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Adenylate cyclase type 5 (EC 4.6.1.1) (ATP pyrophosphate-lyase 5) (Adenylate cyclase type V) (Adenylyl cyclase 5) (Ca(2 )-inhibitable adenylyl cyclase)

 ADCY5_CANLF             Reviewed;        1265 AA.
P30803;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
23-MAY-2018, entry version 161.
RecName: Full=Adenylate cyclase type 5;
EC=4.6.1.1 {ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:1618857, ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:8428899};
AltName: Full=ATP pyrophosphate-lyase 5;
AltName: Full=Adenylate cyclase type V;
AltName: Full=Adenylyl cyclase 5;
AltName: Full=Ca(2+)-inhibitable adenylyl cyclase;
Name=ADCY5;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, ENZYME REGULATION, AND TISSUE SPECIFICITY.
TISSUE=Heart muscle;
PubMed=1618857;
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), FUNCTION, CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, ENZYME REGULATION, DOMAIN, AND TISSUE
SPECIFICITY.
TISSUE=Heart muscle;
PubMed=8428899;
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 CHIMERA WITH ADCY5
IN COMPLEX WITH GNAS, INTERACTION WITH GNAS, AND DOMAIN.
PubMed=9417641; DOI=10.1126/science.278.5345.1907;
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 CHIMERA WITH ADCY5
IN COMPLEX WITH ATP ANALOGS; MAGNESIUM; MANGANESE AND GNAS,
INTERACTION WITH GNAS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR,
MUTAGENESIS OF ASP-477 AND ASP-521, AND DOMAIN.
PubMed=10427002; DOI=10.1126/science.285.5428.756;
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).
[6] {ECO:0000244|PDB:1CS4, ECO:0000244|PDB:1CUL}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 445-661 OF CHIMERA WITH
ADCY5 IN COMPLEX WITH GNAS; ATP ANALOG AND MAGNESIUM, CATALYTIC
ACTIVITY, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, INTERACTION WITH
GNAS, AND DOMAIN.
PubMed=11087399; DOI=10.1021/bi0015562;
Tesmer J.J., Dessauer C.W., Sunahara R.K., Murray L.D., Johnson R.A.,
Gilman A.G., Sprang S.R.;
"Molecular basis for P-site inhibition of adenylyl cyclase.";
Biochemistry 39:14464-14471(2000).
[7] {ECO:0000244|PDB:1TL7, ECO:0000244|PDB:1U0H}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 445-661 OF CHIMERA WITH
ADCY5 IN COMPLEX WITH GNAS; MAGNESIUM AND MANGANESE, FUNCTION,
CATALYTIC ACTIVITY, INTERACTION WITH GNAS, AND DOMAIN.
PubMed=15591060; DOI=10.1074/jbc.M409076200;
Mou T.C., Gille A., Fancy D.A., Seifert R., Sprang S.R.;
"Structural basis for the inhibition of mammalian membrane adenylyl
cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-
triphosphate.";
J. Biol. Chem. 280:7253-7261(2005).
[8] {ECO:0000244|PDB:2GVD, ECO:0000244|PDB:2GVZ}
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 444-661 OF CHIMERA WITH
ADCY5 IN COMPLEX WITH GNAS; MANGANESE AND ATP ANALOG, FUNCTION,
CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GNAS, AND DOMAIN.
PubMed=16766715; DOI=10.1124/mol.106.026427;
Mou T.C., Gille A., Suryanarayana S., Richter M., Seifert R.,
Sprang S.R.;
"Broad specificity of mammalian adenylyl cyclase for interaction with
2',3'-substituted purine- and pyrimidine nucleotide inhibitors.";
Mol. Pharmacol. 70:878-886(2006).
[9] {ECO:0000244|PDB:3C14, ECO:0000244|PDB:3C15, ECO:0000244|PDB:3C16, ECO:0000244|PDB:3MAA}
X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 444-661 OF CHIMERA WITH
ADCY5 IN COMPLEX WITH GNAS; ATP AND MAGNESIUM, FUNCTION, CATALYTIC
ACTIVITY, COFACTOR, INTERACTION WITH GNAS, AND DOMAIN.
