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Adenylate cyclase type 6 (EC 4.6.1.1) (ATP pyrophosphate-lyase 6) (Adenylate cyclase type VI) (ACVI) (Adenylyl cyclase 6) (AC6) (Ca(2 )-inhibitable adenylyl cyclase)

 ADCY6_RAT               Reviewed;        1166 AA.
Q03343;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
22-NOV-2017, entry version 150.
RecName: Full=Adenylate cyclase type 6;
EC=4.6.1.1 {ECO:0000269|PubMed:1409703, ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:21606183, ECO:0000269|PubMed:9391159};
AltName: Full=ATP pyrophosphate-lyase 6;
AltName: Full=Adenylate cyclase type VI;
Short=ACVI;
AltName: Full=Adenylyl cyclase 6;
Short=AC6 {ECO:0000303|PubMed:9391159};
AltName: Full=Ca(2+)-inhibitable adenylyl cyclase;
Name=Adcy6;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1332969;
Krupinski J., Lehman T.C., Frankenfield C.D., Zwaagstra J.C.,
Watson P.A.;
"Molecular diversity in the adenylylcyclase family. Evidence for eight
forms of the enzyme and cloning of type VI.";
J. Biol. Chem. 267:24858-24862(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=1409703; DOI=10.1073/pnas.89.20.9809;
Premont R.T., Chen J., Ma H.-W., Ponnapalli M., Iyengar R.;
"Two members of a widely expressed subfamily of hormone-stimulated
adenylyl cyclases.";
Proc. Natl. Acad. Sci. U.S.A. 89:9809-9813(1992).
[3]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, ENZYME
REGULATION, MUTAGENESIS OF SER-660, AND PHOSPHORYLATION AT SER-660.
PubMed=9391159; DOI=10.1073/pnas.94.25.14100;
Chen Y., Harry A., Li J., Smit M.J., Bai X., Magnusson R.,
Pieroni J.P., Weng G., Iyengar R.;
"Adenylyl cyclase 6 is selectively regulated by protein kinase A
phosphorylation in a region involved in Galphas stimulation.";
Proc. Natl. Acad. Sci. U.S.A. 94:14100-14104(1997).
[4]
PHOSPHORYLATION AT SER-554; SER-660 AND THR-917, AND MUTAGENESIS OF
SER-311; SER-554; SER-660 AND THR-917.
PubMed=11877398; DOI=10.1074/jbc.M111537200;
Lin T.-H., Lai H.-L., Kao Y.-Y., Sun C.-N., Hwang M.-J., Chern Y.;
"Protein kinase C inhibits type VI adenylyl cyclase by phosphorylating
the regulatory N domain and two catalytic C1 and C2 domains.";
J. Biol. Chem. 277:15721-15728(2002).
[5]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PHOSPHORYLATION BY RAF1,
INTERACTION WITH RAF1, AND ENZYME REGULATION.
PubMed=15385642; DOI=10.1124/mol.66.4.;
Ding Q., Gros R., Gray I.D., Taussig R., Ferguson S.S., Feldman R.D.;
"Raf kinase activation of adenylyl cyclases: isoform-selective
regulation.";
Mol. Pharmacol. 66:921-928(2004).
[6]
CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, AND SUBCELLULAR
LOCATION.
PubMed=17110384; DOI=10.1074/jbc.M607522200;
Gao X., Sadana R., Dessauer C.W., Patel T.B.;
"Conditional stimulation of type V and VI adenylyl cyclases by G
protein betagamma subunits.";
J. Biol. Chem. 282:294-302(2007).
[7]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND TISSUE
SPECIFICITY.
PubMed=21606183; DOI=10.1093/cvr/cvr137;
Nelson C.P., Rainbow R.D., Brignell J.L., Perry M.D., Willets J.M.,
Davies N.W., Standen N.B., Challiss R.A.;
"Principal role of adenylyl cyclase 6 in K? channel regulation and
vasodilator signalling in vascular smooth muscle cells.";
Cardiovasc. Res. 91:694-702(2011).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND SER-574, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP
downstream of G protein-coupled receptors (PubMed:1409703,
PubMed:15385642, PubMed:17110384, PubMed:21606183). Functions in
signaling cascades downstream of beta-adrenergic receptors in the
heart and in vascular smooth muscle cells (PubMed:21606183).
