8EOI
Structure of a human EMC:human Cav1.2 channel complex in GDN detergent
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0072546 | cellular_component | EMC complex |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0016020 | cellular_component | membrane |
B | 0032977 | molecular_function | membrane insertase activity |
B | 0042406 | cellular_component | extrinsic component of endoplasmic reticulum membrane |
B | 0045050 | biological_process | protein insertion into ER membrane by stop-transfer membrane-anchor sequence |
B | 0071816 | biological_process | tail-anchored membrane protein insertion into ER membrane |
B | 0072546 | cellular_component | EMC complex |
C | 0005515 | molecular_function | protein binding |
C | 0005783 | cellular_component | endoplasmic reticulum |
C | 0005789 | cellular_component | endoplasmic reticulum membrane |
C | 0016020 | cellular_component | membrane |
C | 0032977 | molecular_function | membrane insertase activity |
C | 0045050 | biological_process | protein insertion into ER membrane by stop-transfer membrane-anchor sequence |
C | 0071816 | biological_process | tail-anchored membrane protein insertion into ER membrane |
C | 0072546 | cellular_component | EMC complex |
D | 0005515 | molecular_function | protein binding |
D | 0005783 | cellular_component | endoplasmic reticulum |
D | 0005789 | cellular_component | endoplasmic reticulum membrane |
D | 0006915 | biological_process | apoptotic process |
D | 0016020 | cellular_component | membrane |
D | 0032977 | molecular_function | membrane insertase activity |
D | 0045050 | biological_process | protein insertion into ER membrane by stop-transfer membrane-anchor sequence |
D | 0071816 | biological_process | tail-anchored membrane protein insertion into ER membrane |
D | 0072546 | cellular_component | EMC complex |
F | 0000045 | biological_process | autophagosome assembly |
F | 0005515 | molecular_function | protein binding |
F | 0005783 | cellular_component | endoplasmic reticulum |
F | 0005789 | cellular_component | endoplasmic reticulum membrane |
F | 0016020 | cellular_component | membrane |
F | 0032977 | molecular_function | membrane insertase activity |
F | 0045050 | biological_process | protein insertion into ER membrane by stop-transfer membrane-anchor sequence |
F | 0071816 | biological_process | tail-anchored membrane protein insertion into ER membrane |
F | 0072546 | cellular_component | EMC complex |
F | 1903349 | cellular_component | omegasome membrane |
G | 0030246 | molecular_function | carbohydrate binding |
H | 0005515 | molecular_function | protein binding |
H | 0005737 | cellular_component | cytoplasm |
H | 0005783 | cellular_component | endoplasmic reticulum |
H | 0005789 | cellular_component | endoplasmic reticulum membrane |
H | 0005794 | cellular_component | Golgi apparatus |
H | 0016020 | cellular_component | membrane |
H | 0032977 | molecular_function | membrane insertase activity |
H | 0045050 | biological_process | protein insertion into ER membrane by stop-transfer membrane-anchor sequence |
H | 0071816 | biological_process | tail-anchored membrane protein insertion into ER membrane |
H | 0072546 | cellular_component | EMC complex |
J | 0005245 | molecular_function | voltage-gated calcium channel activity |
J | 0005891 | cellular_component | voltage-gated calcium channel complex |
J | 0070588 | biological_process | calcium ion transmembrane transport |
K | 0005216 | molecular_function | monoatomic ion channel activity |
K | 0005245 | molecular_function | voltage-gated calcium channel activity |
K | 0005891 | cellular_component | voltage-gated calcium channel complex |
K | 0006811 | biological_process | monoatomic ion transport |
K | 0016020 | cellular_component | membrane |
K | 0055085 | biological_process | transmembrane transport |
K | 0070588 | biological_process | calcium ion transmembrane transport |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 61 |
Details | TRANSMEM: Helical => ECO:0000305|PubMed:32459176 |
Chain | Residue | Details |
D | LYS67-MET87 | |
D | THR99-PHE120 | |
