G5E8Q8 · AGRF5_MOUSE

  • Protein
    Adhesion G protein-coupled receptor F5
  • Gene
    Adgrf5
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Features

Showing features for site.

113481002003004005006007008009001,0001,1001,2001,300
TypeIDPosition(s)Description
Site51-52Cleavage; by furin
Site223-224Cleavage
Site992-993Cleavage; by autolysis

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentapical part of cell
Cellular Componentcell surface
Cellular Componentcytoplasmic vesicle
Cellular Componentplasma membrane
Molecular FunctionG protein-coupled receptor activity
Biological Processadenylate cyclase-activating G protein-coupled receptor signaling pathway
Biological Processcell surface receptor signaling pathway
Biological Processenergy reserve metabolic process
Biological Processerythrocyte development
Biological Processfat cell differentiation
Biological Processglomerular filtration
Biological Processglucose homeostasis
Biological Processmacrophage activation
Biological Processnegative regulation of macrophage activation
Biological Processpharyngeal arch artery morphogenesis
Biological Processphospholipid biosynthetic process
Biological Processpositive regulation of phospholipid biosynthetic process
Biological Processregulation of lipid metabolic process
Biological Processsurfactant homeostasis

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Adhesion G protein-coupled receptor F5
  • Alternative names
    • G-protein coupled receptor 116

Gene names

    • Name
      Adgrf5
    • Synonyms
      Gpr116

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    G5E8Q8

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain22-1019Extracellular
Transmembrane1020-1040Helical
Topological domain1041-1055Cytoplasmic
Transmembrane1056-1076Helical
Topological domain1077-1092Extracellular
Transmembrane1093-1113Helical
Topological domain1114-1130Cytoplasmic
Transmembrane1131-1151Helical
Topological domain1152-1175Extracellular
Transmembrane1176-1196Helical
Topological domain1197-1221Cytoplasmic
Transmembrane1222-1242Helical
Topological domain1243-1250Extracellular
Transmembrane1251-1271Helical
Topological domain1272-1348Cytoplasmic

Keywords

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.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond, modified residue.

TypeIDPosition(s)Description
Signal1-21
ChainPRO_000043356422-1348Adhesion G protein-coupled receptor F5
Glycosylation270N-linked (GlcNAc...) asparagine
Glycosylation286N-linked (GlcNAc...) asparagine
Disulfide bond291↔348
Glycosylation337N-linked (GlcNAc...) asparagine
Glycosylation349N-linked (GlcNAc...) asparagine
Disulfide bond389↔447
Glycosylation470N-linked (GlcNAc...) asparagine
Disulfide bond490↔543
Glycosylation538N-linked (GlcNAc...) asparagine
Glycosylation665N-linked (GlcNAc...) asparagine
Modified residue818Phosphoserine
Disulfide bond953↔987
Disulfide bond972↔989
Modified residue1302Phosphothreonine
Modified residue1309Phosphoserine

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

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.

TypeIDPosition(s)Description
Domain163-271SEA
Domain268-366Ig-like 1
Domain367-464Ig-like 2
Domain469-559Ig-like 3
Domain841-1005GAIN-B
Region953-1005GPS
Region1328-1348Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Protein family/group databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,348
  • Mass (Da)
    149,387
  • Last updated
    2011-12-14 v1
  • Checksum
    BC2CDA96C63B7018
MRSPRTFTFYFLLLVICSSEAALSTPTEPIVQPSILQEHELAGEELLRPKRAAAAGDRVAEEYMVDIEISFENVSFLESIRAHLNNLSFPIRGTEADILNIAMTTVCTPAGNDLLCFCEKGYQWSEERCLHSLTCQDYDSALPGGYCSCLKGLPPQGPFCQLPEAFITLKLKVRLNIGFQEDLKNTSSALYRSYKTDLERAFRAGYRTLPGFRSVTVTQFTKGSVVVNYVVRVTSAPLPGSIHKANEQVIQNLNHTYKMDYNSFQGTPSNETKFTVIPEFIFEGDNVTLECETEFVTSNTSWYYGEKRSDIQNSDKYSIHTTVINNISLITRLTIYNFTQHDAGMYGCNVTLDIFEYGTVRKLDVTPIRILAKEERKVVCDNHPISLNCCSENIANWSSIEWKQEGKISILGNPESDLESSCSTYTLKADGTQCPSGSSGTTVIYTCEFVSAYGARGSKNIAVTFTSVANLTITRDPISVSEGQSFSITCLSDVSSFDEVYWNTSAGIKIHPRFYTMRRYQDGAESVLMVKTSTREWNGTYHCIFRYKNSYSIATKDVTVHPLPLVSDIMMDPLEASGLCTSSHQFKCCVEEDAGEEYAVTFHVDSSSFPAEREVIGKQACYTYSLPANLPRCPKDIAVFCHFTNAANSSVRSPSMKLKLIPRENVTCQDPIIGIGDPGKVIQKLCQFSGVYGSPGQAIGGTVTYKCVGTQWKEESRACISAPINGLLQVAKALIKSPTQDQKLPTYLRDLSVSAGKEEQDIRSSPGSLGAIISILDLLSTVPTQVNSEMMRDILATINVILDKSALNSWEKLLQQQSNQSSQFLHSVERFSQALQLGDSTPPFLAHPNVQMKSMVIKRGHPQIYQQQFIFKDSDLWGDVAIDECQLGNLQPDSSIVTVAFPTLKAILAQDVQRKTSSNSLVMTTTVSHNIVKPFRISMTFKNNHRSGGKPQCVFWNFSLANNTGGWDSSGCSVEDDGRDNRDRVFCKCNHLTSFSILMSPDSPDPGSLLKILLDIISYIGLGFSIVSLAACLVVEAMVWKSVTKNRTSYMRHICIVNIAFCLLIADIWFIVAGAIHDGRYPLNETACVAATFFIHFFYLSVFFWMLTLGLMLFYRLIFILHDASKSTQKAIAFSLGYGCPLIISSITVGVTQPQEVYMRKNACWLNWEDTRALLAFAIPALIIVVVNVSITVVVITKILRPSIGDKPGKQEKSSLFQISKSIGVLTPLLGLTWGFGLATVIQGSNAVFHIIFTLLNAFQGLFILLFGCLWDQKVQEALLHKFSLSRWSSQHSKSTSIGSSTPVFSMSSPISRRFNNLFGKTGTYNVSTPETTSSSLENSSSAYSLLN

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A286YD74A0A286YD74_MOUSEAdgrf5142
A0A286YCD3A0A286YCD3_MOUSEAdgrf5149
A0A286YDT5A0A286YDT5_MOUSEAdgrf51143
A0A286YE42A0A286YE42_MOUSEAdgrf582

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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