Functions in signaling cascades downstream of the vasopressin
receptor in the kidney and has a role in renal water reabsorption.
Functions in signaling cascades downstream of PTH1R and plays a
role in regulating renal phosphate excretion. Functions in
signaling cascades downstream of the VIP and SCT receptors in
pancreas and contributes to the regulation of pancreatic amylase
and fluid secretion (By similarity). Signaling mediates cAMP-
dependent activation of protein kinase PKA (PubMed:21606183). This
promotes increased phosphorylation of various proteins, including
AKT. Plays a role in regulating cardiac sarcoplasmic reticulum
Ca(2+) uptake and storage, and is required for normal heart
ventricular contractibility. May contribute to normal heart
function (By similarity). Mediates vasodilatation after activation
of beta-adrenergic receptors by isoproterenol (By similarity).
Contributes to bone cell responses to mechanical stimuli (By
similarity). {ECO:0000250|UniProtKB:O43306,
ECO:0000250|UniProtKB:Q01341, ECO:0000269|PubMed:1409703,
ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:17110384,
ECO:0000269|PubMed:21606183}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
{ECO:0000269|PubMed:1409703, ECO:0000269|PubMed:15385642,
ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:21606183,
ECO:0000269|PubMed:9391159}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15385642};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:15385642,
ECO:0000269|PubMed:9391159};
Note=Binds 2 magnesium ions per subunit. Is also active with
manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
-!- ENZYME REGULATION: Activated by forskolin (PubMed:9391159).
Inhibited by calcium ions, already at micromolar concentrations
(By similarity). Inhibited by adenosine, AMP and their analogs (By
similarity). Activated by GNAS (PubMed:9391159, PubMed:17110384).
Is further activated by the complex formed by GNB1 and GNG2
(PubMed:17110384). Phosphorylation by RAF1 results in its
activation (PubMed:15385642). {ECO:0000250|UniProtKB:P30804,
ECO:0000250|UniProtKB:Q01341, ECO:0000269|PubMed:15385642,
ECO:0000269|PubMed:17110384}.
-!- SUBUNIT: Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2
(By similarity). Interacts with RAF1 (PubMed:15385642). Interacts
(via cytoplasmic N-terminus) with GNAS, GNB1 and GNG2 (By
similarity). {ECO:0000250|UniProtKB:O43306,
ECO:0000250|UniProtKB:Q01341, ECO:0000269|PubMed:15385642}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15385642,
ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:9391159}; Multi-
pass membrane protein {ECO:0000305}. Cell projection, cilium
{ECO:0000250|UniProtKB:Q01341}.
-!- TISSUE SPECIFICITY: Detected in brain and kidney (PubMed:1409703).
Detected in vascular smooth muscle cells (PubMed:21606183).
{ECO:0000269|PubMed:1409703, ECO:0000269|PubMed:21606183}.
-!- 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:0000250|UniProtKB:P26769}.
-!- PTM: Phosphorylation by RAF1 increases enzyme activity
(PubMed:15385642). Phosphorylation by PKA on Ser-660 inhibits the
GNAS-mediated increase in catalytic activity (PubMed:9391159).
Phosphorylation by PKC on Ser-554, Ser-660 and Thr-917 inhibits
catalytic activity (PubMed:11877398).
{ECO:0000269|PubMed:11877398, ECO:0000269|PubMed:15385642,
ECO:0000269|PubMed:9391159}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
-!- SEQUENCE CAUTION:
Sequence=AAA40678.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; L01115; AAA40676.1; -; mRNA.
EMBL; M96160; AAA40678.1; ALT_INIT; mRNA.
PIR; A47202; A47202.
RefSeq; NP_036953.4; NM_012821.4.
UniGene; Rn.3313; -.
ProteinModelPortal; Q03343; -.
SMR; Q03343; -.
IntAct; Q03343; 2.
STRING; 10116.ENSRNOP00000016624; -.
ChEMBL; CHEMBL2095179; -.
iPTMnet; Q03343; -.
PhosphoSitePlus; Q03343; -.
SwissPalm; Q03343; -.
PaxDb; Q03343; -.
