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

 ADCY6_CANLF             Reviewed;        1165 AA.
P30804;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
25-OCT-2017, entry version 120.
RecName: Full=Adenylate cyclase type 6;
EC=4.6.1.1 {ECO:0000269|PubMed:1528892, ECO:0000269|PubMed:17110384};
AltName: Full=ATP pyrophosphate-lyase 6;
AltName: Full=Adenylate cyclase type VI;
AltName: Full=Adenylyl cyclase 6;
AltName: Full=Ca(2+)-inhibitable adenylyl cyclase;
Name=ADCY6;
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], CATALYTIC ACTIVITY, FUNCTION, COFACTOR,
ENZYME REGULATION, AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=1528892; DOI=10.1073/pnas.89.18.8774;
Katsushika S., Chen L., Kawabe J., Nilakantan R., Halnon N.J.,
Homcy C.J., Ishikawa Y.;
"Cloning and characterization of a sixth adenylyl cyclase isoform:
types V and VI constitute a subgroup within the mammalian adenylyl
cyclase family.";
Proc. Natl. Acad. Sci. U.S.A. 89:8774-8778(1992).
[2]
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).
-!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP
downstream of G protein-coupled receptors (PubMed:1528892,
PubMed:17110384). 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 (By
similarity). 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:0000250|UniProtKB:Q03343,
ECO:0000269|PubMed:1528892, ECO:0000269|PubMed:17110384}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
{ECO:0000269|PubMed:1528892, ECO:0000269|PubMed:17110384}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:O43306};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:1528892};
Note=Binds 2 magnesium ions per subunit. Is also active with
manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
-!- ENZYME REGULATION: Activated by forskolin. Inhibited by calcium
ions, already at micromolar concentrations. Inhibited by
adenosine, AMP and their analogs (PubMed:1528892). Activated by
GNAS (PubMed:17110384). Is further activated by the complex formed
by GNB1 and GNG2 (PubMed:17110384). Phosphorylation by RAF1
results in its activation (By similarity).
{ECO:0000250|UniProtKB:Q03343, ECO:0000269|PubMed:1528892,
ECO:0000269|PubMed:17110384}.
-!- SUBUNIT: Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2
(By similarity). Interacts with RAF1. Interacts (via cytoplasmic
N-terminus) with GNAS, GNB1 and GNG2 (By similarity).
{ECO:0000250|UniProtKB:O43306, ECO:0000250|UniProtKB:Q01341}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1528892,
ECO:0000269|PubMed:17110384}; Multi-pass membrane protein
{ECO:0000305}. Cell projection, cilium
{ECO:0000250|UniProtKB:Q01341}.
-!- TISSUE SPECIFICITY: Detected in brain and heart.
{ECO:0000269|PubMed:1528892}.
-!- 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.
Phosphorylation by PKA on Ser-659 inhibits the GNAS-mediated
increase in catalytic activity. Phosphorylation by PKC on Ser-553,
Ser-659 and Thr-916 inhibits catalytic activity.
{ECO:0000250|UniProtKB:Q03343}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
-----------------------------------------------------------------------
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EMBL; M94968; -; NOT_ANNOTATED_CDS; mRNA.
PIR; A46180; A46180.
UniGene; Cfa.3893; -.
ProteinModelPortal; P30804; -.
SMR; P30804; -.
STRING; 9615.ENSCAFP00000013079; -.
PaxDb; P30804; -.
eggNOG; KOG3619; Eukaryota.
eggNOG; COG2114; LUCA.
HOGENOM; HOG000006941; -.
HOVERGEN; HBG050458; -.
InParanoid; P30804; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
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: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:1904117; P:cellular response to vasopressin; ISS:UniProtKB.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0035811; P:negative regulation of urine volume; ISS:UniProtKB.
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 1165 Adenylate cyclase type 6.
/FTId=PRO_0000195698.
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 304 670 Cytoplasmic. {ECO:0000255}.
TRANSMEM 671 688 Helical. {ECO:0000255}.
TRANSMEM 699 715 Helical. {ECO:0000255}.
