7SUN
Atomic model of prestin from gerbil (Meriones unguiculatus)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003674 | molecular_function | molecular_function |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006091 | biological_process | generation of precursor metabolites and energy |
| A | 0006821 | biological_process | chloride transport |
| A | 0007605 | biological_process | sensory perception of sound |
| A | 0008218 | biological_process | bioluminescence |
| A | 0008271 | molecular_function | secondary active sulfate transmembrane transporter activity |
| A | 0008272 | biological_process | obsolete sulfate transport |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0015106 | molecular_function | bicarbonate transmembrane transporter activity |
| A | 0015108 | molecular_function | chloride transmembrane transporter activity |
| A | 0015116 | molecular_function | sulfate transmembrane transporter activity |
| A | 0015701 | biological_process | bicarbonate transport |
| A | 0016020 | cellular_component | membrane |
| A | 0016323 | cellular_component | basolateral plasma membrane |
| A | 0016328 | cellular_component | lateral plasma membrane |
| A | 0019531 | molecular_function | oxalate transmembrane transporter activity |
| A | 0019532 | biological_process | oxalate transport |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0140900 | molecular_function | chloride:bicarbonate antiporter activity |
| A | 1902358 | biological_process | sulfate transmembrane transport |
| A | 1902476 | biological_process | chloride transmembrane transport |
| B | 0003674 | molecular_function | molecular_function |
| B | 0005575 | cellular_component | cellular_component |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006091 | biological_process | generation of precursor metabolites and energy |
| B | 0006821 | biological_process | chloride transport |
| B | 0007605 | biological_process | sensory perception of sound |
| B | 0008218 | biological_process | bioluminescence |
| B | 0008271 | molecular_function | secondary active sulfate transmembrane transporter activity |
| B | 0008272 | biological_process | obsolete sulfate transport |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0015106 | molecular_function | bicarbonate transmembrane transporter activity |
| B | 0015108 | molecular_function | chloride transmembrane transporter activity |
| B | 0015116 | molecular_function | sulfate transmembrane transporter activity |
| B | 0015701 | biological_process | bicarbonate transport |
| B | 0016020 | cellular_component | membrane |
| B | 0016323 | cellular_component | basolateral plasma membrane |
| B | 0016328 | cellular_component | lateral plasma membrane |
| B | 0019531 | molecular_function | oxalate transmembrane transporter activity |
| B | 0019532 | biological_process | oxalate transport |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0055085 | biological_process | transmembrane transport |
| B | 0140900 | molecular_function | chloride:bicarbonate antiporter activity |
| B | 1902358 | biological_process | sulfate transmembrane transport |
| B | 1902476 | biological_process | chloride 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 | 756 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| A | MET1-TYR79 | |
| B | PHE126-PHE137 | |
| B | ARG197-PRO208 | |
| B | LYS283-PRO291 | |
| B | ALA362-ASP370 | |
| B | GLY407-THR410 | |
| B | SER456-LEU469 | |
| B | THR498-ALA744 | |
| A | PHE126-PHE137 | |
| A | ARG197-PRO208 | |
| A | LYS283-PRO291 | |
| A | ALA362-ASP370 | |
| A | GLY407-THR410 | |
| A | SER456-LEU469 | |
| A | THR498-ALA744 | |
| B | MET1-TYR79 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 50 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | VAL80-ALA105 | |
| B | VAL80-ALA105 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 192 |
| Details | TOPO_DOM: Extracellular => ECO:0000305 |
| Chain | Residue | Details |
| A | ALA106-PRO109 | |
| B | ALA148-VAL178 | |
| B | GLY231-VAL243 | |
| B | ASN253-ASN258 | |
| B | ALA305-HIS337 | |
| B | GLN389-SER396 | |
| B | PHE430-PRO436 | |
| B | ASP485 | |
| A | ALA148-VAL178 | |
| A | GLY231-VAL243 | |
| A | ASN253-ASN258 | |
| A | ALA305-HIS337 | |
| A | GLN389-SER396 | |
| A | PHE430-PRO436 | |
| A | ASP485 | |
| B | ALA106-PRO109 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 30 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | VAL110-PHE125 | |
| B | VAL110-PHE125 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | ALA138-VAL147 | |
| B | ALA138-VAL147 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 34 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | ALA179-CYS196 | |
| B | ALA179-CYS196 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 42 |
| Details | TRANSMEM: Helical; Name=5a => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | LEU209-PHE230 | |
| B | LEU209-PHE230 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 16 |
| Details | INTRAMEM: Helical; Name=5b => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | VAL244-GLN252 | |
| B | VAL244-GLN252 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | VAL259-PHE282 | |
| B | VAL259-PHE282 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 24 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | LEU292-SER304 | |
| B | LEU292-SER304 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | LEU338-LEU361 | |
| B | LEU338-LEU361 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 34 |
| Details | TRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | GLY371-PHE388 | |
| B | GLY371-PHE388 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 18 |
| Details | TRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | LEU397-THR406 | |
| B | LEU397-THR406 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 36 |
| Details | TRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | GLN411-GLY429 | |
| B | GLN411-GLY429 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 36 |
| Details | TRANSMEM: Helical; Name=12 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | GLN437-PHE455 | |
| B | GLN437-PHE455 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 28 |
| Details | TRANSMEM: Helical; Name=13 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | THR470-LEU484 | |
| B | THR470-LEU484 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 22 |
| Details | TRANSMEM: Helical; Name=14 => ECO:0000269|PubMed:35022426, ECO:0007744|PDB:7SUN |
| Chain | Residue | Details |
| A | TYR486-LEU497 | |
| B | TYR486-LEU497 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P58743 |
| Chain | Residue | Details |
| A | SER398 | |
| B | SER398 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | SITE: Controls the electromotile activity => ECO:0000250|UniProtKB:A0FKN5, ECO:0000250|UniProtKB:Q9EPH0 |
| Chain | Residue | Details |
| A | SER398 | |
| B | SER398 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 2 |
| Details | SITE: Contributes to anion binding => ECO:0000250|UniProtKB:Q9EPH0 |
| Chain | Residue | Details |
| A | ARG399 | |
| B | ARG399 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN163 | |
| A | ASN166 | |
| B | ASN163 | |
| B | ASN166 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | MOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132 |
| Chain | Residue | Details |
| A | TYR819 | |
| B | TYR819 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 4 |
| Details | CROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 |
| Chain | Residue | Details |
| A | GLY818 | |
| A | GLY820 | |
| B | GLY818 | |
| B | GLY820 |