PRIDE; Q03343; -.
GeneID; 25289; -.
KEGG; rno:25289; -.
UCSC; RGD:2035; rat.
CTD; 112; -.
RGD; 2035; Adcy6.
eggNOG; KOG3619; Eukaryota.
eggNOG; COG2114; LUCA.
HOGENOM; HOG000006941; -.
HOVERGEN; HBG050458; -.
InParanoid; Q03343; -.
KO; K08046; -.
PhylomeDB; Q03343; -.
PRO; PR:Q03343; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:RGD.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0031528; C:microvillus membrane; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0004016; F:adenylate cyclase activity; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008294; F:calcium- and calmodulin-responsive adenylate cyclase activity; IDA:RGD.
GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
GO; GO:0005102; F:receptor binding; IPI:RGD.
GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
GO; GO:0000149; F:SNARE binding; IDA:ParkinsonsUK-UCL.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006171; P:cAMP biosynthetic process; IDA:RGD.
GO; GO:0071870; P:cellular response to catecholamine stimulus; ISO:RGD.
GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:RGD.
GO; GO:1904117; P:cellular response to vasopressin; ISS:UniProtKB.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0007212; P:dopamine receptor signaling pathway; ISO:RGD.
GO; GO:0072660; P:maintenance of protein location in plasma membrane; IMP:ParkinsonsUK-UCL.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:ParkinsonsUK-UCL.
GO; GO:0035811; P:negative regulation of urine volume; ISS:UniProtKB.
GO; GO:0097746; P:regulation of blood vessel diameter; ISO:RGD.
GO; GO:0003091; P:renal water homeostasis; 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;
ATP-binding; cAMP biosynthesis; Cell membrane; Cell projection;
Cilium; Complete proteome; Glycoprotein; Lyase; Magnesium; Manganese;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix.
CHAIN 1 1166 Adenylate cyclase type 6.
/FTId=PRO_0000195701.
TOPO_DOM 1 149 Cytoplasmic. {ECO:0000255}.
TRANSMEM 150 166 Helical. {ECO:0000255}.
TRANSMEM 179 195 Helical. {ECO:0000255}.
TRANSMEM 212 228 Helical. {ECO:0000255}.
TRANSMEM 237 253 Helical. {ECO:0000255}.
TRANSMEM 257 273 Helical. {ECO:0000255}.
TRANSMEM 287 303 Helical. {ECO:0000255}.
TOPO_DOM 304 671 Cytoplasmic. {ECO:0000255}.
TRANSMEM 672 689 Helical. {ECO:0000255}.
TRANSMEM 700 716 Helical. {ECO:0000255}.
TRANSMEM 741 757 Helical. {ECO:0000255}.
TOPO_DOM 758 817 Extracellular. {ECO:0000255}.
TRANSMEM 818 834 Helical. {ECO:0000255}.
TRANSMEM 837 853 Helical. {ECO:0000255}.
TRANSMEM 895 911 Helical. {ECO:0000255}.
TOPO_DOM 912 1166 Cytoplasmic. {ECO:0000255}.
NP_BIND 382 387 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 424 426 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 1103 1105 ATP. {ECO:0000250|UniProtKB:P26769}.
NP_BIND 1110 1114 ATP. {ECO:0000250|UniProtKB:P26769}.
METAL 382 382 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 382 382 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 383 383 Magnesium 2; via carbonyl oxygen;
catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
METAL 426 426 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 426 426 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
BINDING 470 470 ATP. {ECO:0000250|UniProtKB:P30803}.
BINDING 1029 1029 ATP. {ECO:0000250|UniProtKB:P26769}.
BINDING 1150 1150 ATP. {ECO:0000250|UniProtKB:P26769}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 554 554 Phosphoserine; by PKC; in vitro.
{ECO:0000269|PubMed:11877398}.
MOD_RES 574 574 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 660 660 Phosphoserine; by PKA; in vitro.
{ECO:0000269|PubMed:9391159}.
MOD_RES 660 660 Phosphoserine; by PKC; in vitro.
{ECO:0000269|PubMed:11877398}.
MOD_RES 917 917 Phosphothreonine; by PKC; in vitro.
{ECO:0000269|PubMed:11877398}.
