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8SL4

Dimeric form of human adenylyl cyclase 5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001973biological_processG protein-coupled adenosine receptor signaling pathway
A0004016molecular_functionadenylate cyclase activity
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0006171biological_processcAMP biosynthetic process
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
A0007195biological_processadenylate cyclase-inhibiting dopamine receptor signaling pathway
A0007204biological_processpositive regulation of cytosolic calcium ion concentration
A0007626biological_processlocomotory behavior
A0008179molecular_functionadenylate cyclase binding
A0009190biological_processcyclic nucleotide biosynthetic process
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0016849molecular_functionphosphorus-oxygen lyase activity
A0035556biological_processintracellular signal transduction
A0042995cellular_componentcell projection
A0046872molecular_functionmetal ion binding
A0050885biological_processneuromuscular process controlling balance
A0061178biological_processregulation of insulin secretion involved in cellular response to glucose stimulus
A0097110molecular_functionscaffold protein binding
A1904322biological_processcellular response to forskolin
B0000166molecular_functionnucleotide binding
B0001973biological_processG protein-coupled adenosine receptor signaling pathway
B0004016molecular_functionadenylate cyclase activity
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0005929cellular_componentcilium
B0006171biological_processcAMP biosynthetic process
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0007195biological_processadenylate cyclase-inhibiting dopamine receptor signaling pathway
B0007204biological_processpositive regulation of cytosolic calcium ion concentration
B0007626biological_processlocomotory behavior
B0008179molecular_functionadenylate cyclase binding
B0009190biological_processcyclic nucleotide biosynthetic process
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0016849molecular_functionphosphorus-oxygen lyase activity
B0035556biological_processintracellular signal transduction
B0042995cellular_componentcell projection
B0046872molecular_functionmetal ion binding
B0050885biological_processneuromuscular process controlling balance
B0061178biological_processregulation of insulin secretion involved in cellular response to glucose stimulus
B0097110molecular_functionscaffold protein binding
B1904322biological_processcellular response to forskolin
Functional Information from PROSITE/UniProt
site_idPS00452
Number of Residues24
DetailsGUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVL.GlrkwqFdVWSNDVTlanhmE
ChainResidueDetails
AGLY573-GLU596
AGLY1187-ASP1210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues440
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues104
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues254
DetailsDomain: {"description":"Guanylate cyclase 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues278
DetailsDomain: {"description":"Guanylate cyclase 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P30803","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P26769","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q03343","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q03343","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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