TRANSMEM 740 756 Helical. {ECO:0000255}.
TOPO_DOM 757 816 Extracellular. {ECO:0000255}.
TRANSMEM 817 833 Helical. {ECO:0000255}.
TRANSMEM 836 852 Helical. {ECO:0000255}.
TRANSMEM 894 910 Helical. {ECO:0000255}.
TOPO_DOM 911 1165 Cytoplasmic. {ECO:0000255}.
NP_BIND 382 387 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 424 426 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 1102 1104 ATP. {ECO:0000250|UniProtKB:P26769}.
NP_BIND 1109 1113 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 1028 1028 ATP. {ECO:0000250|UniProtKB:P26769}.
BINDING 1149 1149 ATP. {ECO:0000250|UniProtKB:P26769}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000250|UniProtKB:O43306}.
MOD_RES 553 553 Phosphoserine.
{ECO:0000250|UniProtKB:Q03343}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000250|UniProtKB:O43306}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000250|UniProtKB:Q03343}.
MOD_RES 916 916 Phosphothreonine.
{ECO:0000250|UniProtKB:Q03343}.
CARBOHYD 790 790 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 875 875 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 1165 AA; 130324 MW; BA9D2D329120615E CRC64;
MSWFSGLLVP KVDERKTAWG ERNGQKRPRR GTRTSGFCTP RYMSCLRDAQ PPSPTPAAPP
RCPWQDEAFI RRGGPGKGTE LGLRAVALGF EDTEAMSAVG AAGGGPDVTP GSRRSCWRRL
AQVFQSKQFR SAKLERLYQR YFFQMNQSSL TLLMAVLVLL TAVLLAFHAA PARPQPAYVA
LLACAATLFV ALMVVCNRHS FRQDSMWVVS YVVLGILAAV QVGGALAANP RSPSVGLWCP
VFFVYITYTL LPIRMRAAVF SGLGLSTLHL ILAWQLNRGD AFLWKQLGAN MLLFLCTNVI
GICTHYPAEV SQRQAFQETR GYIQARLHLP DENRQQERLL LSVLPQHVAM EMKEDINTKK
EDMMFHKIYI QKHDNVSILF ADIEGFTSLA SQCTAQELVM TLNELFARFD KLAAENHCLR
IKILGDCYYC VSGLPEARAD HAHCCVEMGV DMIEAISLVR EVTGVNVNMR VGIHSGRVHC
GVLGLRKWQF DVWSNDVTLA NHMEAARAGR IHITRATLQY LNGDYEVEPG RGGERNAYLK
EQHIETFLIL GASQKRKEEK AMLAKLQRTR ANSMEGLMPR WVPDRAFSRT KDSKAFRQMG
IDDSSKDNRG AQDALNPEDE VDEFLGRAID ARSIDQLRKD HVRRFLLTFQ REDLEKKYSR
KVDPRFGAYV ACALLVFCFI CFIQLLVFPH STVMLGIYAS IFVLLLITVL TCAVYSCGSL
FPKALRRLSR SIVRSRAHST VVGIFSVLLV FTSAIANMFT CNHTPIRTCA ARMLNVTPAD
ITACHLQQLN YSLGLDAPLC EGTAPTCSFP EYFVGNMLLS LLASSVFLHI SSIGKLAMIF
VLGLIYLVLL LLGPPSTIFD NYDLLLGVHG LASSNDTFDG LDCPAAGRVA LKYMTPVILL
VFALALYLHA QQVESTARLD FLWKLQATGE KEEMEELQAY NRRLLHNILP KDVAAHFLAR
ERRNDELYYQ SCECVAVMFA SIANFSEFYV ELEANNEGVE CLRLLNEIIA DFDEIISEER
FRQLEKIKTI GSTYMAASGL NASTYDQAGR SHITALADYA MRLMEQMKHI NEHSFNNFQM
KIGLNMGPVV AGVIGARKPQ YDIWGNTVNV SSRMDSTGVP DRIQVTTDLY QVLAAKRYQL
ECRGVVKVKG KGEMTTYFLN GGPPS


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