CARBOHYD 791 791 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 876 876 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 311 311 S->A: No effect on phosphorylation by
PKC. {ECO:0000269|PubMed:11877398}.
MUTAGEN 554 554 S->A: Reduces phosphorylation by PKC and
PKC-mediated inhibition.
{ECO:0000269|PubMed:11877398}.
MUTAGEN 660 660 S->A: Abolishes phosphorylation by PKA
and PKA-mediated down-regulation of
enzyme activity.
{ECO:0000269|PubMed:9391159}.
MUTAGEN 660 660 S->A: Reduces phosphorylation by PKC and
PKC-mediated inhibition.
{ECO:0000269|PubMed:11877398}.
MUTAGEN 917 917 T->A: Reduces phosphorylation by PKC,
abolishes PKC-mediated inhibition.
{ECO:0000269|PubMed:11877398}.
CONFLICT 80 80 K -> E (in Ref. 2; AAA40678).
{ECO:0000305}.
CONFLICT 130 130 R -> P (in Ref. 2; AAA40678).
{ECO:0000305}.
CONFLICT 538 538 G -> A (in Ref. 2; AAA40678).
{ECO:0000305}.
CONFLICT 790 790 I -> L (in Ref. 2; AAA40678).
{ECO:0000305}.
SEQUENCE 1166 AA; 130506 MW; 5042C650546E4E79 CRC64;
MSWFSGLLVP KVDERKTAWG ERNGQKRPRQ ATRARGFCAP RYMSCLKNVE PPSPTPAART
RCPWQDEAFI RRAGPGRGVK LGLRSVALGF DDTEVTTPMG TAEVAPDTSP RSGPSCWHRL
AQVFQSKQFR SAKLERLYQR YFFQMNQSSL TLLMAVLVLL MAVLLTFHAA PALPQPAYVA
LLTCASVLFV VLMVVCNRHS FRQDSMWVVS YVVLGILAAV QVGGALAANP RSPSAGLWCP
VFFVYITYTL LPIRMRAAVL SGLGLSTLHL ILAWHLNNGD PFLWKQLGAN VVLFLCTNAI
GVCTHYPAEV SQRQAFQETR GYIQARLHLQ HENRQQERLL LSVLPQHVAM EMKEDINTKK
EDMMFHKIYI QKHDNVSILF ADIEGFTSLA SQCTAQELVM TLNELFARFD KLAAENHCLR
IKILGDCYYC VSGLPEARAD HAHCCVEMGV DMIEAISLVR EVTGVNVNMR VGIHSGRVHC
GVLGLRKWQF DVWSNDVTLA NHMEAGGRAG RIHITRATLQ YLNGDYEVEP GRGGERNGYL
KEQCIETFLI LGASQKRKEE KAMLVKLQRT RANSMEGLMP RWVPDRAFSR TKDSKAFRQM
GIDDSSKENR GAQDALNPED EVDEFLGRAI DARSIDQLRK DHVRRFLLTF QREDLEKKYS
RKVDPRFGAY VACALLVFCF ICFIQFLVFP HSALILGIYA GIFLLLLVTV LICAVCSCGS
FFPNALQRLS RSIVRSRVHS TAVGVFSVLL VFISAIANMF TCSHTPLRTC AARMLNLTPS
DVTACHLRQI NYSLGLEAPL CEGTAPTCSF PEYFVGSVLL SLLASSVFLH ISSIGKLVMT
FVLGFIYLLL LLLGPPATIF DNYDLLLSVH GLASSNETFD GLDCPAVGRV ALKYMTPVIL
LVFALALYLH AQQVESTARL DFLWKLQATG EKEEMEELQA YNRRLLHNIL PKDVAAHFLA
RERRNDELYY QSCECVAVMF ASIANFSEFY VELEANNEGV ECLRLLNEII ADFDEIISEE
RFRQLEKIKT IGSTYMAASG LNASTYDQVG RSHITALADY AMRLMEQMKH INEHSFNNFQ
MKIGLNMGPV VAGVIGARKP QYDIWGNTVN VSSRMDSTGV PDRIQVTTDL YQVLAAKGYQ
LECRGVVKVK GKGEMTTYFL NGGPSS


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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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