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Protein

Adenylate cyclase type 8

Gene

Adcy8

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

Functioni

This is a membrane-bound, calcium-stimulable adenylyl cyclase. May be involved in learning, in memory and in drug dependence (By similarity).By similarity

Catalytic activityi

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

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 calcium/calmodulin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi417Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi417Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi418Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi461Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi461Magnesium 2; catalyticPROSITE-ProRule annotation1
Binding sitei505ATPBy similarity1
Binding sitei1032ATPBy similarity1
Binding sitei1154ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi417 – 422ATPBy similarity6
Nucleotide bindingi459 – 461ATPBy similarity3
Nucleotide bindingi1107 – 1109ATPBy similarity3
Nucleotide bindingi1114 – 1118ATPBy similarity5

GO - Molecular functioni

  • adenylate cyclase activity Source: MGI
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

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.
ReactomeiR-MMU-163359. Glucagon signaling in metabolic regulation.
R-MMU-163615. PKA activation.
R-MMU-164378. PKA activation in glucagon signalling.
R-MMU-170660. Adenylate cyclase activating pathway.
R-MMU-170670. Adenylate cyclase inhibitory pathway.
R-MMU-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-MMU-418555. G alpha (s) signalling events.
R-MMU-418597. G alpha (z) signalling events.
R-MMU-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-MMU-442720. CREB phosphorylation through the activation of Adenylate Cyclase.
R-MMU-5610787. Hedgehog 'off' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 8 (EC:4.6.1.1)
Alternative name(s):
ATP pyrophosphate-lyase 8
Adenylate cyclase type VIII
Adenylyl cyclase 8
Ca(2+)/calmodulin-activated adenylyl cyclase
Gene namesi
Name:Adcy8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1341110. Adcy8.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 180CytoplasmicSequence analysisAdd BLAST180
Transmembranei181 – 201HelicalSequence analysisAdd BLAST21
Transmembranei210 – 230HelicalSequence analysisAdd BLAST21
Transmembranei245 – 265HelicalSequence analysisAdd BLAST21
Transmembranei272 – 292HelicalSequence analysisAdd BLAST21
Transmembranei294 – 314HelicalSequence analysisAdd BLAST21
Transmembranei319 – 339HelicalSequence analysisAdd BLAST21
Topological domaini340 – 713CytoplasmicSequence analysisAdd BLAST374
Transmembranei714 – 734HelicalSequence analysisAdd BLAST21
Transmembranei736 – 756HelicalSequence analysisAdd BLAST21
Transmembranei785 – 805HelicalSequence analysisAdd BLAST21
Transmembranei829 – 849HelicalSequence analysisAdd BLAST21
Transmembranei859 – 879HelicalSequence analysisAdd BLAST21
Transmembranei892 – 912HelicalSequence analysisAdd BLAST21
Topological domaini913 – 1249CytoplasmicSequence analysisAdd BLAST337

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001957061 – 1249Adenylate cyclase type 8Add BLAST1249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei55Omega-N-methylarginineCombined sources1
Modified residuei612PhosphoserineCombined sources1
Modified residuei622PhosphoserineCombined sources1
Glycosylationi815N-linked (GlcNAc...)Sequence analysis1
Glycosylationi819N-linked (GlcNAc...)Sequence analysis1
Glycosylationi886N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP97490.
PaxDbiP97490.
PeptideAtlasiP97490.
PRIDEiP97490.

PTM databases

iPTMnetiP97490.
PhosphoSitePlusiP97490.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022376.
CleanExiMM_ADCY8.
GenevisibleiP97490. MM.

Interactioni

Protein-protein interaction databases

BioGridi197977. 4 interactors.
MINTiMINT-4997019.
STRINGi10090.ENSMUSP00000023007.

Structurei

3D structure databases

ProteinModelPortaliP97490.
SMRiP97490.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.
GeneTreeiENSGT00760000119042.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiP97490.
KOiK08048.
OMAiVVLFMCM.
OrthoDBiEOG091G05JR.
TreeFamiTF313845.

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.

P97490-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSDVHCLS GSEELYTIQP TPPAGDDGSG SRPQRLLWQT AVRHITEQRF
60 70 80 90 100
IHGHRGGGGG GVSRKASNPA GSGPNHHAPQ LSSDSVLPLY SLGPGERAHN
110 120 130 140 150
TGGTKVFPER SGSGSASGSG GGGDLGFLHL DCAPSNSDFF LNGGYSYRGV
160 170 180 190 200
IFPTLRNSFK SRDLERLYQR YFLGQRRKSE VVMNVLDVLT KLTLLVLHLS
210 220 230 240 250
LASAPMDPLK GILLGFFTGI EVVICALVVV RKDNTSHTYL QYSGVVTWVA
260 270 280 290 300
MTTQILAAGL GYGLLGDGIG YVLFTLFATY SMLPLPLTWA ILAGLGTSLL
310 320 330 340 350
QVTLQVLIPR LAVFSINQVL AQVVLFMCMN TAGIFISYLS DRAQRQAFLE
360 370 380 390 400
TRRCVEARLR LETENQRQER LVLSVLPRFV VLEMINDMTN VEDEHLQHQF
410 420 430 440 450
HRIYIHRYEN VSILFADVKG FTNLSTTLSA QELVRMLNEL FARFDRLAHE
460 470 480 490 500
HHCLRIKILG DCYYCVSGLP EPRRDHAHCC VEMGLSMIKT IRFVRSRTKH
510 520 530 540 550
DVDMRIGIHS GSVLCGVLGL RKWQFDVWSW DVDIANKLES GGIPGRIHIS
560 570 580 590 600
KATLDCLNGD YNVEEGHGKE RNEFLRKHNI ETYLIKQPEE SLLCLPEDIV
610 620 630 640 650
KESVSCSDRR NSGATFTEGS WSPELPFDNI VGKQNTLAAL TRNSINLLPN
660 670 680 690 700
HLAQALHVQS GPEEINKRIE HTIDLRSGDK LRREHIKPFS LMFKDSSLEH
710 720 730 740 750
KYSQMRDEVF KSNLVCAFIV LLFITAIQSL LPSSRLMPMT IQFSILIMLH
760 770 780 790 800
SALVLITTAE DYKCLPLILR KTCCWINETY LARNVIIFAS ILINFLGAVL
810 820 830 840 850
NILWCDFDKS IPLKNLTFNS SAVFTDICSY PEYFVFTGVL AMVTCAVFLR
860 870 880 890 900
LNSVLKLAVL LIMIAIYALL TETIYAGLFL SYDNLNHSGE DFLGTKEASL
910 920 930 940 950
LLMAMFLLAV FYHGQQLEYT ARLDFLWRVQ AKEEINEMKE LREHNENMLR
960 970 980 990 1000
NILPSHVARH FLEKDRDNEE LYSQSYDAVG VMFASIPGFA DFYSQTEMNN
1010 1020 1030 1040 1050
QGVECLRLLN EIIADFDELL GEDRFQDIEK IKTIGSTYMA VSGLSPEKQQ
1060 1070 1080 1090 1100
CEDKWGHLCA LADFSLALTE SIQEINKHSF NNFELRIGIS HGSVVAGVIG
1110 1120 1130 1140 1150
AKKPQYDIWG KTVNLASRMD STGVSGRIQV PEETYLILKD QGFAFDYRGE
1160 1170 1180 1190 1200
IYVKGISEQE GKIKTYFLLG RVQPNPFILP PRRLPGQYSL AAVVLGLVQS
1210 1220 1230 1240
LNRQRQKQLL NENSNSGIIK SHYNRRTLLT PSGPEPGAQA EGTDKSDLP
Length:1,249
Mass (Da):140,095
Last modified:October 3, 2012 - v2
Checksum:i26103B6E0DB9C701
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24A → V in AAB41885 (Ref. 1) Curated1
Sequence conflicti59G → C in AAB41885 (Ref. 1) Curated1
Sequence conflicti849L → V in AAB41885 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85021 mRNA. Translation: AAB41885.1.
AC116996 Genomic DNA. No translation available.
AC160934 Genomic DNA. No translation available.
CH466545 Genomic DNA. Translation: EDL29360.1.
CH466545 Genomic DNA. Translation: EDL29361.1.
CCDSiCCDS27506.1.
RefSeqiNP_033753.2. NM_009623.2.
UniGeneiMm.1425.

Genome annotation databases

EnsembliENSMUST00000023007; ENSMUSP00000023007; ENSMUSG00000022376.
GeneIDi11514.
KEGGimmu:11514.
UCSCiuc007vzo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85021 mRNA. Translation: AAB41885.1.
AC116996 Genomic DNA. No translation available.
AC160934 Genomic DNA. No translation available.
CH466545 Genomic DNA. Translation: EDL29360.1.
CH466545 Genomic DNA. Translation: EDL29361.1.
CCDSiCCDS27506.1.
RefSeqiNP_033753.2. NM_009623.2.
UniGeneiMm.1425.

3D structure databases

ProteinModelPortaliP97490.
SMRiP97490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197977. 4 interactors.
MINTiMINT-4997019.
STRINGi10090.ENSMUSP00000023007.

PTM databases

iPTMnetiP97490.
PhosphoSitePlusiP97490.

Proteomic databases

MaxQBiP97490.
PaxDbiP97490.
PeptideAtlasiP97490.
PRIDEiP97490.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023007; ENSMUSP00000023007; ENSMUSG00000022376.
GeneIDi11514.
KEGGimmu:11514.
UCSCiuc007vzo.1. mouse.

Organism-specific databases

CTDi114.
MGIiMGI:1341110. Adcy8.

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000119042.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiP97490.
KOiK08048.
OMAiVVLFMCM.
OrthoDBiEOG091G05JR.
TreeFamiTF313845.

Enzyme and pathway databases

BRENDAi4.6.1.1. 3474.
ReactomeiR-MMU-163359. Glucagon signaling in metabolic regulation.
R-MMU-163615. PKA activation.
R-MMU-164378. PKA activation in glucagon signalling.
R-MMU-170660. Adenylate cyclase activating pathway.
R-MMU-170670. Adenylate cyclase inhibitory pathway.
R-MMU-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-MMU-418555. G alpha (s) signalling events.
R-MMU-418597. G alpha (z) signalling events.
R-MMU-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-MMU-442720. CREB phosphorylation through the activation of Adenylate Cyclase.
R-MMU-5610787. Hedgehog 'off' state.

Miscellaneous databases

PROiP97490.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022376.
CleanExiMM_ADCY8.
GenevisibleiP97490. MM.

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 nameiADCY8_MOUSE
AccessioniPrimary (citable) accession number: P97490
Secondary accession number(s): G3X8V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2012
Last modified: November 2, 2016
This is version 130 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.