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UniProtKB/Swiss-Prot entry P30803


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADCY5_CANFA
Primary accession number P30803
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 88)
Name and origin of the protein
Protein name Adenylate cyclase type 5
Synonyms EC 4.6.1.1
Adenylate cyclase type V
ATP pyrophosphate-lyase 5
Adenylyl cyclase 5
Ca(2+)-inhibitable adenylyl cyclase
Gene name
Name: ADCY5
From
Canis familiaris (Dog) [TaxID: 9615] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart muscle;
PubMed=1618857 [NCBI, ExPASy, EBI, Israel, Japan]
Ishikawa Y., Katsushika S., Chen L., Halnon N.J., Kawabe J., Homcy C.J.;
"Isolation and characterization of a novel cardiac adenylylcyclase cDNA.";
J. Biol. Chem. 267:13553-13557(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Heart muscle;
PubMed=8428899 [NCBI, ExPASy, EBI, Israel, Japan]
Katsushika S., Kawabe J., Homcy C.J., Ishikawa Y.;
"In vivo generation of an adenylylcyclase isoform with a half-molecule motif.";
J. Biol. Chem. 268:2273-2276(1993).
[3]
SEQUENCE REVISION TO N-TERMINUS.
Tomlinson J., Okumura S., Ishikawa Y.;
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[4]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 445-661 OF COMPLEX WITH G(S)-ALPHA.
DOI=10.1126/science.278.5345.1907; PubMed=9417641 [NCBI, ExPASy, EBI, Israel, Japan]
Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.;
"Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS.";
Science 278:1907-1916(1997).
[5]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 445-661 OF COMPLEX WITH G(S)-ALPHA.
DOI=10.1126/science.285.5428.756; PubMed=10427002 [NCBI, ExPASy, EBI, Israel, Japan]
Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R.;
"Two-metal-ion catalysis in adenylyl cyclase.";
Science 285:756-760(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M88649; AAC32726.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M97886; AAA30827.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A42904; A42904.
A45195; A45195.
UniGene Cfa.1267
3D structure databases
PDB
1AZS; X-ray; 2.30 A; A=442-656.[ExPASy / RCSB / EBI]
1CJK; X-ray; 3.00 A; A=445-661.[ExPASy / RCSB / EBI]
1CJT; X-ray; 2.80 A; A=445-661.[ExPASy / RCSB / EBI]
1CJU; X-ray; 2.80 A; A=445-661.[ExPASy / RCSB / EBI]
1CJV; X-ray; 3.00 A; A=445-661.[ExPASy / RCSB / EBI]
1CS4; X-ray; 2.50 A; A=442-661.[ExPASy / RCSB / EBI]
1CUL; X-ray; 2.40 A; A=445-661.[ExPASy / RCSB / EBI]
1TL7; X-ray; 2.80 A; A=445-661.[ExPASy / RCSB / EBI]
1U0H; X-ray; 2.90 A; A=442-661.[ExPASy / RCSB / EBI]
2GVD; X-ray; 2.90 A; A=442-661.[ExPASy / RCSB / EBI]
2GVZ; X-ray; 3.27 A; A=442-661.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AZS; -.
1CJK; -.
1CJT; -.
1CJU; -.
1CJV; -.
1CS4; -.
1CUL; -.
1TL7; -.
1U0H; -.
2GVD; -.
2GVZ; -.
ModBase P30803.
Protein-protein interaction databases
DIP DIP:179N; -.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0004016; Molecular function: adenylate cyclase activity (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006171; Biological process: cAMP biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0007242; Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001054; A/G_cyclase.
IPR009398; Aden_cycl_like.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.1230; A/G_cyclase; 2.
Pfam PF06327; DUF1053; 1.
PF00211; Guanylate_cyc; 2.
Pfam graphical view of domain structure.
SMART SM00044; CYCc; 2.
SMART graphical view of domain structure.
PROSITE PS00452; GUANYLATE_CYCLASE_1; 2.
PS50125; GUANYLATE_CYCLASE_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P30803.
ProtoNet P30803.
Genome annotation databases
Ensembl ENSCAFG00000012084; Canis familiaris. [Contig view]
Phylogenomic databases
HOVERGEN P30803; -.
Other
LinkHub P30803; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; cAMP biosynthesis; Glycoprotein; Lyase; Magnesium; Membrane; Metal-binding; Phosphoprotein; Repeat; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1265  1265     Adenylate cyclase type 5. PRO_0000195693
TOPO_DOM   1    244  244     Cytoplasmic (Potential). 
TRANSMEM   245    265  21     Potential. 
TRANSMEM   271    291  21     Potential. 
TRANSMEM   302    322  21     Potential. 
TRANSMEM   328    348  21     Potential. 
TRANSMEM   352    372  21     Potential. 
TRANSMEM   377    397  21     Potential. 
TOPO_DOM   398    765  368     Cytoplasmic (Potential). 
TRANSMEM   766    786  21     Potential. 
TRANSMEM   792    812  21     Potential. 
TRANSMEM   839    859  21     Potential. 
TRANSMEM   908    928  21     Potential. 
TRANSMEM   930    950  21     Potential. 
TRANSMEM   988   1008  21     Potential. 
TOPO_DOM   1009   1265  257     Cytoplasmic (Potential). 
DOMAIN   472    599  128     Guanylate cyclase 1. 
DOMAIN   1075   1214  140     Guanylate cyclase 2. 
METAL   477    477        Magnesium 1. 
METAL   477    477        Magnesium 2. 
METAL   478    478        Magnesium 2; via carbonyl oxygen. 
METAL   521    521        Magnesium 1. 
METAL   521    521        Magnesium 2. 
MOD_RES   8      8        Phosphoserine (By similarity). 
CARBOHYD   873    873        N-linked (GlcNAc...) (Potential). 
CARBOHYD   890    890        N-linked (GlcNAc...) (Potential). 
CARBOHYD   976    976        N-linked (GlcNAc...) (Potential). 
VAR_SEQ   653    677        KEEKAMIAKMNRQRTNSIGHNPPHW -> VRRGGGGPRPGGADSPGWWGASAGP (in isoform 2). VSP_000242
VAR_SEQ   678   1265        Missing (in isoform 2). VSP_000243
STRAND   464    479  16      
HELIX   481    487  7      
HELIX   490    511  22      
STRAND   514    519  6      
STRAND   522    527  6      
HELIX   536    558  23      
STRAND   563    577  15      
STRAND   579    582  4      
STRAND   586    589  4      
HELIX   590    600  11      
STRAND   606    609  4      
TURN   612    619  8      
STRAND   623    625  3      
HELIX   628    630  3      
HELIX   633    637  5      
STRAND   643    645  3      
Sequence information
Length: 1265 AA [This is the length of the unprocessed precursor] Molecular weight: 140319 Da [This is the MW of the unprocessed precursor] CRC64: 414322F64153DFB4 [This is a checksum on the sequence]
        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 

P30803 in FASTA format

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