2F43
Rat liver F1-ATPase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001937 | biological_process | negative regulation of endothelial cell proliferation |
| A | 0002020 | molecular_function | protease binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006754 | biological_process | ATP biosynthetic process |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0009986 | cellular_component | cell surface |
| A | 0014850 | biological_process | response to muscle activity |
| A | 0015986 | biological_process | proton motive force-driven ATP synthesis |
| A | 0016020 | cellular_component | membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0032559 | molecular_function | adenyl ribonucleotide binding |
| A | 0042288 | molecular_function | MHC class I protein binding |
| A | 0042776 | biological_process | proton motive force-driven mitochondrial ATP synthesis |
| A | 0043531 | molecular_function | ADP binding |
| A | 0043532 | molecular_function | angiostatin binding |
| A | 0043536 | biological_process | positive regulation of blood vessel endothelial cell migration |
| A | 0045121 | cellular_component | membrane raft |
| A | 0045259 | cellular_component | proton-transporting ATP synthase complex |
| A | 0045471 | biological_process | response to ethanol |
| A | 0046034 | biological_process | ATP metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
| A | 0071549 | biological_process | cellular response to dexamethasone stimulus |
| A | 0071732 | biological_process | cellular response to nitric oxide |
| A | 0097229 | cellular_component | sperm end piece |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0001525 | biological_process | angiogenesis |
| B | 0001889 | biological_process | liver development |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006754 | biological_process | ATP biosynthetic process |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0006898 | biological_process | receptor-mediated endocytosis |
| B | 0006933 | biological_process | negative regulation of cell adhesion involved in substrate-bound cell migration |
| B | 0009631 | biological_process | cold acclimation |
| B | 0009986 | cellular_component | cell surface |
| B | 0010042 | biological_process | response to manganese ion |
| B | 0015986 | biological_process | proton motive force-driven ATP synthesis |
| B | 0016020 | cellular_component | membrane |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0030228 | molecular_function | lipoprotein particle receptor activity |
| B | 0031966 | cellular_component | mitochondrial membrane |
| B | 0042288 | molecular_function | MHC class I protein binding |
| B | 0042645 | cellular_component | mitochondrial nucleoid |
| B | 0042776 | biological_process | proton motive force-driven mitochondrial ATP synthesis |
| B | 0043531 | molecular_function | ADP binding |
| B | 0043532 | molecular_function | angiostatin binding |
| B | 0043536 | biological_process | positive regulation of blood vessel endothelial cell migration |
| B | 0045121 | cellular_component | membrane raft |
| B | 0045259 | cellular_component | proton-transporting ATP synthase complex |
| B | 0046034 | biological_process | ATP metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
| B | 0046961 | molecular_function | proton-transporting ATPase activity, rotational mechanism |
| B | 0051453 | biological_process | regulation of intracellular pH |
| B | 0098761 | biological_process | cellular response to interleukin-7 |
| B | 1901652 | biological_process | response to peptide |
| B | 1901653 | biological_process | cellular response to peptide |
| B | 1902600 | biological_process | proton transmembrane transport |
| B | 1904643 | biological_process | response to curcumin |
| B | 1905242 | biological_process | response to 3,3',5-triiodo-L-thyronine |
| G | 0005739 | cellular_component | mitochondrion |
| G | 0005743 | cellular_component | mitochondrial inner membrane |
| G | 0006754 | biological_process | ATP biosynthetic process |
| G | 0006811 | biological_process | monoatomic ion transport |
| G | 0015986 | biological_process | proton motive force-driven ATP synthesis |
| G | 0016887 | molecular_function | ATP hydrolysis activity |
| G | 0042776 | biological_process | proton motive force-driven mitochondrial ATP synthesis |
| G | 0045259 | cellular_component | proton-transporting ATP synthase complex |
| G | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
| G | 0071732 | biological_process | cellular response to nitric oxide |
| G | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE VO4 B 601 |
| Chain | Residue |
| A | SER344 |
| B | ALA158 |
| B | GLY159 |
| B | LYS162 |
| B | GLU188 |
| B | ARG189 |
| B | TYR311 |
| B | ADP604 |
| B | MG605 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 602 |
| Chain | Residue |
| A | THR176 |
| A | GLN208 |
| A | ASP269 |
| A | ATP603 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 605 |
| Chain | Residue |
| B | THR163 |
| B | GLU188 |
| B | ARG189 |
| B | VO4601 |
| B | ADP604 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ATP A 603 |
| Chain | Residue |
| A | GLN172 |
| A | THR173 |
| A | GLY174 |
| A | LYS175 |
| A | THR176 |
| A | SER177 |
| A | ARG362 |
| A | GLY431 |
| A | GLN432 |
| A | MG602 |
| B | SER355 |
| B | ASP359 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP B 604 |
| Chain | Residue |
| A | VAL371 |
| A | ARG373 |
| B | GLY159 |
| B | GLY161 |
| B | LYS162 |
| B | THR163 |
| B | VAL164 |
| B | ARG189 |
| B | TYR345 |
| B | PHE418 |
| B | ALA421 |
| B | PHE424 |
| B | VO4601 |
| B | MG605 |
Functional Information from PROSITE/UniProt
| site_id | PS00152 |
| Number of Residues | 10 |
| Details | ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS |
| Chain | Residue | Details |
| A | PRO363-SER372 | |
| B | PRO346-SER355 |
| site_id | PS00153 |
| Number of Residues | 14 |
| Details | ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA |
| Chain | Residue | Details |
| G | ILE258-ALA271 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Site: {"description":"Required for activity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; alternate","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 11 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) serine; alternate","evidences":[{"source":"PubMed","id":"24098488","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00829","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06576","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06576","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"24098488","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P36542","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| B | ARG356 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| A | ARG373 | |
| B | ARG189 | |
| B | GLU188 | |
| B | LYS162 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| A | LYS175 | |
| A | LYS209 | |
| A | GLN208 |
