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Protein

Adenylate cyclase type 1

Gene

Adcy1

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

Functioni

Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates responses to increased cellular Ca2+/calmodulin levels (PubMed:9662407, PubMed:7816821). May be involved in regulatory processes in the central nervous system (PubMed:9662407). May play a role in memory and learning (PubMed:7816821). Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina (PubMed:24048828).3 Publications

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.1 Publication

Cofactori

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

Activity regulationi

Activated by calcium/calmodulin (PubMed:9662407). Activated by forskolin. Activated by the G protein alpha subunit GNAS. Inhibited by the G protein beta and gamma subunit complex. Inhibited by the ATP analogs adenosine, 2'-deoxyadenosine and 2'-deoxy-3'-AMP.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi307Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi307Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi308Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi351Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi351Magnesium 2; catalyticPROSITE-ProRule annotation1
Binding sitei395ATPBy similarity1
Binding sitei919ATPBy similarity1
Binding sitei1043ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi307 – 312ATPBy similarity6
Nucleotide bindingi349 – 351ATPBy similarity3
Nucleotide bindingi996 – 998ATPBy similarity3
Nucleotide bindingi1003 – 1007ATPBy similarity5

GO - Molecular functioni

  • adenylate cyclase activity Source: MGI
  • ATP binding Source: UniProtKB-KW
  • calcium- and calmodulin-responsive adenylate cyclase activity Source: UniProtKB
  • calmodulin binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionCalmodulin-binding, Lyase
Biological processBiological rhythms, cAMP biosynthesis
LigandATP-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-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 1 (EC:4.6.1.11 Publication)
Alternative name(s):
ATP pyrophosphate-lyase 1
Adenylate cyclase type I
Adenylyl cyclase 1
Ca(2+)/calmodulin-activated adenylyl cyclase
Gene namesi
Name:Adcy1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:99677 Adcy1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 62CytoplasmicSequence analysisAdd BLAST62
Transmembranei63 – 83HelicalSequence analysisAdd BLAST21
Transmembranei87 – 107HelicalSequence analysisAdd BLAST21
Transmembranei124 – 144HelicalSequence analysisAdd BLAST21
Transmembranei157 – 177HelicalSequence analysisAdd BLAST21
Transmembranei182 – 202HelicalSequence analysisAdd BLAST21
Transmembranei213 – 233HelicalSequence analysisAdd BLAST21
Topological domaini234 – 609CytoplasmicSequence analysisAdd BLAST376
Transmembranei610 – 630HelicalSequence analysisAdd BLAST21
Transmembranei634 – 654HelicalSequence analysisAdd BLAST21
Transmembranei673 – 693HelicalSequence analysisAdd BLAST21
Transmembranei724 – 744HelicalSequence analysisAdd BLAST21
Transmembranei752 – 772HelicalSequence analysisAdd BLAST21
Transmembranei774 – 793HelicalSequence analysisAdd BLAST20
Topological domaini794 – 1118CytoplasmicSequence analysisAdd BLAST325

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice appear grossly normal and healthy, but have decreased levels of calmodulin-sensitive adenylyl cyclase activity in the brain (PubMed:7816821). They show impaired spatial memory (PubMed:7816821). Mice show a significant reduction in daytime contrast sensitivity (PubMed:24048828).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001956831 – 1118Adenylate cyclase type 1Add BLAST1118

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei550PhosphoserineCombined sources1
Glycosylationi703N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO88444
PaxDbiO88444
PeptideAtlasiO88444
PRIDEiO88444

PTM databases

iPTMnetiO88444
PhosphoSitePlusiO88444
SwissPalmiO88444

Expressioni

Tissue specificityi

Expressed throughout inner ear development.1 Publication

Inductioni

Expression in the retina oscillates in a circadian manner.1 Publication

Gene expression databases

BgeeiENSMUSG00000020431 Expressed in 227 organ(s), highest expression level in cerebellum
CleanExiMM_ADCY1
GenevisibleiO88444 MM

Interactioni

Subunit structurei

Interacts with CALM.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020706

Structurei

3D structure databases

ProteinModelPortaliO88444
SMRiO88444
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni492 – 519Interaction with calmodulinBy similarityAdd BLAST28
Regioni1023 – 1046Interaction with calmodulinBy similarityAdd BLAST24