PubMed=19243146; DOI=10.1021/bi802122k;
Mou T.C., Masada N., Cooper D.M., Sprang S.R.;
"Structural basis for inhibition of mammalian adenylyl cyclase by
calcium.";
Biochemistry 48:3387-3397(2009).
-!- FUNCTION: Isoform 1: Catalyzes the formation of the signaling
molecule cAMP in response to G-protein signaling (PubMed:1618857,
PubMed:8428899, PubMed:10427002, PubMed:11087399, PubMed:15591060,
PubMed:16766715, PubMed:19243146). Mediates signaling downstream
of ADRB1. Regulates the increase of free cytosolic Ca(2+) in
response to increased blood glucose levels and contributes to the
regulation of Ca(2+)-dependent insulin secretion (By similarity).
{ECO:0000250|UniProtKB:O95622, ECO:0000269|PubMed:10427002,
ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060,
ECO:0000269|PubMed:1618857, ECO:0000269|PubMed:16766715,
ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:8428899}.
-!- FUNCTION: Isoform 2: Lacks catalytic activity by itself, but can
associate with isoform 1 to form active adenylyl cyclase.
{ECO:0000269|PubMed:8428899}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
{ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399,
ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:1618857,
ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146,
ECO:0000269|PubMed:8428899}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11087399,
ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:11087399,
ECO:0000269|PubMed:16766715};
Note=Binds 2 magnesium ions per subunit (PubMed:16766715,
PubMed:19243146). Is also active with manganese (in vitro)
(PubMed:11087399, PubMed:16766715). {ECO:0000269|PubMed:10427002,
ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:16766715,
ECO:0000305|PubMed:19243146};
-!- ENZYME REGULATION: Activated by forskolin (PubMed:1618857,
PubMed:8428899). Activated by GNAS. Activity is further increased
by interaction with the G-protein beta and gamma subunit complex
formed by GNB1 and GNG2 (By similarity). Is not activated by
calmodulin. Inhibited by adenosine and ATP analogs. Inhibited by
calcium ions, already at micromolar concentrations
(PubMed:1618857). Phosphorylation by RAF1 results in its
activation (By similarity). {ECO:0000250|UniProtKB:O95622,
ECO:0000269|PubMed:1618857, ECO:0000269|PubMed:8428899}.
-!- SUBUNIT: Interacts with GNAS (PubMed:9417641, PubMed:10427002,
PubMed:11087399, PubMed:15591060, PubMed:16766715,
PubMed:19243146). Interacts with GNB1 and GNG2 (By similarity).
Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2 (By
similarity). Interacts with RAF1 (By similarity).
{ECO:0000250|UniProtKB:O95622, ECO:0000250|UniProtKB:P84309,
ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399,
ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:16766715,
ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9417641}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1618857,
ECO:0000269|PubMed:8428899}; Multi-pass membrane protein
{ECO:0000305}. Cell projection, cilium
{ECO:0000250|UniProtKB:P84309}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=V;
IsoId=P30803-1; Sequence=Displayed;
Name=2; Synonyms=V-alpha;
IsoId=P30803-2; Sequence=VSP_000242, VSP_000243;
-!- TISSUE SPECIFICITY: Isoform 1 is detected in heart, and at lower
levels in brain (PubMed:1618857). Isoform 2 is detected in heart
(PubMed:8428899). {ECO:0000269|PubMed:1618857,
ECO:0000269|PubMed:8428899}.
-!- DOMAIN: The protein contains two modules with six transmembrane
helices each; both are required for catalytic activity. Isolated
N-terminal or C-terminal guanylate cyclase domains have no
catalytic activity, but when they are brought together, enzyme
activity is restored. The active site is at the interface of the
two domains. Both contribute substrate-binding residues, but the
catalytic metal ions are bound exclusively via the N-terminal
guanylate cyclase domain. {ECO:0000269|PubMed:10427002,
ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060,
ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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EMBL; M88649; AAC32726.1; -; mRNA.
EMBL; M97886; AAA30827.1; ALT_SEQ; mRNA.
PIR; A42904; A42904.
PIR; A45195; A45195.
