1MCX
STRUCTURE OF FULL-LENGTH ANNEXIN A1 IN THE PRESENCE OF CALCIUM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001786 | molecular_function | phosphatidylserine binding |
| A | 0001891 | cellular_component | phagocytic cup |
| A | 0002250 | biological_process | adaptive immune response |
| A | 0002376 | biological_process | immune system process |
| A | 0002548 | biological_process | monocyte chemotaxis |
| A | 0002685 | biological_process | regulation of leukocyte migration |
| A | 0004859 | molecular_function | phospholipase inhibitor activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005544 | molecular_function | calcium-dependent phospholipid binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005768 | cellular_component | endosome |
| A | 0005769 | cellular_component | early endosome |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005929 | cellular_component | cilium |
| A | 0006909 | biological_process | phagocytosis |
| A | 0006954 | biological_process | inflammatory response |
| A | 0007165 | biological_process | signal transduction |
| A | 0007187 | biological_process | G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0012506 | cellular_component | vesicle membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0016323 | cellular_component | basolateral plasma membrane |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0016328 | cellular_component | lateral plasma membrane |
| A | 0019834 | molecular_function | phospholipase A2 inhibitor activity |
| A | 0030036 | biological_process | actin cytoskeleton organization |
| A | 0030659 | cellular_component | cytoplasmic vesicle membrane |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0031514 | cellular_component | motile cilium |
| A | 0031901 | cellular_component | early endosome membrane |
| A | 0032652 | biological_process | regulation of interleukin-1 production |
| A | 0032743 | biological_process | positive regulation of interleukin-2 production |
| A | 0042102 | biological_process | positive regulation of T cell proliferation |
| A | 0042119 | biological_process | neutrophil activation |
| A | 0045087 | biological_process | innate immune response |
| A | 0045627 | biological_process | positive regulation of T-helper 1 cell differentiation |
| A | 0045629 | biological_process | negative regulation of T-helper 2 cell differentiation |
| A | 0045920 | biological_process | negative regulation of exocytosis |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046883 | biological_process | regulation of hormone secretion |
| A | 0050727 | biological_process | regulation of inflammatory response |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071385 | biological_process | cellular response to glucocorticoid stimulus |
| A | 0071621 | biological_process | granulocyte chemotaxis |
| A | 0090303 | biological_process | positive regulation of wound healing |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 347 |
| Chain | Residue |
| A | GLY59 |
| A | VAL60 |
| A | GLU62 |
| A | HOH355 |
| A | HOH356 |
| A | HOH656 |
| A | HOH657 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 348 |
| Chain | Residue |
| A | GLU105 |
| A | ASP196 |
| A | HOH357 |
| A | HOH358 |
| A | HOH658 |
| A | LYS97 |
| A | LEU100 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 349 |
| Chain | Residue |
| A | MET127 |
| A | GLY129 |
| A | GLY131 |
| A | ASP171 |
| A | HOH359 |
| A | HOH404 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 350 |
| Chain | Residue |
| A | THR132 |
| A | GLU134 |
| A | HOH360 |
| A | HOH361 |
| A | HOH362 |
| A | HOH385 |
| A | HOH560 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 351 |
| Chain | Residue |
| A | GLY210 |
| A | ARG213 |
| A | GLY215 |
| A | GLU255 |
| A | HOH363 |
| A | HOH644 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 352 |
| Chain | Residue |
| A | MET286 |
| A | GLY288 |
| A | GLY290 |
| A | GLU330 |
| A | HOH364 |
| A | HOH365 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 353 |
| Chain | Residue |
| A | LEU328 |
| A | THR331 |
| A | GLU336 |
| A | HOH366 |
| A | HOH367 |
| A | HOH492 |
| A | HOH531 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 354 |
| Chain | Residue |
| A | ASP253 |
| A | LEU256 |
| A | GLU261 |
| A | HOH368 |
| A | HOH588 |
| A | HOH660 |
Functional Information from PROSITE/UniProt
| site_id | PS00223 |
| Number of Residues | 53 |
| Details | ANNEXIN_1 Annexin repeat signature. GVdeatiieiLtkRtnaQrqQikaaYlqekgkpLdeaLkkaltGhleevAlaL |
| Chain | Residue | Details |
| A | GLY59-LEU111 | |
| A | GLY131-LEU183 | |
| A | GLY215-VAL267 | |
| A | GLY290-LEU342 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 71 |
| Details | Repeat: {"description":"Annexin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 71 |
| Details | Repeat: {"description":"Annexin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 72 |
| Details | Repeat: {"description":"Annexin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 71 |
| Details | Repeat: {"description":"Annexin 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1MCX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P10107","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"UniProtKB","id":"P04083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"UniProtKB","id":"P10107","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
