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Q01341 (ADCY6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenylate cyclase type 6

EC=4.6.1.1
Alternative name(s):
ATP pyrophosphate-lyase 6
Adenylate cyclase type VI
Adenylyl cyclase 6
Ca(2+)-inhibitable adenylyl cyclase
Gene names
Name:Adcy6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1165 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Membrane-bound, calcium-inhibitable adenylyl cyclase.

Catalytic activity

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

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Enzyme regulation

Inhibition by calcium in the submicromolar concentration range. Phosphorylation by RAF1 results in its activation By similarity.

Subunit structure

Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2. Interacts with RAF1 By similarity. Ref.3

Subcellular location

Membrane; Multi-pass membrane protein. Cell projectioncilium Ref.3.

Tissue specificity

Most abundant in heart but weakly detectable in brain, intestine, lung and spleen.

Post-translational modification

Phosphorylated by RAF1 By similarity.

Sequence similarities

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

Contains 2 guanylate cyclase domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11651165Adenylate cyclase type 6
PRO_0000195700

Regions

Topological domain1 – 149149Cytoplasmic Potential
Transmembrane150 – 16617Helical; Potential
Transmembrane179 – 19517Helical; Potential
Transmembrane212 – 22817Helical; Potential
Transmembrane237 – 25317Helical; Potential
Transmembrane257 – 27317Helical; Potential
Transmembrane287 – 30317Helical; Potential
Topological domain304 – 670367Cytoplasmic Potential
Transmembrane671 – 68818Helical; Potential
Transmembrane699 – 71517Helical; Potential
Transmembrane740 – 75617Helical; Potential
Topological domain757 – 81660Extracellular Potential
Transmembrane817 – 83317Helical; Potential
Transmembrane836 – 85217Helical; Potential
Transmembrane894 – 91017Helical; Potential
Topological domain911 – 1165255Cytoplasmic Potential

Sites

Metal binding3821Magnesium 1 By similarity
Metal binding3821Magnesium 2 By similarity
Metal binding3831Magnesium 2; via carbonyl oxygen By similarity
Metal binding4261Magnesium 1 By similarity
Metal binding4261Magnesium 2 By similarity

Amino acid modifications

Modified residue5531Phosphoserine By similarity
Modified residue5731Phosphoserine By similarity
Modified residue6591Phosphoserine By similarity
Modified residue9161Phosphothreonine By similarity
Glycosylation2771N-linked (GlcNAc...) Potential
Glycosylation7901N-linked (GlcNAc...) Potential
Glycosylation8751N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict471K → N in AAA37182. Ref.2
Sequence conflict761G → A in AAA37182. Ref.2
Sequence conflict508 – 5092GR → RAG in AAA37182. Ref.2
Sequence conflict7371V → G in AAA37182. Ref.2
Sequence conflict8811L → Q in AAA37182. Ref.2
Sequence conflict9901V → M in AAA37182. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q01341 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 24EE1BB45DF1E87E

FASTA1,165130,319
        10         20         30         40         50         60 
MSWFSGLLVP KVDERKTAWG ERNGQKRPRH ANRASGFCAP RYMSCLKNAE PPSPTPAAHT 

        70         80         90        100        110        120 
RCPWQDEAFI RRAGPGRGVE LGLRSVALGF DDTEVTTPMG TAEVAPDTSP RSGPSCWHRL 

       130        140        150        160        170        180 
VQVFQSKQFR SAKLERLYQR YFFQMNQSSL TLLMAVLVLL MAVLLTFHAA PAQPQPAYVA 

       190        200        210        220        230        240 
LLTCASVLFV VLMVVCNRHS FRQDSMWVVS YVVLGILAAV QVGGALAANP HSPSAGLWCP 

       250        260        270        280        290        300 
VFFVYITYTL LPIRMRAAVL SGLGLSTLHL ILAWQLNSSD PFLWKQLGAN VVLFLCTNAI 

       310        320        330        340        350        360 
GVCTHYPAEV SQRQAFQETR GYIQARLHLQ HENRQQERLL LSVLPQHVAM EMKEDINTKK 