RefSeq; NP_001161932.1; NM_001168460.1. [P30803-1]
UniGene; Cfa.1267; -.
PDB; 1AZS; X-ray; 2.30 A; A=442-656.
PDB; 1CJK; X-ray; 3.00 A; A=445-661.
PDB; 1CJT; X-ray; 2.80 A; A=445-661.
PDB; 1CJU; X-ray; 2.80 A; A=445-661.
PDB; 1CJV; X-ray; 3.00 A; A=445-661.
PDB; 1CS4; X-ray; 2.50 A; A=442-661.
PDB; 1CUL; X-ray; 2.40 A; A=445-661.
PDB; 1TL7; X-ray; 2.80 A; A=445-661.
PDB; 1U0H; X-ray; 2.90 A; A=442-661.
PDB; 2GVD; X-ray; 2.90 A; A=444-661.
PDB; 2GVZ; X-ray; 3.27 A; A=444-661.
PDB; 3C14; X-ray; 2.68 A; A=444-661.
PDB; 3C15; X-ray; 2.78 A; A=444-661.
PDB; 3C16; X-ray; 2.87 A; A=444-661.
PDB; 3G82; X-ray; 3.11 A; A=444-661.
PDB; 3MAA; X-ray; 3.00 A; A=444-661.
PDBsum; 1AZS; -.
PDBsum; 1CJK; -.
PDBsum; 1CJT; -.
PDBsum; 1CJU; -.
PDBsum; 1CJV; -.
PDBsum; 1CS4; -.
PDBsum; 1CUL; -.
PDBsum; 1TL7; -.
PDBsum; 1U0H; -.
PDBsum; 2GVD; -.
PDBsum; 2GVZ; -.
PDBsum; 3C14; -.
PDBsum; 3C15; -.
PDBsum; 3C16; -.
PDBsum; 3G82; -.
PDBsum; 3MAA; -.
ProteinModelPortal; P30803; -.
SMR; P30803; -.
DIP; DIP-179N; -.
IntAct; P30803; 1.
STRING; 9615.ENSCAFP00000017783; -.
PaxDb; P30803; -.
PRIDE; P30803; -.
GeneID; 403859; -.
KEGG; cfa:403859; -.
CTD; 111; -.
eggNOG; KOG3619; Eukaryota.
eggNOG; COG2114; LUCA.
HOGENOM; HOG000006941; -.
HOVERGEN; HBG050458; -.
InParanoid; P30803; -.
KO; K08045; -.
EvolutionaryTrace; P30803; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005929; C:cilium; ISS:UniProtKB.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0004016; F:adenylate cyclase activity; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006171; P:cAMP biosynthetic process; ISS:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
Gene3D; 3.30.70.1230; -; 2.
InterPro; IPR001054; A/G_cyclase.
InterPro; IPR018297; A/G_cyclase_CS.
InterPro; IPR032628; AC_N.
InterPro; IPR030672; Adcy.
InterPro; IPR009398; Adcy_conserved_dom.
InterPro; IPR029787; Nucleotide_cyclase.
Pfam; PF16214; AC_N; 1.
Pfam; PF06327; DUF1053; 1.
Pfam; PF00211; Guanylate_cyc; 2.
PIRSF; PIRSF039050; Ade_cyc; 1.
SMART; SM00044; CYCc; 2.
SUPFAM; SSF55073; SSF55073; 2.
PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; cAMP biosynthesis;
Cell membrane; Cell projection; Cilium; Complete proteome;
Glycoprotein; Lyase; Magnesium; Membrane; Metal-binding; Methylation;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Transmembrane; Transmembrane helix.
CHAIN 1 1265 Adenylate cyclase type 5.
/FTId=PRO_0000195693.
TOPO_DOM 1 244 Cytoplasmic. {ECO:0000255}.
TRANSMEM 245 265 Helical. {ECO:0000255}.
TRANSMEM 271 291 Helical. {ECO:0000255}.
TRANSMEM 302 322 Helical. {ECO:0000255}.
TRANSMEM 328 348 Helical. {ECO:0000255}.