Domaini

The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal modules have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two modules.By similarity

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3619 Eukaryota
COG2114 LUCA
GeneTreeiENSGT00760000119042
HOGENOMiHOG000006941
HOVERGENiHBG050458
InParanoidiO88444
KOiK08041
OMAiKYKQIER
OrthoDBiEOG091G05JR
PhylomeDBiO88444
TreeFamiTF313845

Family and domain databases

Gene3Di3.30.70.1230, 2 hits
InterProiView protein in InterPro
IPR001054 A/G_cyclase
IPR018297 A/G_cyclase_CS
IPR032628 AC_N
IPR030672 Adcy
IPR029787 Nucleotide_cyclase
PfamiView protein in Pfam
PF16214 AC_N, 1 hit
PF00211 Guanylate_cyc, 2 hits
PIRSFiPIRSF039050 Ade_cyc, 1 hit
SMARTiView protein in SMART
SM00044 CYCc, 2 hits
SUPFAMiSSF55073 SSF55073, 2 hits
PROSITEiView protein in PROSITE
PS00452 GUANYLATE_CYCLASE_1, 2 hits
PS50125 GUANYLATE_CYCLASE_2, 2 hits

Sequencei

Sequence statusi: Complete.

O88444-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGAPRGQGG GGGAGEPGGA ERAAGPGGRR GFRACGEEFA CPELEALFRG
60 70 80 90 100
YTLRLEQAAT LKALAVLSLL AGALALAELL GAPGPAPGLA KGSHPVHCIL
110 120 130 140 150
FLALFVVTNV RSLQVSQLQQ VGQLALFFSL TFALLCCPFA LGGPARSSAG
160 170 180 190 200
GAMGSTVAEQ GVWQLLLVTF VSYALLPVRS LLAIGFGLVV AASHLLVTAA
210 220 230 240 250
LVPAKRPRLW RTLGANALLF FGVNMYGVFV RILTERSQRK AFLQARNCIE
260 270 280 290 300
DRLRLEDENE KQERLLMSLL PRNVAMEMKE DFLKPPERIF HKIYIQRHDN
310 320 330 340 350
VSILFADIVG FTGLASQCTA QELVKLLNEL FGKFDELATE NHCRRIKILG
360 370 380 390 400
DCYYCVSGLT QPKTDHAHCC VEMGLDMIDT ITSVAEATEV DLNMRVGLHT
410 420 430 440 450
GRVLCGVLGL RKWQYDVWSN DVTLANVMEA AGLPGKVHIT KTTLACLNGD
460 470 480 490 500
YEVEPGHGHE RNTFLRTHNI ETFFIVPSHR RKIFPGLILS DIKPAKRMKF
510 520 530 540 550
KTVCYLLVQL MHCRKMFKAE IPFSNVMTCE DDDKRRALRT ASEKLRNRSS
560 570 580 590 600
FSTNVVYTTP GTRVNRYISR LLEARQTELE MADLNFFTLK YKHVEREQKY
610 620 630 640 650
HQLQDEYFTS AVVLALILAA LFGLIYLLVI PQSVAVLLLL VFSICFLVAC
660 670 680 690 700
TLYLHITRVQ CFPGCLTIQI RTALCVFIVV LIYSVAQGCV VGCLPWAWSS
710 720 730 740 750
QSNSSLVVLA AGGRRTVLPA LPCESAHHAL LCCLVGTLPL AIFLRVSSLP
760 770 780 790 800
KMILLSGLTT SYILVLELSG YTKVGGGALS GRSYEPIMAI LLFSCTLALH
810 820 830 840 850
ARQVDVRLRL DYLWAAQAEE ERDDMERVKL DNKRILFNLL PAHVAQHFLM
860 870 880 890 900
SNPRNMDLYY QSYSQVGVMF ASIPNFNDFY IELDGNNMGV ECLRLLNEII
910 920 930 940 950
ADFDELMDKD FYKDLEKIKT IGSTYMAAVG LAPTAGTRAK KSISSHLCTL
960 970 980 990 1000
ADFAIDMFDV LDEINYQSYN DFVLRVGINV GPVVAGVIGA RRPQYDIWGN
1010 1020 1030 1040 1050
TVNVASRMDS TGVQGRIQVT EEVHRLLKRC SYQFVCRGKV SVKGKGEMLT
1060 1070 1080 1090 1100
YFLEGRTDGN SSHGRTFRLE RRMCPYGRGG GQARRPPLCP AAGPPVRPGL
1110
PPAPTSQYLS STAAGKEA
Length:1,118
Mass (Da):123,373
Last modified:April 12, 2005 - v2
Checksum:iCEFAFF3940B22277
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti147 – 155SSAGGAMGS → ALQEAQWAR in AAC29478 (PubMed:9662407).Curated9
Sequence conflicti234T → A in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti270L → M in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti319T → K in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti466R → K in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti523F → I in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti542S → T in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti549S → T in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti570R → L in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti598Q → R in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti692G → V in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti697A → S in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti707V → L in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti713G → C in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti720 – 721AL → GP in AAC29478 (PubMed:9662407).Curated2
Sequence conflicti774 – 776VGG → AMGA in AAC29478 (PubMed:9662407).Curated3
Sequence conflicti867 – 869GVM → AVL in AAC29478 (PubMed:9662407).Curated3
Sequence conflicti938R → K in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti991R → C in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti1020T → I in AAC29478 (PubMed:9662407).Curated1
Sequence conflicti1030C → S in AAC29478 (PubMed:9662407).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL669838 Genomic DNA No translation available.
AF053980 mRNA Translation: AAC29478.1
CCDSiCCDS24426.1
RefSeqiNP_033752.1, NM_009622.1
UniGeneiMm.259733

Genome annotation databases

EnsembliENSMUST00000020706; ENSMUSP00000020706; ENSMUSG00000020431
GeneIDi432530
KEGGimmu:432530
UCSCiuc007hzf.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL669838 Genomic DNA No translation available.
AF053980 mRNA Translation: AAC29478.1
CCDSiCCDS24426.1
RefSeqiNP_033752.1, NM_009622.1
UniGeneiMm.259733

3D structure databases

ProteinModelPortaliO88444
SMRiO88444
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020706

PTM databases

iPTMnetiO88444
PhosphoSitePlusiO88444
SwissPalmiO88444

Proteomic databases

MaxQBiO88444
PaxDbiO88444
PeptideAtlasiO88444
PRIDEiO88444

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020706; ENSMUSP00000020706; ENSMUSG00000020431
GeneIDi432530
KEGGimmu:432530
UCSCiuc007hzf.1 mouse

Organism-specific databases

CTDi107
MGIiMGI:99677 Adcy1

Phylogenomic databases

eggNOGiKOG3619 Eukaryota
COG2114 LUCA
GeneTreeiENSGT00760000119042
HOGENOMiHOG000006941
HOVERGENiHBG050458
InParanoidiO88444
KOiK08041
OMAiKYKQIER
OrthoDBiEOG091G05JR
PhylomeDBiO88444
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-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

ChiTaRSiAdcy1 mouse
PROiPR:O88444
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020431 Expressed in 227 organ(s), highest expression level in cerebellum
CleanExiMM_ADCY1
GenevisibleiO88444 MM

Family and domain databases

Gene3Di3.30.70.1230, 2 hits
InterProiView protein in InterPro
IPR001054 A/G_cyclase
IPR018297 A/G_cyclase_CS
IPR032628 AC_N
IPR030672 Adcy
IPR029787 Nucleotide_cyclase
PfamiView protein in Pfam
PF16214 AC_N, 1 hit
PF00211 Guanylate_cyc, 2 hits
PIRSFiPIRSF039050 Ade_cyc, 1 hit
SMARTiView protein in SMART
SM00044 CYCc, 2 hits
SUPFAMiSSF55073 SSF55073, 2 hits
PROSITEiView protein in PROSITE
PS00452 GUANYLATE_CYCLASE_1, 2 hits
PS50125 GUANYLATE_CYCLASE_2, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiADCY1_MOUSE
AccessioniPrimary (citable) accession number: O88444
Secondary accession number(s): Q5SS89
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: April 12, 2005
Last modified: November 7, 2018
This is version 142 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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