8SL4
Dimeric form of human adenylyl cyclase 5
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001973 | biological_process | G protein-coupled adenosine receptor signaling pathway |
A | 0004016 | molecular_function | adenylate cyclase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0005929 | cellular_component | cilium |
A | 0006171 | biological_process | cAMP biosynthetic process |
A | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
A | 0007191 | biological_process | adenylate cyclase-activating dopamine receptor signaling pathway |
A | 0007193 | biological_process | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
A | 0007195 | biological_process | adenylate cyclase-inhibiting dopamine receptor signaling pathway |
A | 0007204 | biological_process | positive regulation of cytosolic calcium ion concentration |
A | 0007626 | biological_process | locomotory behavior |
A | 0008179 | molecular_function | adenylate cyclase binding |
A | 0016020 | cellular_component | membrane |
A | 0016829 | molecular_function | lyase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050885 | biological_process | neuromuscular process controlling balance |
A | 0061178 | biological_process | regulation of insulin secretion involved in cellular response to glucose stimulus |
A | 0097110 | molecular_function | scaffold protein binding |
A | 1904322 | biological_process | cellular response to forskolin |
B | 0001973 | biological_process | G protein-coupled adenosine receptor signaling pathway |
B | 0004016 | molecular_function | adenylate cyclase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005886 | cellular_component | plasma membrane |
B | 0005929 | cellular_component | cilium |
B | 0006171 | biological_process | cAMP biosynthetic process |
B | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
B | 0007191 | biological_process | adenylate cyclase-activating dopamine receptor signaling pathway |
B | 0007193 | biological_process | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
B | 0007195 | biological_process | adenylate cyclase-inhibiting dopamine receptor signaling pathway |
B | 0007204 | biological_process | positive regulation of cytosolic calcium ion concentration |
B | 0007626 | biological_process | locomotory behavior |
B | 0008179 | molecular_function | adenylate cyclase binding |
B | 0016020 | cellular_component | membrane |
B | 0016829 | molecular_function | lyase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050885 | biological_process | neuromuscular process controlling balance |
B | 0061178 | biological_process | regulation of insulin secretion involved in cellular response to glucose stimulus |
B | 0097110 | molecular_function | scaffold protein binding |
B | 1904322 | biological_process | cellular response to forskolin |
Functional Information from PROSITE/UniProt
site_id | PS00452 |
Number of Residues | 24 |
Details | GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVL.GlrkwqFdVWSNDVTlanhmE |
Chain | Residue | Details |
A | GLY573-GLU596 | |
A | GLY1187-ASP1210 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1648 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | MET1-SER195 | |
A | CYS395-SER769 | |
A | ALA1005-SER1261 | |
B | MET1-SER195 | |
B | CYS395-SER769 | |
B | ALA1005-SER1261 |
site_id | SWS_FT_FI2 |
Number of Residues | 480 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | GLY196-PHE216 | |
A | PHE910-ILE930 | |
A | LEU935-PHE955 | |
A | VAL984-HIS1004 | |
B | GLY196-PHE216 | |
B | LEU242-ALA262 | |
B | LEU268-CYS288 | |
B | GLY299-LEU319 | |
B | ALA325-VAL345 | |
B | PHE374-VAL394 | |
B | LEU770-LEU790 | |
A | LEU242-ALA262 | |
B | PHE792-CYS812 | |
B | LEU836-CYS856 | |
B | PHE910-ILE930 | |
B | LEU935-PHE955 | |
B | VAL984-HIS1004 | |
A | LEU268-CYS288 | |
A | GLY299-LEU319 | |
A | ALA325-VAL345 | |
A | PHE374-VAL394 | |
A | LEU770-LEU790 | |
A | PHE792-CYS812 | |
A | LEU836-CYS856 |
site_id | SWS_FT_FI3 |
Number of Residues | 104 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | ASN857-TYR909 | |
B | ASN857-TYR909 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00099 |
Chain | Residue | Details |
A | ASP474 | |
A | ILE475 | |
A | ASP518 | |
B | ASP474 | |
B | ILE475 | |
B | ASP518 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30803 |
Chain | Residue | Details |
A | LEU516 | |
A | ARG562 | |
B | LEU516 | |
B | ARG562 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P26769 |
Chain | Residue | Details |
A | LYS1123 | |
A | ASP1197 | |
A | ASN1204 | |
A | LYS1244 | |
B | LYS1123 | |
B | ASP1197 | |
B | ASN1204 | |
B | LYS1244 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P84309 |
Chain | Residue | Details |
A | ARG23 | |
B | ARG23 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84309 |
Chain | Residue | Details |
A | SER96 | |
A | SER155 | |
B | SER96 | |
B | SER155 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O43306 |
Chain | Residue | Details |
A | SER666 | |
B | SER666 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q03343 |
Chain | Residue | Details |
A | SER754 | |
B | SER754 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q03343 |
Chain | Residue | Details |
A | THR1011 | |
B | THR1011 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN870 | |
A | ASN887 | |
B | ASN870 | |
B | ASN887 |