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Protein

Adenylate cyclase type 2

Gene

Adcy2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Down-stream signaling cascades mediate changes in gene expression patterns and lead to increased IL6 production. Functions in signaling cascades downstream of the muscarinic acetylcholine receptors.By similarity

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.By similarity

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).By similarity

Enzyme regulationi

Activated by forskolin. Is not activated by calmodulin. Inhibited by calcium ions, already at micromolar concentration. Activated by the G protein alpha subunit GNAS. Activated by the G protein beta and gamma subunit complex. Phosphorylation by RAF1 results in its activation (By similarity). Phosphorylation by PKC activates the enzyme (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi294Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi294Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi295Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi338Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi338Magnesium 2; catalyticPROSITE-ProRule annotation1
Binding sitei382ATPBy similarity1
Binding sitei938ATPBy similarity1
Binding sitei1065ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi294 – 299ATPBy similarity6
Nucleotide bindingi336 – 338ATPBy similarity3
Nucleotide bindingi1018 – 1020ATPBy similarity3
Nucleotide bindingi1025 – 1029ATPBy similarity5

GO - Molecular functioni

  • adenylate cyclase activity Source: UniProtKB
  • adenylate cyclase binding Source: BHF-UCL
  • ATP binding Source: UniProtKB-KW
  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cAMP biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.1. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 2 (EC:4.6.1.1)
Alternative name(s):
ATP pyrophosphate-lyase 2
Adenylate cyclase type II
Adenylyl cyclase 2
Gene namesi
Name:Adcy2
Synonyms:Kiaa1060
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:99676. Adcy2.

Subcellular locationi

  • Membrane By similarity; Multi-pass membrane protein By similarity
  • Cell membrane By similarity; Multi-pass membrane protein By similarity
  • Cytoplasm By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 44CytoplasmicSequence analysisAdd BLAST44
Transmembranei45 – 65HelicalSequence analysisAdd BLAST21
Transmembranei75 – 95HelicalSequence analysisAdd BLAST21
Transmembranei107 – 127HelicalSequence analysisAdd BLAST21
Transmembranei132 – 152HelicalSequence analysisAdd BLAST21
Transmembranei157 – 177HelicalSequence analysisAdd BLAST21
Transmembranei186 – 206HelicalSequence analysisAdd BLAST21
Topological domaini207 – 600CytoplasmicSequence analysisAdd BLAST394
Transmembranei601 – 621HelicalSequence analysisAdd BLAST21
Transmembranei626 – 646HelicalSequence analysisAdd BLAST21
Transmembranei679 – 699HelicalSequence analysisAdd BLAST21
Transmembranei734 – 754HelicalSequence analysisAdd BLAST21
Transmembranei763 – 783HelicalSequence analysisAdd BLAST21
Transmembranei800 – 820HelicalSequence analysisAdd BLAST21
Topological domaini821 – 1090CytoplasmicSequence analysisAdd BLAST270

GO - Cellular componenti

  • cytoplasm Source: MGI
  • dendrite Source: MGI
  • integral component of plasma membrane Source: UniProtKB
  • membrane Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001956851 – 1090Adenylate cyclase type 2Add BLAST1090

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei490Phosphoserine; by PKCBy similarity1
Modified residuei543Phosphoserine; by PKCBy similarity1
Glycosylationi712N-linked (GlcNAc...)Sequence analysis1
Glycosylationi717N-linked (GlcNAc...)Sequence analysis1
Glycosylationi723N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Phosphorylated by RAF1.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ80TL1.
MaxQBiQ80TL1.
PaxDbiQ80TL1.
PRIDEiQ80TL1.

PTM databases

iPTMnetiQ80TL1.
PhosphoSitePlusiQ80TL1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000021536.
CleanExiMM_ADCY2.

Interactioni

Subunit structurei

Interacts with RAF1 (By similarity). Interacts with GNAS. Interacts with the G protein beta and gamma subunit complex (By similarity).By similarity

GO - Molecular functioni

  • adenylate cyclase binding Source: BHF-UCL
  • protein heterodimerization activity Source: BHF-UCL

Protein-protein interaction databases

IntActiQ80TL1. 1 interactor.
MINTiMINT-4087163.
STRINGi10090.ENSMUSP00000022013.

Structurei

3D structure databases

ProteinModelPortaliQ80TL1.
SMRiQ80TL1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni904 – 921Interaction with GNASBy similarityAdd BLAST18
Regioni989 – 992Interaction with GNASBy similarity4

Domaini

The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain.By similarity

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 2 guanylate cyclase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOVERGENiHBG050458.
InParanoidiQ80TL1.
PhylomeDBiQ80TL1.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR009398. Adcy_conserved_dom.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80TL1-1 [UniParc]FASTAAdd to basket

« Hide

        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 SVLTSSSHTI 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 FFYNKNIEKE YRATALPAFK
610 620 630 640 650
YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL
660 670 680 690 700
LQCSKKASAS LLWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL
710 720 730 740 750
SNSEETTLPT ANASNANVSV PDNQTAILHA RNLFFLPYFI YSCILGLISC
760 770 780 790 800
SVFLRVNYEL KMLIMMVALV GYNIILLHTH 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
SAVPSQEHAQ EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI
1010 1020 1030 1040 1050
NHGPVIAGVI GAQKPQYDIW GNTVNVASRM DSTGVLDKIQ VTEETSLILQ
1060 1070 1080 1090
TLGYTCTCRG IINVKGKGDL KTYFVNTEMS RSLSQSNLAS
Length:1,090
Mass (Da):123,270
Last modified:December 21, 2004 - v2
Checksum:i461CDF5E6C828CCB
GO

Sequence cautioni

The sequence BAC65714 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122432 mRNA. Translation: BAC65714.1. Different initiation.
BC037107 mRNA. Translation: AAH37107.1.
UniGeneiMm.390617.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122432 mRNA. Translation: BAC65714.1. Different initiation.
BC037107 mRNA. Translation: AAH37107.1.
UniGeneiMm.390617.

3D structure databases

ProteinModelPortaliQ80TL1.
SMRiQ80TL1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80TL1. 1 interactor.
MINTiMINT-4087163.
STRINGi10090.ENSMUSP00000022013.

PTM databases

iPTMnetiQ80TL1.
PhosphoSitePlusiQ80TL1.

Proteomic databases

EPDiQ80TL1.
MaxQBiQ80TL1.
PaxDbiQ80TL1.
PRIDEiQ80TL1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:99676. Adcy2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOVERGENiHBG050458.
InParanoidiQ80TL1.
PhylomeDBiQ80TL1.

Enzyme and pathway databases

BRENDAi4.6.1.1. 3474.

Miscellaneous databases

PROiQ80TL1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021536.
CleanExiMM_ADCY2.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR009398. Adcy_conserved_dom.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADCY2_MOUSE
AccessioniPrimary (citable) accession number: Q80TL1
Secondary accession number(s): Q8CFU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.