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Reviewed, UniProtKB/Swiss-Prot Q9DGG6 (ADCY9_CHICK)

Last modified October 13, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Adenylate cyclase type 9
    EC=4.6.1.1
Alternative name(s):
    Adenylate cyclase type IX
    ATP pyrophosphate-lyase 9
    Adenylyl cyclase 9
Gene names
Name: ADCY9
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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Protein attributes

Sequence length1334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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 By similarity.

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 By similarity.

Subcellular location

Membrane; Multi-pass membrane protein By similarity.

Sequence similarities

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

Contains 2 guanylate cyclase domains.

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Ontologies

Keywords
   Biological processcAMP biosynthesis
   Cellular componentMembrane
   DomainRepeat
Transmembrane
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLyase
   PTMGlycoprotein
Phosphoprotein
Gene Ontology (GO)
   Biological processcAMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signaling cascade

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate cyclase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13341334Adenylate cyclase type 9
PRO_0000195710

Regions

Topological domain1 – 113113Cytoplasmic Potential
Transmembrane114 – 13421 Potential
Topological domain135 – 1373Extracellular Potential
Transmembrane138 – 15821 Potential
Topological domain159 – 1679Cytoplasmic Potential
Transmembrane168 – 18720 Potential
Topological domain188 – 20720Extracellular Potential
Transmembrane208 – 22720 Potential
Topological domain228 – 2336Cytoplasmic Potential
Transmembrane234 – 25017 Potential
Topological domain251 – 26919Extracellular Potential
Transmembrane270 – 29021 Potential
Topological domain291 – 768478Cytoplasmic Potential
Transmembrane769 – 78921 Potential
Topological domain790 – 80011Extracellular Potential
Transmembrane801 – 82121 Potential
Topological domain822 – 84928Cytoplasmic Potential
Transmembrane850 – 87021 Potential
Topological domain871 – 8733Extracellular Potential
Transmembrane874 – 89421 Potential
Topological domain895 – 9028Cytoplasmic Potential
Transmembrane903 – 92321 Potential
Topological domain924 – 95734Extracellular Potential
Transmembrane958 – 97821 Potential
Topological domain979 – 1334356Cytoplasmic Potential
Compositional bias59 – 6810Poly-Gly

Sites

Metal binding3881Magnesium 1 By similarity
Metal binding3881Magnesium 2 By similarity
Metal binding3891Magnesium 2; via carbonyl oxygen By similarity
Metal binding4321Magnesium 1 By similarity
Metal binding4321Magnesium 2 By similarity

Amino acid modifications

Glycosylation9371N-linked (GlcNAc...) Potential
Glycosylation9461N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9DGG6-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F05594AADE1CC403

FASTA1,334149,292
        10         20         30         40         50         60 
MASPPHQQLL HHHSTEVSCD SSGDSNSVTV RINPRQQQAL SAKRCKYSIS SSCSSGESGG 

        70         80         90        100        110        120 
VGRGGGGGLR RQKKLPQLFE RASSRWWDPK FDSTNLEEAS MERCFPQTQR RFRYALFYIG 

       130        140        150        160        170        180 
SACLLWGIYF GVHMREKQMV FMVPALCFLL VCVAFFAFTF TKAYARRYVW TSGYTLLVFA 

       190        200        210        220        230        240 
LTLAPQFQPW TLGERQRVQP RPAAPVDTCL SQVGSFSMCV EVLLLLYTVM HLPLYLSLFL 

       250        260        270        280        290        300 
GLSYSVLFET SAFRDESCTL LGGGAVYWEL LSKAFLHVCI HAIGIHLFIM SEVRSRSTFL 

       310        320        330        340        350        360 
KVGQSIMHGK DLEVEKALKE RMIHSVMPRI IADDLMKQGD DESENSVKRH STSSPKNRKK 

       370        380        390        400        410        420 
KPSIQKTPII FRPFKMQQIE QVSILFADIV GFTKMSANKS AHALVGLLND LFGRFDRLCE 

       430        440        450        460        470        480 
DTKCEKISTL GDCYYCVAGC PEPRADHAYC CIEMGLGMIK AIEQFCQEKK EMVNMRVGVH 

