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Reviewed, UniProtKB/Swiss-Prot P30803 (ADCY5_CANFA)

Last modified February 9, 2010. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Adenylate cyclase type 5
    EC=4.6.1.1
Alternative name(s):
    Adenylate cyclase type V
    ATP pyrophosphate-lyase 5
    Adenylyl cyclase 5
    Ca(2+)-inhibitable adenylyl cyclase
Gene names
Name: ADCY5
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

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Protein attributes

Sequence length1265 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

This is a membrane-bound, calcium-inhibitable adenylyl cyclase.

Catalytic activity

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

Cofactor

Binds 2 magnesium ions per subunit.

Enzyme regulation

The activity was inhibited in a concentration-dependent manner with either P-site active agents such as adenosine or in the presence of calcium.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Most abundant in heart but weakly detectable in brain.

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
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLyase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
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

plasma membrane

Inferred from Experiment. Source: Reactome

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate cyclase activity

Inferred from Experiment. Source: Reactome

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30803-1)

Also known as: V;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P30803-2)

Also known as: V-alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     653-677: KEEKAMIAKMNRQRTNSIGHNPPHW → VRRGGGGPRPGGADSPGWWGASAGP
     678-1265: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12651265Adenylate cyclase type 5
PRO_0000195693

Regions

Topological domain1 – 244244Cytoplasmic Potential
Transmembrane245 – 26521 Potential
Transmembrane271 – 29121 Potential
Transmembrane302 – 32221 Potential
Transmembrane328 – 34821 Potential
Transmembrane352 – 37221 Potential
Transmembrane377 – 39721 Potential
Topological domain398 – 765368Cytoplasmic Potential
Transmembrane766 – 78621 Potential
Transmembrane792 – 81221 Potential
Transmembrane839 – 85921 Potential
Transmembrane908 – 92821 Potential
Transmembrane930 – 95021 Potential
Transmembrane988 – 100821 Potential
Topological domain1009 – 1265257Cytoplasmic Potential
Domain472 – 599128Guanylate cyclase 1
Domain1075 – 1214140Guanylate cyclase 2

Sites

Metal binding4771Magnesium 1
Metal binding4771Magnesium 2
Metal binding4781Magnesium 2; via carbonyl oxygen
Metal binding5211Magnesium 1
Metal binding5211Magnesium 2

Amino acid modifications

Modified residue81Phosphoserine By similarity
Glycosylation8731N-linked (GlcNAc...) Potential
Glycosylation8901N-linked (GlcNAc...) Potential
Glycosylation9761N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence653 – 67725KEEKA…NPPHW → VRRGGGGPRPGGADSPGWWG ASAGP in isoform 2.
VSP_000242
Alternative sequence678 – 1265588Missing in isoform 2.
VSP_000243

Secondary structure

1 ................................ 1265
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (V) [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 414322F64153DFB4

FASTA1,265140,319
        10         20         30         40         50         60 
MSGPRSASPP GCAATRGGPE HRAAWGEAEA RANGHPHAAG GATRGCSKKP GGAVTPQLQQ 

        70         80         90        100        110        120 
QQQQQQHEQQ HEQQQHEQQQ HVQQQQRLAK RWRGDDDPPL GGDDPLAGGF GFSFRSRSAW 

       130        140        150        160        170        180 
QERGGDDCGR GSRRRRRGAA GGGSSRAPPA GGGGGPAAAG GAEVRPRSVE LGLDERRGRG 

       190        200        210        220        230        240 
RAEPEPEAEA GAPGGDRGAR DGDGPAGPGA CCRALLQIFR SKKFPSDKLE RLYQRYFFRL 

       250        260        270        280        290        300 
NQSSLTMLMA VLVLVCLVML AFHAARPPLR LPHLAVLAAA VGVILVMAVL CNRAAFHQDH 

       310        320        330        340        350        360 
MGLACYALIA VVLAVQVVGL LLPQPRSASE GIWWTVFFIY TIYTLLPVRM RAAVLSGVLL 

       370        380        390        400        410        420 
SALHLAIALR ANAQDRFLLK QLVSNVLIFS CTNIVGVCTH YPAEVSQRQA FQETRECIQA 

       430        440        450        460        470        480 
RLHSQRENQQ QERLLLSVLP RHVAMEMKAD INAKQEDMMF HKIYIQKHDN VSILFADIEG 

       490        500        510        520        530        540 
FTSLASQCTA QELVMTLNEL FARFDKLAAE NHCLRIKILG DCYYCVSGLP EARADHAHCC 

       550        560        570        580        590        600 
VEMGMDMIEA ISLVREVTGV NVNMRVGIHS GRVHCGVLGL RKWQFDVWSN DVTLANHMEA 

       610        620        630        640        650        660 
GGKAGRIHIT KATLSYLNGD YEVEPGCGGE RNAYLKEHSI ETFLILRCTQ KRKEEKAMIA 

