8S3E
Structure of rabbit Slo1 in complex with gamma1/LRRC26
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005267 | molecular_function | potassium channel activity |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0022839 | molecular_function | monoatomic ion-gated channel activity |
| A | 0034702 | cellular_component | monoatomic ion channel complex |
| A | 0042311 | biological_process | vasodilation |
| A | 0042391 | biological_process | regulation of membrane potential |
| A | 0045211 | cellular_component | postsynaptic membrane |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0060072 | molecular_function | large conductance calcium-activated potassium channel activity |
| A | 0071805 | biological_process | potassium ion transmembrane transport |
| A | 0099094 | molecular_function | ligand-gated monoatomic cation channel activity |
| B | 0005267 | molecular_function | potassium channel activity |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0022839 | molecular_function | monoatomic ion-gated channel activity |
| B | 0034702 | cellular_component | monoatomic ion channel complex |
| B | 0042311 | biological_process | vasodilation |
| B | 0042391 | biological_process | regulation of membrane potential |
| B | 0045211 | cellular_component | postsynaptic membrane |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0060072 | molecular_function | large conductance calcium-activated potassium channel activity |
| B | 0071805 | biological_process | potassium ion transmembrane transport |
| B | 0099094 | molecular_function | ligand-gated monoatomic cation channel activity |
| C | 0005267 | molecular_function | potassium channel activity |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005789 | cellular_component | endoplasmic reticulum membrane |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0022839 | molecular_function | monoatomic ion-gated channel activity |
| C | 0034702 | cellular_component | monoatomic ion channel complex |
| C | 0042311 | biological_process | vasodilation |
| C | 0042391 | biological_process | regulation of membrane potential |
| C | 0045211 | cellular_component | postsynaptic membrane |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0060072 | molecular_function | large conductance calcium-activated potassium channel activity |
| C | 0071805 | biological_process | potassium ion transmembrane transport |
| C | 0099094 | molecular_function | ligand-gated monoatomic cation channel activity |
| D | 0005267 | molecular_function | potassium channel activity |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005789 | cellular_component | endoplasmic reticulum membrane |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0022839 | molecular_function | monoatomic ion-gated channel activity |
| D | 0034702 | cellular_component | monoatomic ion channel complex |
| D | 0042311 | biological_process | vasodilation |
| D | 0042391 | biological_process | regulation of membrane potential |
| D | 0045211 | cellular_component | postsynaptic membrane |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0060072 | molecular_function | large conductance calcium-activated potassium channel activity |
| D | 0071805 | biological_process | potassium ion transmembrane transport |
| D | 0099094 | molecular_function | ligand-gated monoatomic cation channel activity |
Functional Information from PROSITE/UniProt
| site_id | PS00092 |
| Number of Residues | 7 |
| Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. VITNPPY |
| Chain | Residue | Details |
| A | VAL1033-TYR1039 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S0 => ECO:0000255 |
| Chain | Residue | Details |
| A | TRP22-LEU42 | |
| B | TRP22-LEU42 | |
| C | TRP22-LEU42 | |
| D | TRP22-LEU42 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3504 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| A | TRP43-ARG113 | |
| C | ALA171-LYS174 | |
| C | LEU221-LEU235 | |
| C | GLU324-LEU1113 | |
| D | TRP43-ARG113 | |
| D | ALA171-LYS174 | |
| D | LEU221-LEU235 | |