TRANSMEM 352 372 Helical. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TOPO_DOM 398 765 Cytoplasmic. {ECO:0000255, ECO:0000305}.
TRANSMEM 766 786 Helical. {ECO:0000255}.
TRANSMEM 792 812 Helical. {ECO:0000255}.
TRANSMEM 839 859 Helical. {ECO:0000255}.
TRANSMEM 908 928 Helical. {ECO:0000255}.
TRANSMEM 930 950 Helical. {ECO:0000255}.
TRANSMEM 988 1008 Helical. {ECO:0000255}.
TOPO_DOM 1009 1265 Cytoplasmic. {ECO:0000255, ECO:0000305}.
DOMAIN 472 599 Guanylate cyclase 1.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
DOMAIN 1075 1214 Guanylate cyclase 2.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
NP_BIND 477 482 ATP. {ECO:0000305|PubMed:10427002,
ECO:0000305|PubMed:11087399,
ECO:0000305|PubMed:16766715,
ECO:0000305|PubMed:19243146}.
NP_BIND 519 521 ATP. {ECO:0000305|PubMed:10427002,
ECO:0000305|PubMed:11087399,
ECO:0000305|PubMed:16766715,
ECO:0000305|PubMed:19243146}.
NP_BIND 1201 1203 ATP. {ECO:0000250|UniProtKB:P26769}.
NP_BIND 1208 1212 ATP. {ECO:0000250|UniProtKB:P26769}.
METAL 477 477 Magnesium 1; catalytic.
{ECO:0000244|PDB:1CJU,
ECO:0000244|PDB:1CJV,
ECO:0000244|PDB:1CS4,
ECO:0000244|PDB:1CUL,
ECO:0000244|PDB:1U0H,
ECO:0000244|PDB:3C15,
ECO:0000269|PubMed:10427002}.
METAL 477 477 Magnesium 2; catalytic.
{ECO:0000305|PubMed:10427002}.
METAL 478 478 Magnesium 2; via carbonyl oxygen;
catalytic. {ECO:0000305|PubMed:10427002}.
METAL 521 521 Magnesium 1; catalytic.
{ECO:0000244|PDB:1CJU,
ECO:0000244|PDB:1CJV,
ECO:0000244|PDB:1CS4,
ECO:0000244|PDB:1CUL,
ECO:0000244|PDB:1U0H,
ECO:0000244|PDB:3C15,
ECO:0000269|PubMed:10427002}.
METAL 521 521 Magnesium 2; catalytic.
{ECO:0000305|PubMed:10427002}.
BINDING 565 565 ATP. {ECO:0000305|PubMed:10427002,
ECO:0000305|PubMed:11087399,
ECO:0000305|PubMed:16766715,
ECO:0000305|PubMed:19243146}.
BINDING 1127 1127 ATP. {ECO:0000250|UniProtKB:P26769}.
BINDING 1248 1248 ATP. {ECO:0000250|UniProtKB:P26769}.
MOD_RES 16 16 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P84309}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000250|UniProtKB:P84309}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000250|UniProtKB:P84309}.
MOD_RES 669 669 Phosphoserine.
{ECO:0000250|UniProtKB:O43306}.
MOD_RES 757 757 Phosphoserine.
{ECO:0000250|UniProtKB:Q03343}.
MOD_RES 1015 1015 Phosphothreonine.
{ECO:0000250|UniProtKB:Q03343}.
CARBOHYD 873 873 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 890 890 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 976 976 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 653 677 KEEKAMIAKMNRQRTNSIGHNPPHW -> VRRGGGGPRPGG
ADSPGWWGASAGP (in isoform 2).
{ECO:0000303|PubMed:8428899}.
/FTId=VSP_000242.
VAR_SEQ 678 1265 Missing (in isoform 2).
{ECO:0000303|PubMed:8428899}.
/FTId=VSP_000243.
MUTAGEN 477 477 D->A,N: Almost abolishes enzyme activity.
Abolishes enzyme activity; when
associated with A-521 or N-521.
{ECO:0000269|PubMed:10427002}.
MUTAGEN 521 521 D->A,N: Almost abolishes enzyme activity.
