7KYA
Structure of the S. cerevisiae phosphatidylcholine flippase Dnf2-Lem3 complex in the E2P state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005215 | molecular_function | transporter activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005935 | cellular_component | cellular bud neck |
| A | 0006869 | biological_process | lipid transport |
| A | 0006897 | biological_process | endocytosis |
| A | 0007163 | biological_process | establishment or maintenance of cell polarity |
| A | 0015031 | biological_process | protein transport |
| A | 0015247 | molecular_function | aminophospholipid flippase activity |
| A | 0015914 | biological_process | phospholipid transport |
| A | 0016020 | cellular_component | membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0045332 | biological_process | phospholipid translocation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070867 | cellular_component | mating projection tip membrane |
| A | 0071944 | cellular_component | cell periphery |
| A | 0090554 | molecular_function | phosphatidylcholine floppase activity |
| A | 0090556 | molecular_function | phosphatidylserine floppase activity |
| A | 0099040 | biological_process | ceramide translocation |
| A | 0140326 | molecular_function | ATPase-coupled intramembrane lipid transporter activity |
| A | 0140331 | biological_process | aminophospholipid translocation |
| A | 0140346 | molecular_function | phosphatidylserine flippase activity |
| A | 0140351 | molecular_function | glycosylceramide flippase activity |
| A | 1990531 | cellular_component | phospholipid-translocating ATPase complex |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007166 | biological_process | cell surface receptor signaling pathway |
| B | 0015247 | molecular_function | aminophospholipid flippase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0044088 | biological_process | regulation of vacuole organization |
| B | 0045332 | biological_process | phospholipid translocation |
| B | 0140331 | biological_process | aminophospholipid translocation |
| B | 0140345 | molecular_function | phosphatidylcholine flippase activity |
| B | 1990531 | cellular_component | phospholipid-translocating ATPase complex |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 240 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 46 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 34 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Region: {"description":"Involved in phosphatidylcholine substrate selection","evidences":[{"source":"UniProtKB","id":"P32660","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Active site: {"description":"4-aspartylphosphate intermediate","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y2Q0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33320091","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7KY9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P32660","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P39524","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33320091","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7KY8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33320091","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7KY8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7KY9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8NB49","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"G0S196","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in the release of the transported lipid into the cytosolic leaflet","evidences":[{"source":"UniProtKB","id":"C7EXK4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 276 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 20 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 14 |
| Details | Region: {"description":"Required for localization to the plasma membrane","evidences":[{"source":"PubMed","id":"33320091","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"33320091","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"33320091","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7KY5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
