Adenylate cyclase type 6 - Mus musculus (Mouse)

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Q01341 (ADCY6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1165 AA.
Sequence status	Complete.
Protein existence	Evidence 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 projection › cilium 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.

Ontologies

Keywords
Biological process	cAMP biosynthesis
Cellular component	Cell projection Cilium Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of adenylate cyclase activity Traceable author statement Ref.1. Source: MGI intracellular signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cilium Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement Ref.1. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activity Inferred from direct assay PubMed 17593019. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1165

1165

Adenylate cyclase type 6

PRO_0000195700

Regions

Topological domain

1 – 149

149

Cytoplasmic Potential

Transmembrane

150 – 166

Helical; Potential

Transmembrane

179 – 195

Helical; Potential

Transmembrane

212 – 228

Helical; Potential

Transmembrane

237 – 253

Helical; Potential

Transmembrane

257 – 273

Helical; Potential

Transmembrane

287 – 303

Helical; Potential

Topological domain

304 – 670

367

Cytoplasmic Potential

Transmembrane

671 – 688

Helical; Potential

Transmembrane

699 – 715

Helical; Potential

Transmembrane

740 – 756

Helical; Potential

Topological domain

757 – 816

Extracellular Potential

Transmembrane

817 – 833

Helical; Potential

Transmembrane

836 – 852

Helical; Potential

Transmembrane

894 – 910

Helical; Potential

Topological domain

911 – 1165

255

Cytoplasmic Potential

Sites

Metal binding

382

Magnesium 1 By similarity

Metal binding

382

Magnesium 2 By similarity

Metal binding

383

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

426

Magnesium 1 By similarity

Metal binding

426

Magnesium 2 By similarity

Amino acid modifications

Modified residue

553

Phosphoserine By similarity

Modified residue

573

Phosphoserine By similarity

Modified residue

659

Phosphoserine By similarity

Modified residue

916

Phosphothreonine By similarity

Glycosylation

277

N-linked (GlcNAc...) Potential

Glycosylation

790

N-linked (GlcNAc...) Potential

Glycosylation

875

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

K → N in AAA37182. Ref.2

Sequence conflict

G → A in AAA37182. Ref.2

Sequence conflict

508 – 509

GR → RAG in AAA37182. Ref.2

Sequence conflict

737

V → G in AAA37182. Ref.2

Sequence conflict

881

L → Q in AAA37182. Ref.2

Sequence conflict

990

V → M in AAA37182. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q01341 [UniParc].

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

1,165

130,319

        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

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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.
IPI	IPI00122297.
PIR	A49201.
RefSeq	NP_031431.2. NM_007405.2.
UniGene	Mm.157091.
3D structure databases
ProteinModelPortal	Q01341.
SMR	Q01341. Positions 362-550, 967-1142.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000093939.
PTM databases
PhosphoSite	Q01341.
Proteomic databases
PaxDb	Q01341.
PRIDE	Q01341.
Protocols and materials databases
DNASU	11512.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	11512.
KEGG	mmu:11512.
UCSC	uc007xmz.1. mouse.
Organism-specific databases
CTD	112.
MGI	MGI:87917. Adcy6.
Phylogenomic databases
eggNOG	COG2114.
HOGENOM	HOG000006941.
HOVERGEN	HBG050458.
InParanoid	Q01341.
KO	K08046.
OrthoDB	EOG4255S0.
Gene expression databases
CleanEx	MM_ADCY6.
Genevestigator	Q01341.
GermOnline	ENSMUSG00000022994. Mus musculus.
Family and domain databases
Gene3D	3.30.70.1230. 2 hits.
InterPro	IPR001054. A/G_cyclase. IPR018297. A/G_cyclase_CS. IPR009398. Adenylate_cyclase-like. [Graphical view]
Pfam	PF06327. DUF1053. 1 hit. PF00211. Guanylate_cyc. 2 hits. [Graphical view]
SMART	SM00044. CYCc. 2 hits. [Graphical view]
SUPFAM	SSF55073. A/G_cyclase. 2 hits.
PROSITE	PS00452. GUANYLATE_CYCLASE_1. 2 hits. PS50125. GUANYLATE_CYCLASE_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q01341.
ChEMBL	CHEMBL3015.
ChiTaRS	ADCY6. mouse.
NextBio	278914.
SOURCE	Search...

Entry information

Entry name

ADCY6_MOUSE

Accession

Primary (citable) accession number: Q01341

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents