Adenylate cyclase type 9 - Mus musculus (Mouse)

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P51830 (ADCY9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 118. 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 9
EC=4.6.1.1

Alternative name(s):
ATP pyrophosphate-lyase 9
Adenylate cyclase type IX
Adenylyl cyclase 9
Adenylyl cyclase type 10
Short name=ACTP10

Gene names

Name:

Adcy9

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	1353 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a fundamental role in situations where fine interplay between intracellular calcium and cAMP determines the cellular function. May be a physiologically relevant docking site for calcineurin.
Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Cofactor	Binds 2 magnesium ions per subunit.
Enzyme regulation	Insensitive to calcium/calmodulin. Stimulated by magnesium, forskolin and mutationally activated G protein (GS)-alpha. Regulated by calcineurin.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Found in decreasing order in skeletal muscle, heart, adrenal gland, ovary and brain; and to a lesser extent, in kidney, liver, testis, lung, thymus and spleen.
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	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	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 Traceable author statement Ref.1. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1353

1353

Adenylate cyclase type 9

PRO_0000195709

Regions

Topological domain

1 – 117

117

Cytoplasmic Potential

Transmembrane

118 – 138

Helical; Potential

Topological domain

139 – 141

Extracellular Potential

Transmembrane

142 – 162

Helical; Potential

Topological domain

163 – 171

Cytoplasmic Potential

Transmembrane

172 – 192

Helical; Potential

Topological domain

193 – 215

Extracellular Potential

Transmembrane

216 – 235

Helical; Potential

Topological domain

236 – 241

Cytoplasmic Potential

Transmembrane

242 – 259

Helical; Potential

Topological domain

260 – 280

Extracellular Potential

Transmembrane

281 – 301

Helical; Potential

Topological domain

302 – 786

485

Cytoplasmic Potential

Transmembrane

787 – 807

Helical; Potential

Topological domain

808 – 818

Extracellular Potential

Transmembrane

819 – 839

Helical; Potential

Topological domain

840 – 867

Cytoplasmic Potential

Transmembrane

868 – 888

Helical; Potential

Topological domain

889 – 891

Extracellular Potential

Transmembrane

892 – 912

Helical; Potential

Topological domain

913 – 920

Cytoplasmic Potential

Transmembrane

921 – 941

Helical; Potential

Topological domain

942 – 975

Extracellular Potential

Transmembrane

976 – 996

Helical; Potential

Topological domain

997 – 1353

357

Cytoplasmic Potential

Sites

Metal binding

399

Magnesium 1 By similarity

Metal binding

399

Magnesium 2 By similarity

Metal binding

400

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

443

Magnesium 1 By similarity

Metal binding

443

Magnesium 2 By similarity

Amino acid modifications

Modified residue

608

Phosphothreonine Ref.5

Modified residue

610

Phosphoserine Ref.4 Ref.5

Modified residue

613

Phosphoserine Ref.4 Ref.5

Modified residue

1259

Phosphoserine By similarity

Modified residue

1307

Phosphoserine By similarity

Glycosylation

206

N-linked (GlcNAc...) Potential

Glycosylation

955

N-linked (GlcNAc...) Potential

Glycosylation

964

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

893

H → Q in CAA90570. Ref.2

Sequence conflict

1192

N → D no nucleotide entry Ref.3

Sequence conflict

1305

R → H in CAA90570. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P51830 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C65736A8304F689E
Show »

FASTA

1,353

150,954

        10         20         30         40         50         60 
MASSPHQQLL HHHSTEVSCD SSGDSNSVRV KINPKQLSSN THPKHCKYSI SSSCSSSGDS 

        70         80         90        100        110        120 
GGLPRRVGGG GRLRRQKKLP QLFERASSRW WDPKFDSMNL EEACLERCFP QTQRRFRYAL 

       130        140        150        160        170        180 
FYVGFACLLW SIYFAVHMKS KVIVMVVPAL CFLVVCVGFF LFTFTKLYAR HYAWTSLALT 

       190        200        210        220        230        240 
LLVFALTLAA QFQVWTPLSG RVDSSNHTLT ATPADTCLSQ VGSFSICIEV LLLLYTVMQL 

       250        260        270        280        290        300 
PLYLSLFLGV VYSVLFETFG YHFRNEDCYP SPGPGALHWE LLSRALLHVC IHAIGIHLFV 

       310        320        330        340        350        360 
MSQVRSRSTF LKVGQSIMHG KDLEVEKALK ERMIHSVMPR IIADDLMKQG DEESENSVKR 

       370        380        390        400        410        420 
HATSSPKNRK KKSSIQKAPI AFRPFKMQQI EEVSILFADI VGFTKMSANK SAHALVGLLN 

       430        440        450        460        470        480 
DLFGRFDRLC EQTKCEKIST LGDCYYCVAG CPEPRADHAY CCIEMGLGMI KAIEQFCQEK 

       490        500        510        520        530        540 
KEMVNMRVGV HTGTVLCGIL GMRRFKFDVW SNDVNLANLM EQLGVAGKVH ISEATAKYLD 