       370        380        390        400        410        420 
EDMMFHKIYI QKHDNVSILF ADIEGFTSLA SQCTAQELVM TLNELFARFD KLAAENHCLR 

       430        440        450        460        470        480 
IKILGDCYYC VSGLPEARAD HAHCCVEMGV DMIEAISLVR EVTGVNVNMR VGIHSGRVHC 

       490        500        510        520        530        540 
GVLGLRKWQF DVWSNDVTLA NHMEAGGGRR IHITRATLQY LNGDYEVEPG RGGERNAYLK 

       550        560        570        580        590        600 
EQCIETFLIL GASQKRKEEK AMLAKLQRTR ANSMEGLMPR WVPDRAFSRT KDSKAFRQMG 

       610        620        630        640        650        660 
IDDSSKDNRG AQDALNPEDE VDEFLGRAID ARSIDQLRKD HVRRFLLTFQ REDLEKKYSR 

       670        680        690        700        710        720 
KVDPRFGAYV ACALLVFCFI CFIQLLVFPY STLILGIYAA IFLLLLVTVL ICAVCSCGSF 

       730        740        750        760        770        780 
FPKALQRLSR NIVRSRVHST AVGIFSVLLV FISAIANMFT CNHTPIRTCA ARMLNLTPAD 

       790        800        810        820        830        840 
VTACHLQQLN YSLGLDAPLC EGTAPTCSFP EYFVGNVLLS LLASSVFLHI SSIGKLAMTF 

       850        860        870        880        890        900 
ILGFTYLVLL LLGPPAAIFD NYDLLLGVHG LASSNETFDG LDCPAVGRVA LKYMTPVILL 

       910        920        930        940        950        960 
VFALALYLHA QQVESTARLD FLWKLQATGE KEEMEELQAY NRRLLHNILP KDVAAHFLAR 

       970        980        990       1000       1010       1020 
ERRNDELYYQ SCECVAVMFA SIANFSEFYV ELEANNEGVE CLRLLNEIIA DFDEIISEER 

      1030       1040       1050       1060       1070       1080 
FRQLEKIKTI GSTYMAASGL NASTYDQVGR SHITALADYA MRLMEQMKHI NEHSFNNFQM 

      1090       1100       1110       1120       1130       1140 
KIGLNMGPVV AGVIGARKPQ YDIWGNTVNV SSRMDSTGVP DRIQVTTDLY QVLAAKGYQL 

      1150       1160 
ECRGVVKVKG KGEMTTYFLN GGPSS 

« Hide

References

[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].
[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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93422 mRNA. Translation: AAA37174.1.
M96653 mRNA. Translation: AAA37182.1.
PIRA49201.
RefSeqNP_031431.2. NM_007405.2.
UniGeneMm.157091.

3D structure databases

ProteinModelPortalQ01341.
SMRQ01341. Positions 362-550, 967-1142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000093939.

Chemistry

BindingDBQ01341.

PTM databases

PhosphoSiteQ01341.

Proteomic databases

PaxDbQ01341.
PRIDEQ01341.

Protocols and materials databases

DNASU11512.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID11512.
KEGGmmu:11512.

Organism-specific databases

CTD112.
MGIMGI:87917. Adcy6.

Phylogenomic databases

eggNOGCOG2114.
HOGENOMHOG000006941.
HOVERGENHBG050458.
InParanoidQ01341.
KOK08046.
PhylomeDBQ01341.

Gene expression databases

CleanExMM_ADCY6.
GenevestigatorQ01341.

Family and domain databases

Gene3D3.30.70.1230. 2 hits.
InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR009398. Adenylate_cyclase-like.
[Graphical view]
PfamPF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
SMARTSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMSSF55073. SSF55073. 2 hits.
PROSITEPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSADCY6. mouse.
NextBio278914.
PROQ01341.
SOURCESearch...

Entry information

Entry nameADCY6_MOUSE
AccessionPrimary (citable) accession number: Q01341
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 11, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot