFIFKDSDLWGDVAIDECQLGNLQPDSSIVTVAFPTLKAILAQDVQRKTSSNSLVMTTTVSHNIVKPFRISMTFKNNHRSGGKPQCVFWNFSLANNTGGWDSSGCSVEDDGRDNRDRVFCKCNHLTSFSILMSPDSPDPGSLLKILLDIISYIGLGFSIVSLAACLVVEAMVWKSVTKNRTSYMRHICIVNIAFCLLIADIWFIVAGAIHDGRYPLNETACVAATFFIHFFYLSVFFWMLTLGLMLFYRLIFILHDASKSTQKAIAFSLGYGCPLIISSITVGVTQPQEVYMRKNACWLNWEDTRALLAFAIPALIIVVVNVSITVVVITKILRPSIGDKPGKQEKSSLFQISKSIGVLTPLLGLTWGFGLATVIQGSNAVFHIIFTLLNAFQGLFILLFGCLWDQKVQEALLHKFSLSRWSSQHSKSTSIGSSTPVFSMSSPISRRFNNLFGKTGTYNVSTPETTSSSLENSSSAYSLLN | ||||||
Glycosylation | 270 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 286 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 291↔348 | |||||
Sequence: CETEFVTSNTSWYYGEKRSDIQNSDKYSIHTTVINNISLITRLTIYNFTQHDAGMYGC | ||||||
Glycosylation | 337 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 349 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 389↔447 | |||||
Sequence: CCSENIANWSSIEWKQEGKISILGNPESDLESSCSTYTLKADGTQCPSGSSGTTVIYTC | ||||||
Glycosylation | 470 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 490↔543 | |||||
Sequence: CLSDVSSFDEVYWNTSAGIKIHPRFYTMRRYQDGAESVLMVKTSTREWNGTYHC | ||||||
Glycosylation | 538 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 665 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 818 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 953↔987 | |||||
Sequence: CVFWNFSLANNTGGWDSSGCSVEDDGRDNRDRVFC | ||||||
Disulfide bond | 972↔989 | |||||
Sequence: CSVEDDGRDNRDRVFCKC | ||||||
Modified residue | 1302 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1309 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Highly glycosylated.
Proteolytically cleaved at multiple sites: one in the GPS region of the GAIN-B domain (S1 site) and the other in the SEA domain (S2 site). The proteolytic cleavage at S1 site generates an extracellular subunit and a seven-transmembrane subunit. The proteolytic cleavage at S2 site generates a fragment that undergoes proteolytic cleavage by the processing enzyme furin.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed and highly expressed in the lung. In the lung predominantly expressed in the alveolar type II epithelial cells.
Gene expression databases
Interaction
Subunit
Homodimer; disulfide-linked. Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment and the membrane-bound C-terminal fragment predominantly remain associated and non-covalently linked. Fragment generates by the processing enzyme furin remains attached to the extracellular N-terminal fragment. Interacts (via N-terminal extracellular domain) with SFTPD (PubMed:23922714).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 163-271 | SEA | ||||
Sequence: PEAFITLKLKVRLNIGFQEDLKNTSSALYRSYKTDLERAFRAGYRTLPGFRSVTVTQFTKGSVVVNYVVRVTSAPLPGSIHKANEQVIQNLNHTYKMDYNSFQGTPSNE | ||||||
Domain | 268-366 | Ig-like 1 | ||||
Sequence: PSNETKFTVIPEFIFEGDNVTLECETEFVTSNTSWYYGEKRSDIQNSDKYSIHTTVINNISLITRLTIYNFTQHDAGMYGCNVTLDIFEYGTVRKLDVT | ||||||
Domain | 367-464 | Ig-like 2 | ||||
Sequence: PIRILAKEERKVVCDNHPISLNCCSENIANWSSIEWKQEGKISILGNPESDLESSCSTYTLKADGTQCPSGSSGTTVIYTCEFVSAYGARGSKNIAVT | ||||||
Domain | 469-559 | Ig-like 3 | ||||
Sequence: ANLTITRDPISVSEGQSFSITCLSDVSSFDEVYWNTSAGIKIHPRFYTMRRYQDGAESVLMVKTSTREWNGTYHCIFRYKNSYSIATKDVT | ||||||
Domain | 841-1005 | GAIN-B | ||||
Sequence: TPPFLAHPNVQMKSMVIKRGHPQIYQQQFIFKDSDLWGDVAIDECQLGNLQPDSSIVTVAFPTLKAILAQDVQRKTSSNSLVMTTTVSHNIVKPFRISMTFKNNHRSGGKPQCVFWNFSLANNTGGWDSSGCSVEDDGRDNRDRVFCKCNHLTSFSILMSPDSPD | ||||||
Region | 953-1005 | GPS | ||||
Sequence: CVFWNFSLANNTGGWDSSGCSVEDDGRDNRDRVFCKCNHLTSFSILMSPDSPD | ||||||
Region | 1328-1348 | Disordered | ||||
Sequence: STPETTSSSLENSSSAYSLLN |
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.
- Length1,348
- Mass (Da)149,387
- Last updated2011-12-14 v1
- ChecksumBC2CDA96C63B7018
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A286YD74 | A0A286YD74_MOUSE | Adgrf5 | 142 | ||
A0A286YCD3 | A0A286YCD3_MOUSE | Adgrf5 | 149 | ||
A0A286YDT5 | A0A286YDT5_MOUSE | Adgrf5 | 1143 | ||
A0A286YE42 | A0A286YE42_MOUSE | Adgrf5 | 82 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC169504 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CT010585 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CT025700 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466559 EMBL· GenBank· DDBJ | EDL23401.1 EMBL· GenBank· DDBJ | Genomic DNA |