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Protein

Adenylate cyclase type 6

Gene

Adcy6

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 downstream of G protein-coupled receptors (PubMed:18071070, PubMed:24363043). Functions in signaling cascades downstream of beta-adrenergic receptors in the heart and in vascular smooth muscle cells (PubMed:18071070). Functions in signaling cascades downstream of the vasopressin receptor in the kidney and has a role in renal water reabsorption (PubMed:20466003, PubMed:20864687). Functions in signaling cascades downstream of PTH1R and plays a role in regulating renal phosphate excretion (PubMed:24854272). Functions in signaling cascades downstream of the VIP and SCT receptors in pancreas and contributes to the regulation of pancreatic amylase and fluid secretion (PubMed:23753526). Signaling mediates cAMP-dependent activation of protein kinase PKA and promotes increased phosphorylation of various proteins, including AKT (PubMed:18071070, PubMed:23753526). Plays a role in regulating cardiac sarcoplasmic reticulum Ca2+ uptake and storage, and is required for normal heart ventricular contractibility (PubMed:18071070). May contribute to normal heart function (PubMed:18071070, PubMed:20359598). Mediates vasodilatation after activation of beta-adrenergic receptors by isoproterenol (By similarity). Contributes to bone cell responses to mechanical stimuli (PubMed:20371630, PubMed:24277577).By similarity10 Publications

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.7 Publications

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 (PubMed:18071070, PubMed:20466003, PubMed:20864687, PubMed:23753526, PubMed:24363043). Inhibited by calcium ions, already at micromolar concentrations (PubMed:1379717, PubMed:18071070). Inhibited by adenosine, AMP and their analogs (By similarity). Activated by GNAS. Is further activated by the complex formed by GNB1 and GNG2 (By similarity). Phosphorylation by RAF1 results in its activation (By similarity).By similarity6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi382 – 3821Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi382 – 3821Magnesium 2; catalyticPROSITE-ProRule annotation
Metal bindingi383 – 3831Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation
Metal bindingi426 – 4261Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi426 – 4261Magnesium 2; catalyticPROSITE-ProRule annotation
Binding sitei470 – 4701ATPBy similarity
Binding sitei1028 – 10281ATPBy similarity
Binding sitei1149 – 11491ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi382 – 3876ATPBy similarity
Nucleotide bindingi424 – 4263ATPBy similarity
Nucleotide bindingi1102 – 11043ATPBy similarity
Nucleotide bindingi1109 – 11135ATPBy similarity

GO - Molecular functioni

  • adenylate cyclase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • calcium- and calmodulin-responsive adenylate cyclase activity Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • protein kinase binding Source: BHF-UCL
  • scaffold protein binding Source: MGI

