P48145 · NPBW1_HUMAN
- ProteinNeuropeptides B/W receptor type 1
- GeneNPBWR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids328 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Interacts specifically with a number of opioid ligands. Receptor for neuropeptides B and W, which may be involved in neuroendocrine system regulation, food intake and the organization of other signals. Has a higher affinity for neuropeptide B.
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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Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | neuron projection | |
Cellular Component | plasma membrane | |
Cellular Component | synapse | |
Molecular Function | G protein-coupled opioid receptor activity | |
Molecular Function | G protein-coupled receptor activity | |
Molecular Function | neuropeptide binding | |
Molecular Function | neuropeptide receptor activity | |
Biological Process | chemical synaptic transmission | |
Biological Process | G protein-coupled receptor signaling pathway | |
Biological Process | neuropeptide signaling pathway | |
Biological Process | regulation of metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNeuropeptides B/W receptor type 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP48145
- 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 | 1-37 | Extracellular | ||||
Sequence: MDNASFSEPWPANASGPDPALSCSNASTLAPLPAPLA | ||||||
Transmembrane | 38-61 | Helical; Name=1 | ||||
Sequence: VAVPVVYAVICAVGLAGNSAVLYV | ||||||
Topological domain | 62-72 | Cytoplasmic | ||||
Sequence: LLRAPRMKTVT | ||||||
Transmembrane | 73-97 | Helical; Name=2 | ||||
Sequence: NLFILNLAIADELFTLVLPINIADF | ||||||
Topological domain | 98-112 | Extracellular | ||||
Sequence: LLRQWPFGELMCKLI | ||||||
Transmembrane | 113-132 | Helical; Name=3 | ||||
Sequence: VAIDQYNTFSSLYFLTVMSA | ||||||
Topological domain | 133-157 | Cytoplasmic | ||||
Sequence: DRYLVVLATAESRRVAGRTYSAARA | ||||||
Transmembrane | 158-177 | Helical; Name=4 | ||||
Sequence: VSLAVWGIVTLVVLPFAVFA | ||||||
Topological domain | 178-202 | Extracellular | ||||
Sequence: RLDDEQGRRQCVLVFPQPEAFWWRA | ||||||
Transmembrane | 203-224 | Helical; Name=5 | ||||
Sequence: SRLYTLVLGFAIPVSTICVLYT | ||||||
Topological domain | 225-248 | Cytoplasmic | ||||
Sequence: TLLCRLHAMRLDSHAKALERAKKR | ||||||
Transmembrane | 249-273 | Helical; Name=6 | ||||
Sequence: VTFLVVAILAVCLLCWTPYHLSTVV | ||||||
Topological domain | 274-283 | Extracellular | ||||
Sequence: ALTTDLPQTP | ||||||
Transmembrane | 284-298 | Helical; Name=7 | ||||
Sequence: LVIAISYFITSLSYA | ||||||
Topological domain | 299-328 | Cytoplasmic | ||||
Sequence: NSCLNPFLYAFLDASFRRNLRQLITCRAAA |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035765 | 19 | in a breast cancer sample; somatic mutation; dbSNP:rs772418985 | |||
Sequence: P → Q | ||||||
Natural variant | VAR_047788 | 135 | in dbSNP:rs33977775 | |||
Sequence: Y → F | ||||||
Natural variant | VAR_047789 | 319 | in dbSNP:rs36068168 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 517 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000069518 | 1-328 | Neuropeptides B/W receptor type 1 | |||
Sequence: MDNASFSEPWPANASGPDPALSCSNASTLAPLPAPLAVAVPVVYAVICAVGLAGNSAVLYVLLRAPRMKTVTNLFILNLAIADELFTLVLPINIADFLLRQWPFGELMCKLIVAIDQYNTFSSLYFLTVMSADRYLVVLATAESRRVAGRTYSAARAVSLAVWGIVTLVVLPFAVFARLDDEQGRRQCVLVFPQPEAFWWRASRLYTLVLGFAIPVSTICVLYTTLLCRLHAMRLDSHAKALERAKKRVTFLVVAILAVCLLCWTPYHLSTVVALTTDLPQTPLVIAISYFITSLSYANSCLNPFLYAFLDASFRRNLRQLITCRAAA | ||||||
Glycosylation | 3 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 13 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 25 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 109↔188 | |||||
Sequence: CKLIVAIDQYNTFSSLYFLTVMSADRYLVVLATAESRRVAGRTYSAARAVSLAVWGIVTLVVLPFAVFARLDDEQGRRQC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Found in cerebellum and frontal cortex. Detected at high levels in hippocampus, amygdala and trachea; at moderate levels in fetal brain, pituitary gland and prostate. Not in caudate, accumbens, kidney or liver. Also detected at high levels in lung carcinoma.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P48145 | UBQLN2 Q9UHD9 | 3 | EBI-13061492, EBI-947187 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length328
- Mass (Da)36,103
- Last updated2008-11-25 v2
- Checksum7A90F85AD64A3980
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 296 | in Ref. 1; AAC50197 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U22491 EMBL· GenBank· DDBJ | AAC50197.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471068 EMBL· GenBank· DDBJ | EAW86722.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC069117 EMBL· GenBank· DDBJ | AAH69117.1 EMBL· GenBank· DDBJ | mRNA | ||
BC107101 EMBL· GenBank· DDBJ | AAI07102.1 EMBL· GenBank· DDBJ | mRNA |