D | GLN128-VAL148 |
site_id | SWS_FT_FI2 |
Number of Residues | 44 |
Details | TOPO_DOM: Lumenal => ECO:0000305|PubMed:32459176 |
Chain | Residue | Details |
D | TYR88-PRO98 | |
K | GLN1007-VAL1013 | |
K | LYS1072-VAL1121 | |
K | ARG1143-ARG1159 | |
K | GLY1262-ILE1269 | |
K | GLU1322-SER1372 | |
K | GLY1431-GLN1452 | |
K | ALA1472-PHE1499 | |
D | TYR149-LEU183 | |
K | MET291-ALA350 | |
K | ASN373-TRP380 | |
K | GLU544-GLU554 | |
K | GLU607-GLY615 | |
K | GLY674-PRO693 | |
K | ILE716-PRO725 | |
K | GLU920-HIS931 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:32459176 |
Chain | Residue | Details |
D | LYS121-SER127 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
D | SER36 | |
K | ALA1292-ASP1301 | |
K | GLU1392-PRO1409 | |
K | PRO252-LEU268 | |
K | GLY402-ASN524 | |
K | TYR576-SER586 | |
K | ASN635-SER653 | |
K | ASN746-THR900 | |
K | LEU953-ASN987 | |
K | LYS1033-ASN1051 | |
K | VAL1182-THR1239 |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S3 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | ALA189-SER209 |
site_id | SWS_FT_FI6 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | VAL233-VAL251 |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S5 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | LEU269-PHE290 |
site_id | SWS_FT_FI8 |
Number of Residues | 80 |
Details | INTRAMEM: Pore-forming => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | PHE351-VAL372 | |
K | GLN694-GLY715 | |
K | LEU1122-TYR1142 | |
K | ALA1453-LEU1471 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | PRO381-LEU401 |
site_id | SWS_FT_FI10 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S1 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | VAL525-SER543 |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | VAL555-MET575 |
site_id | SWS_FT_FI12 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | LEU587-VAL606 |
site_id | SWS_FT_FI13 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | ILE616-TRP634 |
site_id | SWS_FT_FI14 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | LEU654-PHE673 |
site_id | SWS_FT_FI15 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | GLY726-LEU745 |
site_id | SWS_FT_FI16 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | ILE901-ALA919 |
site_id | SWS_FT_FI17 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S2 of repeat III => ECO:0000255 |
Chain | Residue | Details |
K | ILE932-ILE952 |
site_id | SWS_FT_FI18 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | TYR988-ILE1006 |
site_id | SWS_FT_FI19 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | VAL1014-ALA1032 |
site_id | SWS_FT_FI20 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | ILE1052-PHE1071 |
site_id | SWS_FT_FI21 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | VAL1160-PHE1181 |
site_id | SWS_FT_FI22 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | TYR1240-TYR1261 |
site_id | SWS_FT_FI23 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | ALA1270-ILE1291 |
site_id | SWS_FT_FI24 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | PRO1302-SER1321 |
site_id | SWS_FT_FI25 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | ILE1373-GLY1391 |
site_id | SWS_FT_FI26 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | TYR1410-PHE1430 |
site_id | SWS_FT_FI27 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | ALA1500-MET1524 |
site_id | SWS_FT_FI28 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | GLU363 | |
K | GLU706 | |
K | GLU1135 |
site_id | SWS_FT_FI29 |
Number of Residues | 3 |
Details | SITE: Calcium ion selectivity and permeability => ECO:0000269|PubMed:8099908 |
Chain | Residue | Details |
K | GLU363 | |
K | GLU1135 | |
K | GLU1464 |
site_id | SWS_FT_FI30 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q01815 |
Chain | Residue | Details |
K | SER469 | |
K | SER808 | |
K | SER815 |
site_id | SWS_FT_FI31 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q01815 |
Chain | Residue | Details |
K | THR476 |
site_id | SWS_FT_FI32 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
K | ASN153 | |
K | ASN328 | |
K | ASN1436 | |
K | ASN1487 |