P13945 · ADRB3_HUMAN
- ProteinBeta-3 adrenergic receptor
- GeneADRB3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids408 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis.
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 | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBeta-3 adrenergic receptor
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP13945
- 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 | 1-36 | Extracellular | ||||
Sequence: MAPWPHENSSLAPWPDLPTLAPNTANTSGLPGVPWE | ||||||
Transmembrane | 37-63 | Helical; Name=1 | ||||
Sequence: AALAGALLALAVLATVGGNLLVIVAIA | ||||||
Topological domain | 64-72 | Cytoplasmic | ||||
Sequence: WTPRLQTMT | ||||||
Transmembrane | 73-91 | Helical; Name=2 | ||||
Sequence: NVFVTSLAAADLVMGLLVV | ||||||
Topological domain | 92-111 | Extracellular | ||||
Sequence: PPAATLALTGHWPLGATGCE | ||||||
Transmembrane | 112-133 | Helical; Name=3 | ||||
Sequence: LWTSVDVLCVTASIETLCALAV | ||||||
Topological domain | 134-155 | Cytoplasmic | ||||
Sequence: DRYLAVTNPLRYGALVTKRCAR | ||||||
Transmembrane | 156-178 | Helical; Name=4 | ||||
Sequence: TAVVLVWVVSAAVSFAPIMSQWW | ||||||
Topological domain | 179-203 | Extracellular | ||||
Sequence: RVGADAEAQRCHSNPRCCAFASNMP | ||||||
Transmembrane | 204-225 | Helical; Name=5 | ||||
Sequence: YVLLSSSVSFYLPLLVMLFVYA | ||||||
Topological domain | 226-292 | Cytoplasmic | ||||
Sequence: RVFVVATRQLRLLRGELGRFPPEESPPAPSRSLAPAPVGTCAPPEGVPACGRRPARLLPLREHRALC | ||||||
Transmembrane | 293-314 | Helical; Name=6 | ||||
Sequence: TLGLIMGTFTLCWLPFFLANVL | ||||||
Topological domain | 315-326 | Extracellular | ||||
Sequence: RALGGPSLVPGP | ||||||
Transmembrane | 327-347 | Helical; Name=7 | ||||
Sequence: AFLALNWLGYANSAFNPLIYC | ||||||
Topological domain | 348-408 | Cytoplasmic | ||||
Sequence: RSPDFRSAFRRLLCRCGRRLPPEPCAAARPALFPSGVPAARSSPAQPRLCQRLDGASWGVS |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_003456 | 64 | in dbSNP:rs4994 | |||
Sequence: W → R | ||||||
Natural variant | VAR_029205 | 249 | in dbSNP:rs28364012 | |||
Sequence: E → K | ||||||
Natural variant | VAR_014166 | 265 | in dbSNP:rs4995 | |||
Sequence: T → M | ||||||
Natural variant | VAR_025102 | 353 | in dbSNP:rs36031925 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 612 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond, modified residue (large scale data), lipidation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000069143 | 1-408 | UniProt | Beta-3 adrenergic receptor | |||
Sequence: MAPWPHENSSLAPWPDLPTLAPNTANTSGLPGVPWEAALAGALLALAVLATVGGNLLVIVAIAWTPRLQTMTNVFVTSLAAADLVMGLLVVPPAATLALTGHWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRCARTAVVLVWVVSAAVSFAPIMSQWWRVGADAEAQRCHSNPRCCAFASNMPYVLLSSSVSFYLPLLVMLFVYARVFVVATRQLRLLRGELGRFPPEESPPAPSRSLAPAPVGTCAPPEGVPACGRRPARLLPLREHRALCTLGLIMGTFTLCWLPFFLANVLRALGGPSLVPGPAFLALNWLGYANSAFNPLIYCRSPDFRSAFRRLLCRCGRRLPPEPCAAARPALFPSGVPAARSSPAQPRLCQRLDGASWGVS | |||||||
Glycosylation | 8 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 26 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 110↔196 | UniProt | |||||
Sequence: CELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRCARTAVVLVWVVSAAVSFAPIMSQWWRVGADAEAQRCHSNPRCC | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 145 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Disulfide bond | 189↔195 | UniProt | |||||
Sequence: CHSNPRC | |||||||
Lipidation | 361 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed mainly in adipose tissues.
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Sequence similarities
Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB3 sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Length408
- Mass (Da)43,519
- Last updated1994-02-01 v3
- ChecksumE98BD6C130DD977B
Polymorphism
The variant Arg-64 seems to be associated with weight gain (obesity) and is also associated with susceptibility to non-insulin-dependent diabetes mellitus (NIDDM).
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M29932 EMBL· GenBank· DDBJ | AAA35550.1 EMBL· GenBank· DDBJ | Genomic DNA | Different termination. | |
X72861 EMBL· GenBank· DDBJ | CAA51383.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X70811 EMBL· GenBank· DDBJ | CAA50141.1 EMBL· GenBank· DDBJ | mRNA | ||
X70812 EMBL· GenBank· DDBJ | CAA50142.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
X70812 EMBL· GenBank· DDBJ | CAA50143.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AY487247 EMBL· GenBank· DDBJ | AAR37414.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ104441 EMBL· GenBank· DDBJ | AAY88743.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC075017 EMBL· GenBank· DDBJ | AAH75017.1 EMBL· GenBank· DDBJ | mRNA | ||
S53291 EMBL· GenBank· DDBJ | AAB24837.1 EMBL· GenBank· DDBJ | mRNA |