Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0007165 | biological_process | signal transduction |
R | 0004930 | molecular_function | G protein-coupled receptor activity |
R | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
R | 0016020 | cellular_component | membrane |
R | 0016492 | molecular_function | G protein-coupled neurotensin receptor activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue PIO R 400 |
Chain | Residue |
B | LYS250 |
B | LYS324 |
B | LYS326 |
R | PHE86 |
R | ALA89 |
R | TYR103 |
R | LEU110 |
R | ARG182 |
Functional Information from PROSITE/UniProt
site_id | PS00237 |
Number of Residues | 17 |
Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ATAlNVASLSVERYLaI |
Chain | Residue | Details |
R | ALA154-ILE170 | |
site_id | PS00295 |
Number of Residues | 19 |
Details | ARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL |
Chain | Residue | Details |
B | PHE61-LEU79 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Site: {"description":"Cleavage; by MME","evidences":[{"source":"PubMed","id":"6208535","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Site: {"description":"Cleavage; by ACE and MME","evidences":[{"source":"PubMed","id":"6208535","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 41 |
Details | Region: {"description":"Interaction with CHRM2","evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 32 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI8 |
Number of Residues | 19 |
Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI9 |
Number of Residues | 64 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI10 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI12 |
Number of Residues | 24 |
Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI13 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI14 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI15 |
Number of Residues | 23 |
Details | Region: {"description":"Neurotensin binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"21725197","evidenceCode":"ECO:0000305"}]} |