       670        680        690        700        710        720 
KMNRQRTNSI GHNPPHWGAE RPFYNHLGGN QVSKEMKRMG FEDPKDKNAQ ESANPEDEVD 

       730        740        750        760        770        780 
EFLGRAIDAR SIDRLRSEHV RKFLLTFREP DLEKKYSKQV DDRFGAYVAC ASLVFLFICF 

       790        800        810        820        830        840 
VQITIVPHSV FMLSFYLTCF LLLTLVVFVS VIYSCVKLFP GPLQSLSRKI VRSKTNSTLV 

       850        860        870        880        890        900 
GVFTITLVFL SAFVNMFMCN SEDLLGCLAD EHNISTSRVN ACHVAASAAN LSLGDEQGFC 

       910        920        930        940        950        960 
GTPWPSCNFP EYFTYSVLLS LLACSVFLQI SCIGKLVLML AIELIYVLVV EVPRVTLFDN 

       970        980        990       1000       1010       1020 
ADLLVTANAI DFNNNNGTSQ CPEHATKVAL KVVTPIIISV FVLALYLHAQ QVESTARLDF 

      1030       1040       1050       1060       1070       1080 
LWKLQATEEK EEMEELQAYN RRLLHNILPK DVAAHFLARE RRNDELYYQS CECVAVMFAS 

      1090       1100       1110       1120       1130       1140 
IANFSEFYVE LEANNEGVEC LRVLNEIIAD FDEIISEDRF RQLEKIKTIG STYMAASGLN 

      1150       1160       1170       1180       1190       1200 
DSTYDKVGKT HIKALADFAM KLMDQMKYIN EHSFNNFQMK IGLNIGPVVA GVIGARKPQY 

      1210       1220       1230       1240       1250       1260 
DIWGNTVNVA SRMDSTGVPD RIQVTTDMYQ VLAANTYQLE CRGVVKVKGK GEMMTYFLNG 


GPPLS

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Isoform 2 (V-alpha).

Checksum: AAB94BCFEBE08CC0
Show »

FASTA67773,690

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References

[1]"Isolation and characterization of a novel cardiac adenylylcyclase cDNA."
Ishikawa Y., Katsushika S., Chen L., Halnon N.J., Kawabe J., Homcy C.J.
J. Biol. Chem. 267:13553-13557(1992) [PubMed: 1618857] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart muscle.
[2]"In vivo generation of an adenylylcyclase isoform with a half-molecule motif."
Katsushika S., Kawabe J., Homcy C.J., Ishikawa Y.
J. Biol. Chem. 268:2273-2276(1993) [PubMed: 8428899] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Heart muscle.
[3]Tomlinson J., Okumura S., Ishikawa Y.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO N-TERMINUS.
[4]"Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS."
Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.
Science 278:1907-1916(1997) [PubMed: 9417641] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 445-661 OF COMPLEX WITH G(S)-ALPHA.
[5]"Two-metal-ion catalysis in adenylyl cyclase."
Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R.
Science 285:756-760(1999) [PubMed: 10427002] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 445-661 OF COMPLEX WITH G(S)-ALPHA.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M88649 mRNA. Translation: AAC32726.1.
M97886 mRNA. Translation: AAA30827.1. Sequence problems.
PIRA42904.
A45195.
RefSeqNP_001161932.1.
UniGeneCfa.1267

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZSX-ray2.30A444-656[»]
1CJKX-ray3.00A445-661[»]
1CJTX-ray2.80A445-661[»]
1CJUX-ray2.80A445-661[»]
1CJVX-ray3.00A445-661[»]
1CS4X-ray2.50A444-661[»]
1CULX-ray2.40A445-661[»]
1TL7X-ray2.80A445-661[»]
1U0HX-ray2.90A444-661[»]
2GVDX-ray2.90A444-661[»]
2GVZX-ray3.27A444-661[»]
3C14X-ray2.68A444-661[»]
3C15X-ray2.78A444-661[»]
3C16X-ray2.87A444-661[»]
3E8AX-ray3.00A444-661[»]
SMRP30803. Positions 1066-1241.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-179N.
STRINGP30803.

Genome annotation databases

EnsemblENSCAFT00000019177; ENSCAFP00000017783; ENSCAFG00000012084; Canis familiaris. [Genome view]
GeneID403859.

Phylogenomic databases

eggNOGmaNOG14087.
HOVERGENP30803.
InParanoidP30803.

Enzyme and pathway databases

BRENDA4.6.1.1. 463.

Family and domain databases

InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR009398. Aden_cycl-like.
[Graphical view]
Gene3DG3DSA:3.30.70.1230. A/G_cyclase. 2 hits.
PfamPF06327. DUF1053. 1 hit.
PF00211. 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 nameADCY5_CANFA
AccessionPrimary (citable) accession number: P30803
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 30, 2000
Last modified: February 9, 2010
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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