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Protein

Adenylate cyclase type 5

Gene

Adcy5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

GO - Biological processi

  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: RGD
  • aging Source: RGD
  • brain development Source: RGD
  • cAMP biosynthetic process Source: RGD
  • cellular response to forskolin Source: UniProtKB
  • cGMP biosynthetic process Source: GO_Central
  • heart development Source: RGD
  • positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  • regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • response to morphine Source: RGD
  • signal transduction Source: GO_Central

Keywordsi

Molecular functionLyase
Biological processcAMP biosynthesis
LigandATP-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71014 Adcy5

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 – 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

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...) asparagineSequence analysis1
Glycosylationi888N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi973N-linked (GlcNAc...) asparagineSequence 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
SMRiQ04400
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

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
InterProiView protein in InterPro
IPR001054 A/G_cyclase
IPR018297 A/G_cyclase_CS
IPR032628 AC_N
IPR030672 Adcy
IPR009398 Adcy_conserved_dom
IPR029787 Nucleotide_cyclase
PfamiView protein in Pfam
PF16214 AC_N, 1 hit
PF06327 DUF1053, 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.

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

Similar proteinsi

Entry informationi

Entry nameiADCY5_RAT
AccessioniPrimary (citable) accession number: Q04400
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1997
Last modified: May 23, 2018
This is version 141 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

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