GO - Biological processi

  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • cAMP biosynthetic process Source: UniProtKB
  • cellular response to catecholamine stimulus Source: MGI
  • cellular response to forskolin Source: UniProtKB
  • cellular response to prostaglandin E stimulus Source: MGI
  • cellular response to vasopressin Source: UniProtKB
  • dopamine receptor signaling pathway Source: MGI
  • intracellular signal transduction Source: InterPro
  • negative regulation of neuron projection development Source: ParkinsonsUK-UCL
  • negative regulation of urine volume Source: UniProtKB
  • regulation of vasodilation Source: MGI
  • renal water homeostasis Source: UniProtKB
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 6 (EC:4.6.1.16 Publications)
Alternative name(s):
ATP pyrophosphate-lyase 6
Adenylate cyclase type VI
Adenylyl cyclase 62 Publications
Short name:
AC62 Publications
Ca(2+)-inhibitable adenylyl cyclase
Gene namesi
Name:Adcy6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:87917. Adcy6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 149149CytoplasmicSequence analysisAdd
BLAST
Transmembranei150 – 16617HelicalSequence analysisAdd
BLAST
Transmembranei179 – 19517HelicalSequence analysisAdd
BLAST
Transmembranei212 – 22817HelicalSequence analysisAdd
BLAST
Transmembranei237 – 25317HelicalSequence analysisAdd
BLAST
Transmembranei257 – 27317HelicalSequence analysisAdd
BLAST
Transmembranei287 – 30317HelicalSequence analysisAdd
BLAST
Topological domaini304 – 670367CytoplasmicSequence analysisAdd
BLAST
Transmembranei671 – 68818HelicalSequence analysisAdd
BLAST
Transmembranei699 – 71517HelicalSequence analysisAdd
BLAST
Transmembranei740 – 75617HelicalSequence analysisAdd
BLAST
Topological domaini757 – 81660ExtracellularSequence analysisAdd
BLAST
Transmembranei817 – 83317HelicalSequence analysisAdd
BLAST
Transmembranei836 – 85217HelicalSequence analysisAdd
BLAST
Transmembranei894 – 91017HelicalSequence analysisAdd
BLAST
Topological domaini911 – 1165255CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutant mice are born at the expected Mendelian rate, present no obvious phenotype and are fertile (PubMed:18071070, PubMed:20466003, PubMed:23753526, PubMed:24277577). Their hearts display a decrease in left ventricular pressure, both at the basal level and after activation of beta-adrenergic receptors (PubMed:18071070). Besides, their hearts show defects in sarcoplasmic Ca2+ uptake and storage, and decreased levels of protein phosphorylation (PubMed:18071070). Male mice show increased mortality after transversal aortic constriction (PubMed:20359598). In contrast, female mice do not show increased mortality after transversal aortic constriction, and develop less heart hypertrophy and fibrosis than wild-type (PubMed:20359598). Compared to wild-type, mutant mice drink more and produce greater volumes of urine with decreased osmolarity, but there is no difference in the total quantity of excreted urinary solutes and no difference in blood plasma composition (PubMed:20466003, PubMed:20864687). The impaired urinary water homeostasis is due to retention of AQP2 in intracellular vesicles and decreased AQP2 levels at the cell membrane (PubMed:20466003). Mutant mice display increased urinary inorganic phosphate excretion, but normal plasma phosphate levels (PubMed:24854272). Mutant mice display increased plasma levels of PTH and FGF23, the two principal regulators of urinary phosphate excretion (PubMed:24854272). Mutant mice display no obvious skeleton defects, but display less bone formation after load stress than wild-type (PubMed:24277577). Mutant mice lacking both Adcy6 and Pkd1 survive longer and have less severe polycystic kidney disease than mice lacking only Pkd1 (PubMed:24158982).8 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11651165Adenylate cyclase type 6PRO_0000195700Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531PhosphoserineBy similarity
Modified residuei85 – 851PhosphoserineBy similarity
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence analysis
Modified residuei553 – 5531PhosphoserineBy similarity
Modified residuei573 – 5731PhosphoserineCombined sources
Modified residuei659 – 6591PhosphoserineBy similarity
Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence analysis
Glycosylationi875 – 8751N-linked (GlcNAc...)Sequence analysis
Modified residuei916 – 9161PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylation by RAF1 increases enzyme activity. Phosphorylation by PKA on Ser-659 inhibits the GNAS-mediated increase in catalytic activity. Phosphorylation by PKC on Ser-553, Ser-659 and Thr-916 inhibits catalytic activity.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ01341.
PaxDbiQ01341.
PRIDEiQ01341.

PTM databases

iPTMnetiQ01341.
PhosphoSiteiQ01341.
SwissPalmiQ01341.

Expressioni

Tissue specificityi

Detected in kidney tubules (PubMed:20466003). Detected in primary bone cells with osteocyte morphology (PubMed:24277577). Detected in heart (at protein level) (PubMed:18071070). Highly expressed in heart (PubMed:1379717, PubMed:18071070). Detected in kidney, pancreas acini and ducts (PubMed:23753526). Weakly detectable in brain, intestine, lung and spleen (PubMed:1379717).5 Publications

Gene expression databases

CleanExiMM_ADCY6.

Interactioni

Subunit structurei

Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2 (PubMed:21670265). Interacts with RAF1. Interacts (via cytoplasmic N-terminus) with GNAS, GNB1 and GNG2 (By similarity).By similarity1 Publication

GO - Molecular functioni

  • protein kinase binding Source: BHF-UCL
  • scaffold protein binding Source: MGI

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000093939.

Structurei

3D structure databases

ProteinModelPortaliQ01341.
SMRiQ01341. Positions 362-550.
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.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiQ01341.
KOiK08046.
PhylomeDBiQ01341.

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.

Q01341-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWFSGLLVP KVDERKTAWG ERNGQKRPRH ANRASGFCAP RYMSCLKNAE
60 70 80 90 100
PPSPTPAAHT RCPWQDEAFI RRAGPGRGVE LGLRSVALGF DDTEVTTPMG
110 120 130 140 150
TAEVAPDTSP RSGPSCWHRL VQVFQSKQFR SAKLERLYQR YFFQMNQSSL
160 170 180 190 200
TLLMAVLVLL MAVLLTFHAA PAQPQPAYVA LLTCASVLFV VLMVVCNRHS
210 220 230 240 250
FRQDSMWVVS YVVLGILAAV QVGGALAANP HSPSAGLWCP VFFVYITYTL
260 270 280 290 300
LPIRMRAAVL SGLGLSTLHL ILAWQLNSSD PFLWKQLGAN VVLFLCTNAI
310 320 330 340 350
GVCTHYPAEV SQRQAFQETR GYIQARLHLQ HENRQQERLL LSVLPQHVAM
360 370 380 390 400
EMKEDINTKK EDMMFHKIYI QKHDNVSILF ADIEGFTSLA SQCTAQELVM
410 420 430 440 450
TLNELFARFD KLAAENHCLR IKILGDCYYC VSGLPEARAD HAHCCVEMGV
460 470 480 490 500
DMIEAISLVR EVTGVNVNMR VGIHSGRVHC GVLGLRKWQF DVWSNDVTLA
510 520 530 540 550
NHMEAGGGRR IHITRATLQY LNGDYEVEPG RGGERNAYLK EQCIETFLIL
560 570 580 590 600
GASQKRKEEK AMLAKLQRTR ANSMEGLMPR WVPDRAFSRT KDSKAFRQMG
610 620 630 640 650
IDDSSKDNRG AQDALNPEDE VDEFLGRAID ARSIDQLRKD HVRRFLLTFQ
660 670 680 690 700
REDLEKKYSR KVDPRFGAYV ACALLVFCFI CFIQLLVFPY STLILGIYAA
710 720 730 740 750
IFLLLLVTVL ICAVCSCGSF FPKALQRLSR NIVRSRVHST AVGIFSVLLV
760 770 780 790 800
FISAIANMFT CNHTPIRTCA ARMLNLTPAD VTACHLQQLN YSLGLDAPLC
810 820 830 840 850
EGTAPTCSFP EYFVGNVLLS LLASSVFLHI SSIGKLAMTF ILGFTYLVLL
860 870 880 890 900
LLGPPAAIFD NYDLLLGVHG LASSNETFDG LDCPAVGRVA LKYMTPVILL
910 920 930 940 950
VFALALYLHA QQVESTARLD FLWKLQATGE KEEMEELQAY NRRLLHNILP
960 970 980 990 1000
KDVAAHFLAR ERRNDELYYQ SCECVAVMFA SIANFSEFYV ELEANNEGVE
1010 1020 1030 1040 1050
CLRLLNEIIA DFDEIISEER FRQLEKIKTI GSTYMAASGL NASTYDQVGR
1060 1070 1080 1090 1100
SHITALADYA MRLMEQMKHI NEHSFNNFQM KIGLNMGPVV AGVIGARKPQ
1110 1120 1130 1140 1150
YDIWGNTVNV SSRMDSTGVP DRIQVTTDLY QVLAAKGYQL ECRGVVKVKG
1160
KGEMTTYFLN GGPSS
Length:1,165
Mass (Da):130,319
Last modified:April 1, 1993 - v1
Checksum:i24EE1BB45DF1E87E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471K → N in AAA37182 (PubMed:1332848).Curated
Sequence conflicti76 – 761G → A in AAA37182 (PubMed:1332848).Curated
Sequence conflicti508 – 5092GR → RAG in AAA37182 (PubMed:1332848).Curated
Sequence conflicti737 – 7371V → G in AAA37182 (PubMed:1332848).Curated
Sequence conflicti881 – 8811L → Q in AAA37182 (PubMed:1332848).Curated
Sequence conflicti990 – 9901V → M in AAA37182 (PubMed:1332848).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93422 mRNA. Translation: AAA37174.1.
M96653 mRNA. Translation: AAA37182.1.
PIRiA49201.
RefSeqiNP_031431.2. NM_007405.2.
UniGeneiMm.157091.

Genome annotation databases

GeneIDi11512.
KEGGimmu:11512.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93422 mRNA. Translation: AAA37174.1.
M96653 mRNA. Translation: AAA37182.1.
PIRiA49201.
RefSeqiNP_031431.2. NM_007405.2.
UniGeneiMm.157091.

3D structure databases

ProteinModelPortaliQ01341.
SMRiQ01341. Positions 362-550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000093939.

PTM databases

iPTMnetiQ01341.
PhosphoSiteiQ01341.
SwissPalmiQ01341.

Proteomic databases

MaxQBiQ01341.
PaxDbiQ01341.
PRIDEiQ01341.

Protocols and materials databases

DNASUi11512.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi11512.
KEGGimmu:11512.

