7BSQ
Cryo-EM structure of a human ATP11C-CDC50A flippase in E1AlF-ADP 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 | 0005765 | cellular_component | lysosomal membrane |
A | 0005768 | cellular_component | endosome |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0005886 | cellular_component | plasma membrane |
A | 0006869 | biological_process | lipid transport |
A | 0012505 | cellular_component | endomembrane system |
A | 0015914 | biological_process | phospholipid transport |
A | 0016020 | cellular_component | membrane |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0031901 | cellular_component | early endosome membrane |
A | 0034220 | biological_process | monoatomic ion transmembrane transport |
A | 0045332 | biological_process | phospholipid translocation |
A | 0046872 | molecular_function | metal ion binding |
A | 0055037 | cellular_component | recycling endosome |
A | 0055038 | cellular_component | recycling endosome membrane |
A | 0090555 | molecular_function | phosphatidylethanolamine flippase activity |
A | 0090556 | molecular_function | phosphatidylserine floppase activity |
A | 0140326 | molecular_function | ATPase-coupled intramembrane lipid transporter activity |
A | 0140331 | biological_process | aminophospholipid translocation |
A | 0140346 | molecular_function | phosphatidylserine flippase activity |
A | 1990531 | cellular_component | phospholipid-translocating ATPase complex |
C | 0005198 | molecular_function | structural molecule activity |
C | 0005515 | molecular_function | protein binding |
C | 0005783 | cellular_component | endoplasmic reticulum |
C | 0005794 | cellular_component | Golgi apparatus |
C | 0005886 | cellular_component | plasma membrane |
C | 0006855 | biological_process | xenobiotic transmembrane transport |
C | 0006869 | biological_process | lipid transport |
C | 0010976 | biological_process | positive regulation of neuron projection development |
C | 0015247 | molecular_function | aminophospholipid flippase activity |
C | 0015917 | biological_process | aminophospholipid transport |
C | 0016020 | cellular_component | membrane |
C | 0016324 | cellular_component | apical plasma membrane |
C | 0030658 | cellular_component | transport vesicle membrane |
C | 0031410 | cellular_component | cytoplasmic vesicle |
C | 0031901 | cellular_component | early endosome membrane |
C | 0031902 | cellular_component | late endosome membrane |
C | 0035577 | cellular_component | azurophil granule membrane |
C | 0035579 | cellular_component | specific granule membrane |
C | 0036010 | biological_process | protein localization to endosome |
C | 0045332 | biological_process | phospholipid translocation |
C | 0061092 | biological_process | positive regulation of phospholipid translocation |
C | 0070863 | biological_process | positive regulation of protein exit from endoplasmic reticulum |
C | 0140331 | biological_process | aminophospholipid translocation |
C | 1990531 | cellular_component | phospholipid-translocating ATPase complex |
Functional Information from PROSITE/UniProt
site_id | PS00154 |
Number of Residues | 7 |
Details | ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT |
Chain | Residue | Details |
A | ASP409-THR415 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 238 |
Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 81 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 216 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Active site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"Q9Y2Q0","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 5 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y2Q0","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"32493773","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LKN","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Site: {"description":"Cleavage; by CASP3 and CASP7","evidences":[{"source":"PubMed","id":"24904167","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 254 |
Details | Topological domain: {"description":"Exoplasmic loop","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"31416931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6K7G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7M","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31416931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6K7G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7M","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31416931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6K7G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7M","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |