UniProtKB - P26769 (ADCY2_RAT)
Adenylate cyclase type 2
Adcy2
Functioni
Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:22906005, PubMed:24363043, PubMed:10427002, PubMed:1719547, PubMed:7761832, PubMed:21596131, PubMed:11087399, PubMed:15591060, PubMed:19243146, PubMed:16766715).
Down-stream signaling cascades mediate changes in gene expression patterns and lead to increased IL6 production (PubMed:24363043).
Functions in signaling cascades downstream of the muscarinic acetylcholine receptors (PubMed:22906005).
10 PublicationsCatalytic activityi
- EC:4.6.1.110 Publications
Cofactori
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 294 | Magnesium 1; catalyticPROSITE-ProRule annotationCurated | 1 | |
Metal bindingi | 294 | Magnesium 2; catalyticPROSITE-ProRule annotationCurated1 Publication | 1 | |
Metal bindingi | 295 | Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotationCurated1 Publication | 1 | |
Metal bindingi | 338 | Magnesium 1; catalyticPROSITE-ProRule annotationCurated | 1 | |
Metal bindingi | 338 | Magnesium 2; catalyticPROSITE-ProRule annotationCurated1 Publication | 1 | |
Binding sitei | 382 | ATPBy similarity | 1 | |
Binding sitei | 938 | ATP5 Publications | 1 | |
Binding sitei | 1065 | ATP5 Publications | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 294 – 299 | ATPBy similarity | 6 | |
Nucleotide bindingi | 336 – 338 | ATPBy similarity | 3 | |
Nucleotide bindingi | 1018 – 1020 | ATP5 Publications | 3 | |
Nucleotide bindingi | 1025 – 1029 | ATPCombined sources1 Publication | 5 |
GO - Molecular functioni
- adenylate cyclase activity Source: UniProtKB
- adenylate cyclase binding Source: BHF-UCL
- ATP binding Source: UniProtKB-KW
- G-protein beta/gamma-subunit complex binding Source: RGD
- magnesium ion binding Source: UniProtKB
- manganese ion binding Source: UniProtKB
GO - Biological processi
- adenylate cyclase-activating G protein-coupled receptor signaling pathway Source: UniProtKB
- adenylate cyclase-modulating G protein-coupled receptor signaling pathway Source: BHF-UCL
- cAMP biosynthetic process Source: UniProtKB
- cAMP-mediated signaling Source: UniProtKB
- cellular response to forskolin Source: UniProtKB
Keywordsi
Molecular function | Lyase |
Biological process | cAMP biosynthesis |
Ligand | ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 4.6.1.1, 5301 |
Reactomei | R-RNO-163615, PKA activation R-RNO-170660, Adenylate cyclase activating pathway R-RNO-170670, Adenylate cyclase inhibitory pathway R-RNO-418597, G alpha (z) signalling events R-RNO-5610787, Hedgehog 'off' state |
Names & Taxonomyi
Protein namesi | Recommended name: Adenylate cyclase type 2 (EC:4.6.1.17 Publications)Alternative name(s): ATP pyrophosphate-lyase 2 Adenylate cyclase type II Adenylyl cyclase 2 Short name: AC21 Publication |
Gene namesi | Name:Adcy2 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 619965, Adcy2 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Plasma membrane
- Cell membrane 2 Publications; Multi-pass membrane protein Curated
Other locations
- Membrane 2 Publications; Multi-pass membrane protein Curated
Plasma Membrane
- integral component of plasma membrane Source: UniProtKB
- plasma membrane Source: BHF-UCL
Other locations
- cytoplasm Source: RGD
- dendrite Source: UniProtKB
- membrane Source: BHF-UCL
- membrane raft Source: BHF-UCL
- protein-containing complex Source: RGD
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 44 | CytoplasmicSequence analysisAdd BLAST | 44 | |
Transmembranei | 45 – 65 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 75 – 95 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 107 – 127 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 132 – 152 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 157 – 177 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 186 – 206 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 207 – 600 | CytoplasmicSequence analysisAdd BLAST | 394 | |
Transmembranei | 601 – 621 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 626 – 646 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 679 – 699 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 734 – 754 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 763 – 783 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 800 – 820 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 821 – 1090 | CytoplasmicSequence analysisCuratedAdd BLAST | 270 |
Keywords - Cellular componenti
Cell membrane, Cytoplasm, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 490 | S → A: Reduces activation by PKC. Abolishes activation by PKC; when associated with A-543. 1 Publication | 1 | |
Mutagenesisi | 490 | S → D: Increases basal level of enzyme activity. Abolishes activation by PKC; when associated with D-543. 1 Publication | 1 | |
Mutagenesisi | 543 | S → A: Reduces activation by PKC. Abolishes activation by PKC; when associated with A-490. 1 Publication | 1 | |
Mutagenesisi | 543 | S → D: Increases basal level of enzyme activity. Abolishes activation by PKC; when associated with D-490. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL2958 |
DrugCentrali | P26769 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000195686 | 1 – 1090 | Adenylate cyclase type 2Add BLAST | 1090 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 490 | Phosphoserine; by PKC1 Publication | 1 | |
Modified residuei | 543 | Phosphoserine; by PKC1 Publication | 1 | |
Glycosylationi | 712 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 717 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Post-translational modificationi
Keywords - PTMi
Glycoprotein, PhosphoproteinProteomic databases
PaxDbi | P26769 |
PRIDEi | P26769 |
PTM databases
GlyGeni | P26769, 2 sites |
iPTMneti | P26769 |
PhosphoSitePlusi | P26769 |
Expressioni
Tissue specificityi
Interactioni
Subunit structurei
Binary interactionsi
P26769
With | #Exp. | IntAct |
---|---|---|
AKAP9 - isoform 4 [Q99996-4] from Homo sapiens. | 3 | EBI-1027877,EBI-15676518 |
PDE4D - isoform 3 [Q08499-2] from Homo sapiens. | 3 | EBI-1027877,EBI-8095525 |
GO - Molecular functioni
- adenylate cyclase binding Source: BHF-UCL
Protein-protein interaction databases
BioGRIDi | 249536, 1 interactor |
DIPi | DIP-164N |
IntActi | P26769, 8 interactors |
MINTi | P26769 |
STRINGi | 10116.ENSRNOP00000038994 |
Chemistry databases
BindingDBi | P26769 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P26769 |
SMRi | P26769 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P26769 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 904 – 921 | Interaction with GNAS1 PublicationAdd BLAST | 18 | |
Regioni | 989 – 992 | Interaction with GNAS1 Publication | 4 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3619, Eukaryota |
InParanoidi | P26769 |
OrthoDBi | 363718at2759 |
PhylomeDBi | P26769 |
Family and domain databases
CDDi | cd07302, CHD, 2 hits |
Gene3Di | 3.30.70.1230, 2 hits |
InterProi | View protein in InterPro IPR001054, A/G_cyclase IPR018297, A/G_cyclase_CS IPR032628, AC_N IPR030672, Adcy IPR009398, Adcy_conserved_dom IPR029787, Nucleotide_cyclase |
Pfami | View protein in Pfam PF16214, AC_N, 1 hit PF06327, DUF1053, 1 hit PF00211, Guanylate_cyc, 2 hits |
PIRSFi | PIRSF039050, Ade_cyc, 1 hit |
SMARTi | View protein in SMART SM00044, CYCc, 2 hits |
SUPFAMi | SSF55073, SSF55073, 2 hits |
PROSITEi | View protein in PROSITE PS00452, GUANYLATE_CYCLASE_1, 2 hits PS50125, GUANYLATE_CYCLASE_2, 2 hits |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MRRRRYLRDR AEAAAAAAAG GGEGLQRSRD WLYESYYCMS QQHPLIVFLL
60 70 80 90 100
LIVMGACLAL LAVFFALGLE VEDHVAFLIT VPTALAIFFA IFILVCIESV
110 120 130 140 150
FKKLLRVFSL VIWICLVAMG YLFMCFGGTV SAWDQVSFFL FIIFVVYTML
160 170 180 190 200
PFNMRDAIIA SILTSSSHTI VLSVYLSATP GAKEHLFWQI LANVIIFICG
210 220 230 240 250
NLAGAYHKHL MELALQQTYR DTCNCIKSRI KLEFEKRQQE RLLLSLLPAH
260 270 280 290 300
IAMEMKAEII QRLQGPKAGQ MENTNNFHNL YVKRHTNVSI LYADIVGFTR
310 320 330 340 350
LASDCSPGEL VHMLNELFGK FDQIAKENEC MRIKILGDCY YCVSGLPISL
360 370 380 390 400
PNHAKNCVKM GLDMCEAIKK VRDATGVDIN MRVGVHSGNV LCGVIGLQKW
410 420 430 440 450
QYDVWSHDVT LANHMEAGGV PGRVHISSVT LEHLNGAYKV EEGDGEIRDP
460 470 480 490 500
YLKQHLVKTY FVINPKGERR SPQHLFRPRH TLDGAKMRAS VRMTRYLESW
510 520 530 540 550
GAAKPFAHLH HRDSMTTENG KISTTDVPMG QHNFQNRTLR TKSQKKRFEE
560 570 580 590 600
ELNERMIQAI DGINAQKQWL KSEDIQRISL LFYNKNIEKE YRATALPAFK
610 620 630 640 650
YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL
660 670 680 690 700
LQCSKKASTS LMWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL
710 720 730 740 750
SNSEETTLPT ANTSNANVSV PDNQASILHA RNLFFLPYFI YSCILGLISC
760 770 780 790 800
SVFLRVNYEL KMLIMMVALV GYNTILLHTH AHVLDAYSQV LFQRPGIWKD
810 820 830 840 850
LKTMGSVSLS IFFITLLVLG RQSEYYCRLD FLWKNKFKKE REEIETMENL
860 870 880 890 900
NRVLLENVLP AHVAEHFLAR SLKNEELYHQ SYDCVCVMFA SIPDFKEFYT
910 920 930 940 950
ESDVNKEGLE CLRLLNEIIA DFDDLLSKPK FSGVEKIKTI GSTYMAATGL
960 970 980 990 1000
SAIPSQEHAQ EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI
1010 1020 1030 1040 1050
NHGPVIAGVI GAQKPQYDIW GNTVNVASRM DSTGVLDKIQ VTEETSLILQ
1060 1070 1080 1090
TLGYTCTCRG IINVKGKGDL KTYFVNTEMS RSLSQSNLAS
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF1LV12 | F1LV12_RAT | Adenylate cyclase 2 | Adcy2 rCG_41958 | 1,095 | Annotation score: | ||
A0A8I6AMB0 | A0A8I6AMB0_RAT | Adenylate cyclase type 2 | Adcy2 | 1,042 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M80550 mRNA Translation: AAA40682.1 |
PIRi | A41541 |
RefSeqi | NP_112269.1, NM_031007.1 |
Genome annotation databases
GeneIDi | 81636 |
KEGGi | rno:81636 |
UCSCi | RGD:619965, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M80550 mRNA Translation: AAA40682.1 |
PIRi | A41541 |
RefSeqi | NP_112269.1, NM_031007.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AB8 | X-ray | 2.20 | A/B | 871-1090 | [»] | |
1AZS | X-ray | 2.30 | B | 870-1081 | [»] | |
1CJK | X-ray | 3.00 | B | 870-1081 | [»] | |
1CJT | X-ray | 2.80 | B | 870-1081 | [»] | |
1CJU | X-ray | 2.80 | B | 870-1081 | [»] | |
1CJV | X-ray | 3.00 | B | 870-1081 | [»] | |
1CS4 | X-ray | 2.50 | B | 870-1081 | [»] | |
1CUL | X-ray | 2.40 | B | 874-1081 | [»] | |
1TL7 | X-ray | 2.80 | B | 870-1081 | [»] | |
1U0H | X-ray | 2.90 | B | 870-1081 | [»] | |
2GVD | X-ray | 2.90 | B | 870-1081 | [»] | |
2GVZ | X-ray | 3.27 | B | 870-1081 | [»] | |
3C14 | X-ray | 2.68 | B | 870-1081 | [»] | |
3C15 | X-ray | 2.78 | B | 870-1081 | [»] | |
3C16 | X-ray | 2.87 | B | 870-1081 | [»] | |
3G82 | X-ray | 3.11 | B | 870-1081 | [»] | |
3MAA | X-ray | 3.00 | B | 870-1081 | [»] | |
AlphaFoldDBi | P26769 | |||||
SMRi | P26769 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 249536, 1 interactor |
DIPi | DIP-164N |
IntActi | P26769, 8 interactors |
MINTi | P26769 |
STRINGi | 10116.ENSRNOP00000038994 |
Chemistry databases
BindingDBi | P26769 |
ChEMBLi | CHEMBL2958 |
DrugCentrali | P26769 |
PTM databases
GlyGeni | P26769, 2 sites |
iPTMneti | P26769 |
PhosphoSitePlusi | P26769 |
Proteomic databases
PaxDbi | P26769 |
PRIDEi | P26769 |
Genome annotation databases
GeneIDi | 81636 |
KEGGi | rno:81636 |
UCSCi | RGD:619965, rat |
Organism-specific databases
CTDi | 108 |
RGDi | 619965, Adcy2 |
Phylogenomic databases
eggNOGi | KOG3619, Eukaryota |
InParanoidi | P26769 |
OrthoDBi | 363718at2759 |
PhylomeDBi | P26769 |
Enzyme and pathway databases
BRENDAi | 4.6.1.1, 5301 |
Reactomei | R-RNO-163615, PKA activation R-RNO-170660, Adenylate cyclase activating pathway R-RNO-170670, Adenylate cyclase inhibitory pathway R-RNO-418597, G alpha (z) signalling events R-RNO-5610787, Hedgehog 'off' state |
Miscellaneous databases
EvolutionaryTracei | P26769 |
PROi | PR:P26769 |
Family and domain databases
CDDi | cd07302, CHD, 2 hits |
Gene3Di | 3.30.70.1230, 2 hits |
InterProi | View protein in InterPro IPR001054, A/G_cyclase IPR018297, A/G_cyclase_CS IPR032628, AC_N IPR030672, Adcy IPR009398, Adcy_conserved_dom IPR029787, Nucleotide_cyclase |
Pfami | View protein in Pfam PF16214, AC_N, 1 hit PF06327, DUF1053, 1 hit PF00211, Guanylate_cyc, 2 hits |
PIRSFi | PIRSF039050, Ade_cyc, 1 hit |
SMARTi | View protein in SMART SM00044, CYCc, 2 hits |
SUPFAMi | SSF55073, SSF55073, 2 hits |
PROSITEi | View protein in PROSITE PS00452, GUANYLATE_CYCLASE_1, 2 hits PS50125, GUANYLATE_CYCLASE_2, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | ADCY2_RAT | |
Accessioni | P26769Primary (citable) accession number: P26769 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | August 1, 1992 | |
Last modified: | May 25, 2022 | |
This is version 177 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families