5SY1
Structure of the STRA6 receptor for retinol uptake in complex with calmodulin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005516 | molecular_function | calmodulin binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0016918 | molecular_function | retinal binding |
| A | 0019841 | molecular_function | retinol binding |
| A | 0034632 | molecular_function | retinol transmembrane transporter activity |
| A | 0034633 | biological_process | retinol transport |
| A | 0038023 | molecular_function | signaling receptor activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043009 | biological_process | chordate embryonic development |
| A | 0060090 | molecular_function | molecular adaptor activity |
| A | 0071939 | biological_process | vitamin A import into cell |
| B | 0005516 | molecular_function | calmodulin binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0016918 | molecular_function | retinal binding |
| B | 0019841 | molecular_function | retinol binding |
| B | 0034632 | molecular_function | retinol transmembrane transporter activity |
| B | 0034633 | biological_process | retinol transport |
| B | 0038023 | molecular_function | signaling receptor activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043009 | biological_process | chordate embryonic development |
| B | 0060090 | molecular_function | molecular adaptor activity |
| B | 0071939 | biological_process | vitamin A import into cell |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0030234 | molecular_function | enzyme regulator activity |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0030234 | molecular_function | enzyme regulator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CA C 201 |
| Chain | Residue |
| C | ASP94 |
| C | ASP96 |
| C | ASN98 |
| C | PHE100 |
| C | GLU105 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CA C 202 |
| Chain | Residue |
| C | ALA129 |
| C | ASP132 |
| C | ASP134 |
| C | GLN136 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CA C 203 |
| Chain | Residue |
| C | ASP21 |
| C | ASP23 |
| C | ASP25 |
| C | THR27 |
| C | GLU32 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CA C 204 |
| Chain | Residue |
| C | ASP57 |
| C | ASP59 |
| C | ASN61 |
| C | THR63 |
| C | GLU68 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue CLR A 701 |
| Chain | Residue |
| A | LEU419 |
| A | VAL420 |
| A | ASN519 |
| A | ILE520 |
| B | VAL512 |
| B | THR515 |
| B | CLR701 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CLR B 701 |
| Chain | Residue |
| A | VAL512 |
| A | THR515 |
| A | CLR701 |
| B | VAL420 |
| B | ASN519 |
| B | ILE520 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CA D 201 |
| Chain | Residue |
| D | ASP94 |
| D | ASP96 |
| D | ASN98 |
| D | PHE100 |
| D | GLU105 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CA D 202 |
| Chain | Residue |
| D | ALA129 |
| D | ASP132 |
| D | ASP134 |
| D | GLN136 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue CA D 203 |
| Chain | Residue |
| D | ASP21 |
| D | ASP23 |
| D | ASP25 |
| D | THR27 |
| D | GLU32 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue CA D 204 |
| Chain | Residue |
| D | ASP57 |
| D | ASP59 |
| D | ASN61 |
| D | THR63 |
| D | GLU68 |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL |
| Chain | Residue | Details |
| C | ASP21-LEU33 | |
| C | ASP57-PHE69 | |
| C | ASP94-LEU106 | |
| C | ASP130-PHE142 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 286 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:27563101 |
| Chain | Residue | Details |
| A | MET1-GLY38 | |
| B | ILE423-TRP452 | |
| A | HIS109-GLU121 | |
| A | GLN167-ALA182 | |
| A | GLY296-VAL346 | |
| A | ILE423-TRP452 | |
| B | MET1-GLY38 | |
| B | HIS109-GLU121 | |
| B | GLN167-ALA182 | |
| B | GLY296-VAL346 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 360 |
| Details | TRANSMEM: Helical => ECO:0000269|PubMed:27563101 |
| Chain | Residue | Details |
| A | LEU39-ALA59 | |
| B | LEU39-ALA59 | |
| B | GLY88-HIS108 | |
| B | PHE122-GLY142 | |
| B | ASN146-TRP166 | |
| B | LEU183-LEU203 | |
| B | LEU275-SER295 | |
| B | SER347-HIS367 | |
| B | PHE402-PHE422 | |
| B | PRO453-PHE473 | |
| A | GLY88-HIS108 | |
| A | PHE122-GLY142 | |
| A | ASN146-TRP166 | |
| A | LEU183-LEU203 | |
| A | LEU275-SER295 | |
| A | SER347-HIS367 | |
| A | PHE402-PHE422 | |
| A | PRO453-PHE473 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 578 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:27563101 |
| Chain | Residue | Details |
| A | ARG60-LYS87 | |
| B | ARG368-GLY401 | |
| B | ILE474-SER488 | |
| B | ASP527-ASN670 | |
| A | THR143-HIS145 | |
| A | LEU204-LYS274 | |
| A | ARG368-GLY401 | |
| A | ILE474-SER488 | |
| A | ASP527-ASN670 | |
| B | ARG60-LYS87 | |
| B | THR143-HIS145 | |
| B | LEU204-LYS274 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 74 |
| Details | INTRAMEM: Helical => ECO:0000269|PubMed:27563101 |
| Chain | Residue | Details |
| A | LEU489-LEU526 | |
| B | LEU489-LEU526 |