| D | GLU324-LEU1113 | |
| A | ALA171-LYS174 | |
| A | LEU221-LEU235 | |
| A | GLU324-LEU1113 | |
| B | TRP43-ARG113 | |
| B | ALA171-LYS174 | |
| B | LEU221-LEU235 | |
| B | GLU324-LEU1113 | |
| C | TRP43-ARG113 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S1 => ECO:0000255 |
| Chain | Residue | Details |
| A | VAL114-SER134 | |
| B | VAL114-SER134 | |
| C | VAL114-SER134 | |
| D | VAL114-SER134 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 152 |
| Details | TOPO_DOM: Extracellular => ECO:0000255 |
| Chain | Residue | Details |
| A | SER135-THR149 | |
| C | SER196-LEU199 | |
| C | GLU257-GLN270 | |
| C | TYR294-LEU302 | |
| D | SER135-THR149 | |
| D | SER196-LEU199 | |
| D | GLU257-GLN270 | |
| D | TYR294-LEU302 | |
| A | SER196-LEU199 | |
| A | GLU257-GLN270 | |
| A | TYR294-LEU302 | |
| B | SER135-THR149 | |
| B | SER196-LEU199 | |
| B | GLU257-GLN270 | |
| B | TYR294-LEU302 | |
| C | SER135-THR149 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S2 => ECO:0000255 |
| Chain | Residue | Details |
| A | LEU150-ALA170 | |
| B | LEU150-ALA170 | |
| C | LEU150-ALA170 | |
| D | LEU150-ALA170 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S3 => ECO:0000255 |
| Chain | Residue | Details |
| A | LEU175-VAL195 | |
| B | LEU175-VAL195 | |
| C | LEU175-VAL195 | |
| D | LEU175-VAL195 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Voltage-sensor; Name=Segment S4 => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN200-ILE220 | |
| B | ASN200-ILE220 | |
| C | ASN200-ILE220 | |
| D | ASN200-ILE220 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S5 => ECO:0000255 |
| Chain | Residue | Details |
| A | VAL236-VAL256 | |
| B | VAL236-VAL256 | |
| C | VAL236-VAL256 | |
| D | VAL236-VAL256 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 88 |
| Details | INTRAMEM: Pore-forming; Name=P region => ECO:0000255 |
| Chain | Residue | Details |
| A | ALA271-VAL293 | |
| B | ALA271-VAL293 | |
| C | ALA271-VAL293 | |
| D | ALA271-VAL293 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Segment S6 => ECO:0000255 |
| Chain | Residue | Details |
| A | PHE303-ILE323 | |
| B | PHE303-ILE323 | |
| C | PHE303-ILE323 | |
| D | PHE303-ILE323 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | GLU374 | |
| D | GLU374 | |
| D | GLN397 | |
| D | GLU399 | |
| A | GLN397 | |
| A | GLU399 | |
| B | GLU374 | |
| B | GLN397 | |
| B | GLU399 | |
| C | GLU374 | |
| C | GLN397 | |
| C | GLU399 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:B7ZC96 |
| Chain | Residue | Details |
| A | GLN889 | |
| C | ASP892 | |
| C | ASP895 | |
| C | ASP897 | |
| D | GLN889 | |
| D | ASP892 | |
| D | ASP895 | |
| D | ASP897 | |
| A | ASP892 | |
| A | ASP895 | |
| A | ASP897 | |
| B | GLN889 | |
| B | ASP892 | |
| B | ASP895 | |
| B | ASP897 | |
| C | GLN889 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q08460 |
| Chain | Residue | Details |
| A | THR640 | |
| A | THR847 | |
| B | THR640 | |
| B | THR847 | |
| C | THR640 | |
| C | THR847 | |
| D | THR640 | |
| D | THR847 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 20 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q08460 |
| Chain | Residue | Details |
| A | SER642 | |
| B | SER859 | |
| C | SER642 | |
| C | SER655 | |
| C | SER659 | |
| C | SER855 | |
| C | SER859 | |
| D | SER642 | |
| D | SER655 | |
| D | SER659 | |
| D | SER855 | |
| A | SER655 | |
| D | SER859 | |
| A | SER659 | |
| A | SER855 | |
| A | SER859 | |
| B | SER642 | |
| B | SER655 | |
| B | SER659 | |
| B | SER855 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q28204 |
| Chain | Residue | Details |
| A | SER1098 | |
| A | SER1101 | |
| B | SER1098 | |
| B | SER1101 | |
| C | SER1098 | |
| C | SER1101 | |
| D | SER1098 | |
| D | SER1101 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 12 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS53 | |
| D | CYS53 | |
| D | CYS54 | |
| D | CYS56 | |
| A | CYS54 | |
| A | CYS56 | |
| B | CYS53 | |
| B | CYS54 | |
| B | CYS56 | |
| C | CYS53 | |
| C | CYS54 | |
| C | CYS56 |