       490        500        510        520        530        540 
TGTVLCGILG MRRFKFDVWS NDVNLANLME QLGVAGKVHI SEATAKYLDD RYEMEDGKVT 

       550        560        570        580        590        600 
ERVGQSAVAD QLKGLKTYLI SGQKVKEPHC SCSQALLQLG GWGWSQMQAA PSAENTADST 

       610        620        630        640        650        660 
KALKHVEKPK PCPSCSTTLV PPCDVSIDEG AIQNGCQDEH KNSTKAPGGH SPKTQNGLLS 

       670        680        690        700        710        720 
PPQEEKLSNS QTSLYEMLQE KGRWGGVSLD QSALLPLRFK NIREKTDAHF VDVIKEDSLM 

       730        740        750        760        770        780 
KDYFFKPPIS KLSLNFLDQD LEMAYRTSYQ EEVMRNAPVK TFASATFSSL LDVFLSTTVF 

       790        800        810        820        830        840 
LILSVTCFLK HGMVASPPPP AAVVVFVIAI LLEVLSLVIS VRMVFFLEEV MACTKRLLEL 

       850        860        870        880        890        900 
ISGWLPRHFL GAILVSLPAL AVFSHFTSDF ETNIHYTMFM CCAILIAIVQ YCNFCQLSSW 

       910        920        930        940        950        960 
MRSLLATVVG AVLLILLYVS LCPDSSVETL HLDLAQNLSS RKSPCNSSMP ADVKRPADLI 

       970        980        990       1000       1010       1020 
GQEVILAVFL LLLLVWFLNR SFEVSYRLHY HGDVEADLHR TKIQSMRDQP DSCVRNIIPY 

      1030       1040       1050       1060       1070       1080 
HVADELKVSQ SYSKNHDSGG VIFASIVNFS EFYEENYEGG KECYRVLNEL IGDFDELLSK 

      1090       1100       1110       1120       1130       1140 
PHYSSIEKIK TIGATYMAAS GLNTSQCQDS NHPHGHLQTL FEFAKEMMRV VDDFNNNMLW 

      1150       1160       1170       1180       1190       1200 
FNFKLRIGFN HGPLTAGVIG TTKLLYDIWG DTVNIASRMD TIGVECRIQV SEETYRILSK 

      1210       1220       1230       1240       1250       1260 
MGYDFDYRGT VNVKGKGQMK TYLYPKCMDN GIVPHHQLSI SPDIRVQVDG SIGRSPTDEI 

      1270       1280       1290       1300       1310       1320 
ANLVPSVQNS DKTAHATDNS ETKDALPSSK KLQKEPTKAE ERCRFGKAVE KTDCEEAGTE 

      1330 
EVNELTKLNV SKSV

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References

[1]"Cell-specific properties of type V and type IX adenylyl cyclase isozymes in 293T cells and embryonic chick ventricular myocytes."
Cui H., Green R.D.
Biochem. Biophys. Res. Commun. 283:107-112(2001) [PubMed: 11322775] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.

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Cross-references

Sequence databases

AJ401469 mRNA. Translation: CAC04147.1.
IPIIPI00576467.
RefSeqNP_989961.1.
UniGeneGga.1773

3D structure databases

HSSPHSSP built from PDB template 1CUL based on UniProtKB P26769.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9DGG6.

Genome annotation databases

EnsemblENSGALT00000012620; ENSGALP00000012606; ENSGALG00000007779; Gallus gallus. [Genome view]
GeneID395339.
KEGGgga:395339.

Organism-specific databases

CTD395339.

Phylogenomic databases

HOGENOMQ9DGG6.
HOVERGENQ9DGG6.

Enzyme and pathway databases

BRENDA4.6.1.1. 4.

Family and domain databases

InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
[Graphical view]
Gene3DG3DSA:3.30.70.1230. A/G_cyclase. 2 hits.
PfamPF00211. Guanylate_cyc. 2 hits.
[Graphical view]
SMARTSM00044. CYCc. 2 hits.
[Graphical view]
PROSITEPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameADCY9_CHICK
AccessionPrimary (citable) accession number: Q9DGG6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2001
Last modified: October 13, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents