Functional Information from GO Data
| Chain | GOid | namespace | contents |
| R | 0004930 | molecular_function | G protein-coupled receptor activity |
| R | 0005515 | molecular_function | protein binding |
| R | 0005886 | cellular_component | plasma membrane |
| R | 0007154 | biological_process | cell communication |
| R | 0007165 | biological_process | signal transduction |
| R | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| R | 0007218 | biological_process | neuropeptide signaling pathway |
| R | 0023052 | biological_process | signaling |
| R | 0042593 | biological_process | glucose homeostasis |
| R | 0042923 | molecular_function | neuropeptide binding |
| R | 0043005 | cellular_component | neuron projection |
| R | 0050727 | biological_process | regulation of inflammatory response |
| R | 0097003 | molecular_function | adipokinetic hormone receptor activity |
| R | 0097004 | molecular_function | adipokinetic hormone binding |
Functional Information from PROSITE/UniProt
| site_id | PS00295 |
| Number of Residues | 19 |
| Details | ARRESTINS Arrestins signature. FRYGrEDlDVLGLsFrKDL |
| Chain | Residue | Details |
| A | PHE62-LEU80 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Hydroxyproline; by PHD2","evidences":[{"source":"PubMed","id":"21255264","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P29067","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 41 |
| Details | Region: {"description":"Interaction with CHRM2","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 11 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 41 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 53 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 39 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 34 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