       550        560        570        580        590        600 
DRYEMEDGRV IERLGQSVVA DQLKGLKTYL ISGQRAKESH CSCAEALLSG FEVIDDSRES 

       610        620        630        640        650        660 
SGPRGQGTAS PGSVSDLAQT VKTFDNLKTC PSCGITFAPK SEAGAEGGTV QNGCQDEPKT 

       670        680        690        700        710        720 
STKASGGPNS KTQNGLLSPP AEEKLTNSQT SLCEILQEKG RWAGVSLDQS ALLPLRFKNI 

       730        740        750        760        770        780 
REKTDAHFVD VIKEDSLMKD YFFKPPINQF SLNFLDQELE RSYRTSYQEE VIKNSPVKTF 

       790        800        810        820        830        840 
ASATFSSLLD VFLSTTVFLI LSITCFLKYG ATATPPPPAA LAVFGADLLL EVLSLIVSIR 

       850        860        870        880        890        900 
MVFFLEDVMT CTKWLLEWIA GWLPRHCIGA ILVSLPALAV YSHITSEFET NIHVTMFTGS 

       910        920        930        940        950        960 
AVLVAVVHYC NFCQLSSWMR SSLATIVGAG LLLLLHISLC QDSSIVMSPL DSAQNFSAQR 

       970        980        990       1000       1010       1020 
NPCNSSVLQD GRRPASLIGK ELILTFFLLL LLVWFLNREF EVSYRLHYHG DVEADLHRTK 

      1030       1040       1050       1060       1070       1080 
IQSMRDQADW LLRNIIPYHV AEQLKVSQTY SKNHDSGGVI FASIVNFSEF YEENYEGGKE 

      1090       1100       1110       1120       1130       1140 
CYRVLNELIG DFDELLSKPD YNSIEKIKTI GATYMAASGL NTAQCQEGGH PQEHLRILFE 

      1150       1160       1170       1180       1190       1200 
FAKEMMRVVD DFNNNMLWFN FKLRVGFNHG PLTAGVIGTT KLLYDIWGDT VNIASRMDTT 

      1210       1220       1230       1240       1250       1260 
GVECRIQVSE ESYRVLSKMG YDFDYRGTVN VKGKGQMKTY LYPKCTDNGV VPQHQLSISP 

      1270       1280       1290       1300       1310       1320 
DIRVQVDGSI GRSPTDEIAN LVPSVQYSDK ASLGSDDSTQ AKEARLSSKR SWREPVKAEE 

      1330       1340       1350 
RFPFGKAIEK DSCEDIGVEE ASELSKLNVS KSV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of a widely expressed form of adenylyl cyclase." Premont R.T., Matsuoka I., Mattei M.-G., Pouille Y., Defer N., Hanoune J. J. Biol. Chem. 271:13900-13907(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Brain.
[2]	"Control of a novel adenylyl cyclase by calcineurin." Paterson J.M., Smith S.M., Harmar A.J., Antoni F.A. Biochem. Biophys. Res. Commun. 214:1000-1008(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Identification of adenylyl cyclases by amplification using degenerate primers." Premont R.T. Methods Enzymol. 238:116-127(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1106-1193.
[4]	"Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-613, MASS SPECTROMETRY. Tissue: Forebrain.
[5]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-608; SER-610 AND SER-613, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U30602 mRNA. Translation: AAC52603.1. Z50190 mRNA. Translation: CAA90570.1.
IPI	IPI00313750.
PIR	JC4279.
RefSeq	NP_033754.2. NM_009624.2.
UniGene	Mm.439750. Mm.482493.
3D structure databases
ProteinModelPortal	P51830.
SMR	P51830. Positions 380-553, 1050-1241.
ModBase	Search...
PTM databases
PhosphoSite	P51830.
Proteomic databases
PaxDb	P51830.
PRIDE	P51830.
Protocols and materials databases
DNASU	11515.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005719; ENSMUSP00000005719; ENSMUSG00000005580. ENSMUST00000117801; ENSMUSP00000113498; ENSMUSG00000005580.
GeneID	11515.
KEGG	mmu:11515.
UCSC	uc007xzq.1. mouse.
Organism-specific databases
CTD	115.
MGI	MGI:108450. Adcy9.
Phylogenomic databases
eggNOG	COG2114.
GeneTree	ENSGT00700000104101.
HOGENOM	HOG000001574.
HOVERGEN	HBG050459.
InParanoid	P51830.
KO	K08049.
OMA	HMRSKLI.
OrthoDB	EOG4CRKZB.
Gene expression databases
ArrayExpress	P51830.
Bgee	P51830.
CleanEx	MM_ADCY9.
Genevestigator	P51830.
GermOnline	ENSMUSG00000005580. Mus musculus.
Family and domain databases
Gene3D	3.30.70.1230. 2 hits.
InterPro	IPR001054. A/G_cyclase. IPR018297. A/G_cyclase_CS. [Graphical view]
Pfam	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
ChEMBL	CHEMBL2691.
NextBio	278930.
SOURCE	Search...

Entry information

Entry name

ADCY9_MOUSE

Accession

Primary (citable) accession number: P51830
Secondary accession number(s): Q61279

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 118 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

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