7S8X
Cryo-EM Structure of dolphin Prestin: Sensor Up (compact) state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007605 | biological_process | sensory perception of sound |
| A | 0008271 | molecular_function | secondary active sulfate transmembrane transporter activity |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0016020 | cellular_component | membrane |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0099129 | biological_process | cochlear outer hair cell electromotile response |
| A | 1902358 | biological_process | sulfate transmembrane transport |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007605 | biological_process | sensory perception of sound |
| B | 0008271 | molecular_function | secondary active sulfate transmembrane transporter activity |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0016020 | cellular_component | membrane |
| B | 0055085 | biological_process | transmembrane transport |
| B | 0099129 | biological_process | cochlear outer hair cell electromotile response |
| B | 1902358 | biological_process | sulfate transmembrane transport |
Functional Information from PROSITE/UniProt
| site_id | PS01130 |
| Number of Residues | 22 |
| Details | SLC26A SLC26A transporters signature. PvFGLYSSfypvIMYcffGTSR |
| Chain | Residue | Details |
| A | PRO109-ARG130 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 50 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 210 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 72 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 58 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=5a","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Intramembrane: {"description":"Helical; Name=5b","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 34 |
| Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 36 |
| Details | Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 30 |
| Details | Transmembrane: {"description":"Helical; Name=13","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical; Name=14","evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 20 |
| Details | Motif: {"description":"Involved in motor function","evidences":[{"source":"UniProtKB","id":"Q9JKQ2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"34695838","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S9E","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 2 |
| Details | Site: {"description":"Controls the electromotile activity","evidences":[{"source":"UniProtKB","id":"A0FKN5","evidenceCode":"ECO:0000250"},{"source":"UniProtKB","id":"Q9EPH0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | Site: {"description":"Contributes to anion binding","evidences":[{"source":"UniProtKB","id":"Q9EPH0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
