7MJS
Single-Particle Cryo-EM Structure of Major Facilitator Superfamily Domain containing 2A in complex with LPC-18:3
Functional Information from GO Data
Chain | GOid | namespace | contents |
X | 0005783 | cellular_component | endoplasmic reticulum |
X | 0005789 | cellular_component | endoplasmic reticulum membrane |
X | 0005886 | cellular_component | plasma membrane |
X | 0006869 | biological_process | lipid transport |
X | 0008643 | biological_process | carbohydrate transport |
X | 0015245 | molecular_function | fatty acid transmembrane transporter activity |
X | 0015293 | molecular_function | symporter activity |
X | 0015908 | biological_process | fatty acid transport |
X | 0016020 | cellular_component | membrane |
X | 0051977 | biological_process | lysophospholipid transport |
X | 0051978 | molecular_function | lysophospholipid:sodium symporter activity |
X | 0055085 | biological_process | transmembrane transport |
X | 0140329 | biological_process | lysophospholipid translocation |
X | 1990379 | biological_process | lipid transport across blood-brain barrier |
Functional Information from PROSITE/UniProt
site_id | PS00092 |
Number of Residues | 7 |
Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. CIENPPF |
Chain | Residue | Details |
X | CYS207-PHE213 |
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH |
Chain | Residue | Details |
L | TYR195-HIS201 | |
H | TYR213-HIS219 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 268 |
Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"34135507","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7MJS","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 83 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"34135507","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7MJS","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 26 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"34135507","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7MJS","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 22 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34135507","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7MJS","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |