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Protein

Adenylate cyclase type 5

Gene

Adcy5

Organism
Rattus norvegicus (Rat)
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 (PubMed:1409703). Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca2+ in response to increased blood glucose levels and contributes to the regulation of Ca2+-dependent insulin secretion.By similarity1 Publication

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

Enzyme regulationi

Activated by forskolin. Activated by GNAS. Activity is further increased by interaction with the G protein beta and gamma subunit complex formed by GNB1 and GNG2 (By similarity). Is not activated by calmodulin. Inhibited by adenosine and ATP analogs. Inhibited by calcium ions, already at micromolar concentrations (By similarity). Phosphorylation by RAF1 results in its activation (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi475Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi475Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi476Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi519Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi519Magnesium 2; catalyticPROSITE-ProRule annotation1
Binding sitei563ATPBy similarity1
Binding sitei1124ATPBy similarity1
Binding sitei1245ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi475 – 480ATPBy similarity6
Nucleotide bindingi517 – 519ATPBy similarity3
Nucleotide bindingi1198 – 1200ATPBy similarity3
Nucleotide bindingi1205 – 1209ATPBy similarity5

GO - Molecular functioni

  • adenylate cyclase activity Source: RGD
  • ATP binding Source: UniProtKB-KW
  • calcium- and calmodulin-responsive adenylate cyclase activity Source: RGD
  • 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, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 5 (EC:4.6.1.11 Publication)
Alternative name(s):
ATP pyrophosphate-lyase 5
Adenylate cyclase type V
Adenylyl cyclase 5
Gene namesi
Name:Adcy5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71014. Adcy5.

Subcellular locationi

  • Cell membrane By similarity; Multi-pass membrane protein By similarity
  • Cell projectioncilium By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 242CytoplasmicSequence analysisAdd BLAST242
Transmembranei243 – 263HelicalSequence analysisAdd BLAST21
Transmembranei269 – 289HelicalSequence analysisAdd BLAST21
Transmembranei300 – 320HelicalSequence analysisAdd BLAST21
Transmembranei326 – 346HelicalSequence analysisAdd BLAST21
Transmembranei351 – 371HelicalSequence analysisAdd BLAST21
Transmembranei375 – 395HelicalSequence analysisAdd BLAST21
Topological domaini396 – 763CytoplasmicSequence analysisAdd BLAST368
Transmembranei764 – 784HelicalSequence analysisAdd BLAST21
Transmembranei790 – 810HelicalSequence analysisAdd BLAST21
Transmembranei837 – 857HelicalSequence analysisAdd BLAST21
Topological domaini858 – 910ExtracellularSequence analysisAdd BLAST53
Transmembranei911 – 931HelicalSequence analysisAdd BLAST21
Transmembranei936 – 956HelicalSequence analysisAdd BLAST21
Transmembranei985 – 1005HelicalSequence analysisAdd BLAST21
Topological domaini1006 – 1262CytoplasmicSequence analysisAdd BLAST257

GO - Cellular componenti

  • cilium Source: UniProtKB
  • endosome Source: RGD
  • integral component of membrane Source: UniProtKB
  • membrane raft Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2880.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001956971 – 1262Adenylate cyclase type 5Add BLAST1262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23Omega-N-methylarginineBy similarity1
Modified residuei97PhosphoserineBy similarity1
Modified residuei156PhosphoserineBy similarity1
Modified residuei667PhosphoserineBy similarity1
Modified residuei755PhosphoserineBy similarity1
Glycosylationi871N-linked (GlcNAc...)Sequence analysis1
Glycosylationi888N-linked (GlcNAc...)Sequence analysis1
Glycosylationi973N-linked (GlcNAc...)Sequence analysis1
Modified residuei1012PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylated by RAF1.By similarity

Keywords - PTMi

Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ04400.
PRIDEiQ04400.

PTM databases

SwissPalmiQ04400.

Expressioni

Tissue specificityi

Detected in brain and kidney.1 Publication

Interactioni

Subunit structurei

Interacts with GNAS, GNB1 and GNG2 (By similarity). Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2 (By similarity). Interacts with RAF1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi249116. 1 interactor.
STRINGi10116.ENSRNOP00000046488.

Chemistry databases

BindingDBiQ04400.

Structurei

3D structure databases

ProteinModelPortaliQ04400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini470 – 597Guanylate cyclase 1PROSITE-ProRule annotationAdd BLAST128
Domaini1072 – 1211Guanylate cyclase 2PROSITE-ProRule annotationAdd BLAST140

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi64 – 67Poly-Gln4
Compositional biasi141 – 147Poly-Ala7

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.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiQ04400.
KOiK08045.

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.

Q04400-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGSKSVSPP GYAAQTAASP APRGGPEHRA AWGEADSRAN GYPHAPGGST
60 70 80 90 100
RGSTKRSGGA VTPQQQQRLA SRWRGGDDDE DPPLSGDDPL VGGFGFSFRS
110 120 130 140 150
KSAWQERGGD DGGRGSRRQR RGAAGGGSTR APPAGGSGSS AAAAAAAGGT
160 170 180 190 200
EVRPRSVEVG LEERRGKGRA AEELEPGTGT VEDGDGSEDG GSSVASGSGT
210 220 230 240 250
GTVLSLGACC LALLQIFRSK KFPSDKLERL YQRYFFRLNQ SSLTMLMAVL
260 270 280 290 300
VLVCLVMLAF HAARPPLQVV YLAVLAAAVG VILIMAVLCN RAAFHQDHMG
310 320 330 340 350
LACYALIAVV LAVQVVGLLL PQPRSASEGI WWTVFFIYTI YTLLPVRMRA
360 370 380 390 400
AVLSGVLLSA LHLAISLHTN AQDQFLLKQL VSNVLIFSCT NIVGVCTHYP
410 420 430 440 450
AEVSQRQAFQ ETRECIQARL HSQRENQQQE RLLLSVLPRH VAMEMKADIN
460 470 480 490 500
AKQEDMMFHK IYIQKHDNVS ILFADIEGFT SLASQCTAQE LVMTLNELFA
510 520 530 540 550
RFDKLAAENH CLRIKILGDC YYCVSGLPEA RADHAHCCVE MGMDMIEAIS
560 570 580 590 600
SVREVTGVNV NMRVGIHSGR VHCGVLGLRK WQFDVWSNDV TLANHMEAGG
610 620 630 640 650
KAGRIHITKA TLNYLNGDYE VEPGCGGERN AYLKEHSIET FLILRCTQKR
660 670 680 690 700
KEEKAMIAKM NRQRTNSIGH NPPHWGAERP FYNHLGGNQV SKEMKRMGFE
710 720 730 740 750
DPKDKNAQES ANPEDEVDEF LGRAIDARSI DRLRSEHVRK FLLTFREPDL
760 770 780 790 800
EKKYSKQVDD RFGAYVACAS LVFLFICFVQ ITIVPHSLFM LSFYLSCFLL
810 820 830 840 850
LALVVFISVI YACVKLFPTP LQTLSRKIVR SKKNSTLVGV FTITLVFLSA
860 870 880 890 900
FVNMFMCNSK NLVGCLAEEH NITVNQVNAC HVMESAFNYS LGDEQGFCGS
910 920 930 940 950
PQSNCNFPEY FTYSVLLSLL ACSVFLQISC IGKLVLMLAI ELIYVLIVEV
960 970 980 990 1000
PGVTLFDNAD LLVTANAIDF SNNGTSQCPE HATKVALKVV TPIIISVFVL
1010 1020 1030 1040 1050
ALYLHAQQVE STARLDFLWK LQATEEKEEM EELQAYNRRL LHNILPKDVA
1060 1070 1080 1090 1100
AHFLARERRN DELYYQSCEC VAVMFASIAN FSEFYVELEA NNEGVECLRL
1110 1120 1130 1140 1150
LNEIIADFDE IISEDRFRQL EKIKTIGSTY MAASGLNDST YDKAGKTHIK
1160 1170 1180 1190 1200
ALADFAMKLM DQMKYINEHS FNNFQMKIGL NIGPVVAGVI GARKPQYDIW
1210 1220 1230 1240 1250
GNTVNVASRM DSTGVPDRIQ VTTDMYQVLA ANTYQLECRG VVKVKGKGEM
1260
MTYFLNGGPP LS
Length:1,262
Mass (Da):139,179
Last modified:November 1, 1997 - v2
Checksum:i8B147E201C5DF601
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96159 mRNA. Translation: AAB39764.1.
RefSeqiNP_072122.1. NM_022600.1.
UniGeneiRn.6278.

Genome annotation databases

GeneIDi64532.
KEGGirno:64532.
UCSCiRGD:71014. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96159 mRNA. Translation: AAB39764.1.
RefSeqiNP_072122.1. NM_022600.1.
UniGeneiRn.6278.

3D structure databases

ProteinModelPortaliQ04400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249116. 1 interactor.
STRINGi10116.ENSRNOP00000046488.

Chemistry databases

BindingDBiQ04400.
ChEMBLiCHEMBL2880.

PTM databases

SwissPalmiQ04400.

Proteomic databases

PaxDbiQ04400.
PRIDEiQ04400.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64532.
KEGGirno:64532.
UCSCiRGD:71014. rat.

Organism-specific databases

CTDi111.
RGDi71014. Adcy5.

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiQ04400.
KOiK08045.

Enzyme and pathway databases

BRENDAi4.6.1.1. 5301.

Miscellaneous databases

PROiQ04400.

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 nameiADCY5_RAT
AccessioniPrimary (citable) accession number: Q04400
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 134 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. 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.