Abolishes enzyme activity; when
associated with A-396 or N-396.
{ECO:0000269|PubMed:10427002}.
STRAND 464 479 {ECO:0000244|PDB:1AZS}.
HELIX 481 487 {ECO:0000244|PDB:1AZS}.
HELIX 490 511 {ECO:0000244|PDB:1AZS}.
STRAND 514 519 {ECO:0000244|PDB:1AZS}.
STRAND 522 527 {ECO:0000244|PDB:1AZS}.
HELIX 536 558 {ECO:0000244|PDB:1AZS}.
STRAND 563 577 {ECO:0000244|PDB:1AZS}.
STRAND 579 582 {ECO:0000244|PDB:1AZS}.
STRAND 586 589 {ECO:0000244|PDB:1AZS}.
HELIX 590 600 {ECO:0000244|PDB:1AZS}.
STRAND 603 605 {ECO:0000244|PDB:2GVZ}.
STRAND 606 609 {ECO:0000244|PDB:1AZS}.
TURN 612 619 {ECO:0000244|PDB:1AZS}.
STRAND 623 625 {ECO:0000244|PDB:1AZS}.
HELIX 628 630 {ECO:0000244|PDB:1AZS}.
HELIX 633 637 {ECO:0000244|PDB:1AZS}.
STRAND 643 645 {ECO:0000244|PDB:1AZS}.
SEQUENCE 1265 AA; 140319 MW; 414322F64153DFB4 CRC64;
MSGPRSASPP GCAATRGGPE HRAAWGEAEA RANGHPHAAG GATRGCSKKP GGAVTPQLQQ
QQQQQQHEQQ HEQQQHEQQQ HVQQQQRLAK RWRGDDDPPL GGDDPLAGGF GFSFRSRSAW
QERGGDDCGR GSRRRRRGAA GGGSSRAPPA GGGGGPAAAG GAEVRPRSVE LGLDERRGRG
RAEPEPEAEA GAPGGDRGAR DGDGPAGPGA CCRALLQIFR SKKFPSDKLE RLYQRYFFRL
NQSSLTMLMA VLVLVCLVML AFHAARPPLR LPHLAVLAAA VGVILVMAVL CNRAAFHQDH
MGLACYALIA VVLAVQVVGL LLPQPRSASE GIWWTVFFIY TIYTLLPVRM RAAVLSGVLL
SALHLAIALR ANAQDRFLLK QLVSNVLIFS CTNIVGVCTH YPAEVSQRQA FQETRECIQA
RLHSQRENQQ QERLLLSVLP RHVAMEMKAD INAKQEDMMF HKIYIQKHDN VSILFADIEG
FTSLASQCTA QELVMTLNEL FARFDKLAAE NHCLRIKILG DCYYCVSGLP EARADHAHCC
VEMGMDMIEA ISLVREVTGV NVNMRVGIHS GRVHCGVLGL RKWQFDVWSN DVTLANHMEA
GGKAGRIHIT KATLSYLNGD YEVEPGCGGE RNAYLKEHSI ETFLILRCTQ KRKEEKAMIA
KMNRQRTNSI GHNPPHWGAE RPFYNHLGGN QVSKEMKRMG FEDPKDKNAQ ESANPEDEVD
EFLGRAIDAR SIDRLRSEHV RKFLLTFREP DLEKKYSKQV DDRFGAYVAC ASLVFLFICF
VQITIVPHSV FMLSFYLTCF LLLTLVVFVS VIYSCVKLFP GPLQSLSRKI VRSKTNSTLV
GVFTITLVFL SAFVNMFMCN SEDLLGCLAD EHNISTSRVN ACHVAASAAN LSLGDEQGFC
GTPWPSCNFP EYFTYSVLLS LLACSVFLQI SCIGKLVLML AIELIYVLVV EVPRVTLFDN
ADLLVTANAI DFNNNNGTSQ CPEHATKVAL KVVTPIIISV FVLALYLHAQ QVESTARLDF
LWKLQATEEK EEMEELQAYN RRLLHNILPK DVAAHFLARE RRNDELYYQS CECVAVMFAS
IANFSEFYVE LEANNEGVEC LRVLNEIIAD FDEIISEDRF RQLEKIKTIG STYMAASGLN
DSTYDKVGKT HIKALADFAM KLMDQMKYIN EHSFNNFQMK IGLNIGPVVA GVIGARKPQY
DIWGNTVNVA SRMDSTGVPD RIQVTTDMYQ VLAANTYQLE CRGVVKVKGK GEMMTYFLNG
GPPLS


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Catalog number Product name Quantity
E1349h ELISA ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Homo sapiens,Human 96T
E1349h ELISA kit ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Homo sapiens,Human 96T
U1349h CLIA ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Homo sapiens,Human 96T
E1349b ELISA ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Bos taurus,Bovine,Ca(2+)_calmodulin-activated adenylyl cyclase 96T
U1349m CLIA Adcy1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Mouse,Mus musculus 96T
U1349b CLIA ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Bos taurus,Bovine,Ca(2+)_calmodulin-activated adenylyl cyclase 96T
E1349m ELISA kit Adcy1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Mouse,Mus musculus 96T
E1349b ELISA kit ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Bos taurus,Bovine,Ca(2+)_calmodulin-activated adenylyl cyclase 96T
E1349m ELISA Adcy1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Mouse,Mus musculus 96T
15-288-21024 Adenylate cyclase type 6 - EC 4.6.1.1; Adenylate cyclase type VI; ATP pyrophosphate-lyase 6; Ca(2+)-inhibitable adenylyl cyclase Polyclonal 0.05 mg
15-288-21024 Adenylate cyclase type 6 - EC 4.6.1.1; Adenylate cyclase type VI; ATP pyrophosphate-lyase 6; Ca(2+)-inhibitable adenylyl cyclase Polyclonal 0.1 mg
U1348h CLIA ADCY10,Adenylate cyclase homolog,Adenylate cyclase type 10,AH-related protein,Germ cell soluble adenylyl cyclase,Homo sapiens,hsAC,Human,sAC,SAC,Testicular soluble adenylyl cyclase 96T
E1348h ELISA kit ADCY10,Adenylate cyclase homolog,Adenylate cyclase type 10,AH-related protein,Germ cell soluble adenylyl cyclase,Homo sapiens,hsAC,Human,sAC,SAC,Testicular soluble adenylyl cyclase 96T
E1348h ELISA ADCY10,Adenylate cyclase homolog,Adenylate cyclase type 10,AH-related protein,Germ cell soluble adenylyl cyclase,Homo sapiens,hsAC,Human,sAC,SAC,Testicular soluble adenylyl cyclase 96T
U1348Rb CLIA ADCY10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Oryctolagus cuniculus,Rabbit,sAC,SAC,Testicular soluble adenylyl cyclase 96T
E1348Rb ELISA ADCY10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Oryctolagus cuniculus,Rabbit,sAC,SAC,Testicular soluble adenylyl cyclase 96T
E1348Rb ELISA kit ADCY10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Oryctolagus cuniculus,Rabbit,sAC,SAC,Testicular soluble adenylyl cyclase 96T
E1348m ELISA kit Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Mouse,Mus musculus,sAC,Sac,Sacy,Testicular soluble adenylyl cyclase 96T
E1348m ELISA Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Mouse,Mus musculus,sAC,Sac,Sacy,Testicular soluble adenylyl cyclase 96T
U1348m CLIA Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Mouse,Mus musculus,sAC,Sac,Sacy,Testicular soluble adenylyl cyclase 96T
U1348r CLIA Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Rat,Rattus norvegicus,sAC,Sac,Testicular soluble adenylyl cyclase 96T
E1348r ELISA kit Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Rat,Rattus norvegicus,sAC,Sac,Testicular soluble adenylyl cyclase 96T
E1348r ELISA Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Rat,Rattus norvegicus,sAC,Sac,Testicular soluble adenylyl cyclase 96T
136134-68-4 adenylate cyclase activating peptide frag adenylate cyclase activ 1g
127317-03-7 adenylate cyclase activating peptide_27 adenylate cyclase activ 1g


 

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