Organism-specific databases

CTDi112.
MGIiMGI:87917. Adcy6.

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiQ01341.
KOiK08046.
PhylomeDBiQ01341.

Enzyme and pathway databases

BRENDAi4.6.1.1. 3474.

Miscellaneous databases

ChiTaRSiAdcy6. mouse.
PROiQ01341.
SOURCEiSearch...

Gene expression databases

CleanExiMM_ADCY6.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a Ca(2+)-inhibitable adenylyl cyclase from NCB-20 cells."
    Yoshimura M., Cooper D.M.F.
    Proc. Natl. Acad. Sci. U.S.A. 89:6716-6720(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Lowered responsiveness of the catalyst of adenylyl cyclase to stimulation by GS in heterologous desensitization: a role for adenosine 3',5'-monophosphate-dependent phosphorylation."
    Premont R.T., Jacobowitz O., Iyengar R.
    Endocrinology 131:2774-2784(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-1165.
  3. "Adenylyl cyclase type 6 deletion decreases left ventricular function via impaired calcium handling."
    Tang T., Gao M.H., Lai N.C., Firth A.L., Takahashi T., Guo T., Yuan J.X., Roth D.M., Hammond H.K.
    Circulation 117:61-69(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney and Pancreas.
  5. "Primary cilium-dependent mechanosensing is mediated by adenylyl cyclase 6 and cyclic AMP in bone cells."
    Kwon R.Y., Temiyasathit S., Tummala P., Quah C.C., Jacobs C.R.
    FASEB J. 24:2859-2868(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  6. "Impaired water reabsorption in mice deficient in the type VI adenylyl cyclase (AC6)."
    Chien C.L., Wu Y.S., Lai H.L., Chen Y.H., Jiang S.T., Shih C.M., Lin S.S., Chang C., Chern Y.
    FEBS Lett. 584:2883-2890(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
  7. "Adenylyl cyclase 6 deletion reduces left ventricular hypertrophy, dilation, dysfunction, and fibrosis in pressure-overloaded female mice."
    Tang T., Lai N.C., Hammond H.K., Roth D.M., Yang Y., Guo T., Gao M.H.
    J. Am. Coll. Cardiol. 55:1476-1486(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  8. "Adenylate cyclase 6 determines cAMP formation and aquaporin-2 phosphorylation and trafficking in inner medulla."
    Rieg T., Tang T., Murray F., Schroth J., Insel P.A., Fenton R.A., Hammond H.K., Vallon V.
    J. Am. Soc. Nephrol. 21:2059-2068(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  9. "Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases."
    Choi Y.H., Suzuki A., Hajarnis S., Ma Z., Chapin H.C., Caplan M.J., Pontoglio M., Somlo S., Igarashi P.
    Proc. Natl. Acad. Sci. U.S.A. 108:10679-10684(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AKAP5; ADCY5; PDE4C AND PKD2.
  10. "Adenylyl cyclase 6 mediates the action of cyclic AMP-dependent secretagogues in mouse pancreatic exocrine cells via protein kinase A pathway activation."
    Sabbatini M.E., D'Alecy L., Lentz S.I., Tang T., Williams J.A.
    J. Physiol. (Lond.) 591:3693-3707(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
  11. "Adenylyl cyclase 6 mediates loading-induced bone adaptation in vivo."
    Lee K.L., Hoey D.A., Spasic M., Tang T., Hammond H.K., Jacobs C.R.
    FASEB J. 28:1157-1165(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  12. "Adenylyl cyclase 6 deficiency ameliorates polycystic kidney disease."
    Rees S., Kittikulsuth W., Roos K., Strait K.A., Van Hoek A., Kohan D.E.
    J. Am. Soc. Nephrol. 25:232-237(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  13. "Renal phosphate wasting in the absence of adenylyl cyclase 6."
    Fenton R.A., Murray F., Dominguez Rieg J.A., Tang T., Levi M., Rieg T.
    J. Am. Soc. Nephrol. 25:2822-2834(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  14. "Non-raft adenylyl cyclase 2 defines a cAMP signaling compartment that selectively regulates IL-6 expression in airway smooth muscle cells: differential regulation of gene expression by AC isoforms."
    Bogard A.S., Birg A.V., Ostrom R.S.
    Naunyn Schmiedebergs Arch. Pharmacol. 387:329-339(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.

Entry informationi

Entry nameiADCY6_MOUSE
AccessioniPrimary (citable) accession number: Q01341
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 8, 2016
This is version 148 of the entry and version 1 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.