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Adenylate cyclase type 3 (EC 4.6.1.1) (ATP pyrophosphate-lyase 3) (Adenylate cyclase type III) (AC-III) (Adenylate cyclase, olfactive type) (Adenylyl cyclase 3) (AC3)

 ADCY3_MOUSE             Reviewed;        1145 AA.
Q8VHH7; B8JK57;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
25-OCT-2017, entry version 146.
RecName: Full=Adenylate cyclase type 3;
EC=4.6.1.1 {ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:25329148, ECO:0000269|PubMed:9768837};
AltName: Full=ATP pyrophosphate-lyase 3;
AltName: Full=Adenylate cyclase type III;
Short=AC-III;
AltName: Full=Adenylate cyclase, olfactive type;
AltName: Full=Adenylyl cyclase 3;
Short=AC3 {ECO:0000303|PubMed:9768837};
Name=Adcy3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
Pasternak S., Neumann P.E.;
"Sequence of mouse Adcy3.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-1077, SUBCELLULAR
LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
PubMed=9768837; DOI=10.1016/S0896-6273(00)80561-9;
Wei J., Zhao A.Z., Chan G.C., Baker L.P., Impey S., Beavo J.A.,
Storm D.R.;
"Phosphorylation and inhibition of olfactory adenylyl cyclase by CaM
kinase II in neurons: a mechanism for attenuation of olfactory
signals.";
Neuron 21:495-504(1998).
[5]
DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11055432; DOI=10.1016/S0896-6273(00)00060-X;
Wong S.T., Trinh K., Hacker B., Chan G.C., Lowe G., Gaggar A., Xia Z.,
Gold G.H., Storm D.R.;
"Disruption of the type III adenylyl cyclase gene leads to peripheral
and behavioral anosmia in transgenic mice.";
Neuron 27:487-497(2000).
[6]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15705663; DOI=10.1210/me.2004-0318;
Livera G., Xie F., Garcia M.A., Jaiswal B., Chen J., Law E.,
Storm D.R., Conti M.;
"Inactivation of the mouse adenylyl cyclase 3 gene disrupts male
fertility and spermatozoon function.";
Mol. Endocrinol. 19:1277-1290(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
MUTAGENESIS OF MET-279, FUNCTION, CATALYTIC ACTIVITY, AND ENZYME
REGULATION.
PubMed=25329148; DOI=10.1371/journal.pone.0110226;
Pitman J.L., Wheeler M.C., Lloyd D.J., Walker J.R., Glynne R.J.,
Gekakis N.;
"A gain-of-function mutation in adenylate cyclase 3 protects mice from
diet-induced obesity.";
PLoS ONE 9:E110226-E110226(2014).
[9]
SUMOYLATION, AND TISSUE SPECIFICITY.
PubMed=25908845; DOI=10.1242/jcs.164673;
McIntyre J.C., Joiner A.M., Zhang L., Iniguez-Lluhi J., Martens J.R.;
"SUMOylation regulates ciliary localization of olfactory signaling
proteins.";
J. Cell Sci. 128:1934-1945(2015).
-!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP
in response to G-protein signaling (PubMed:9768837,
PubMed:11055432, PubMed:25329148). Participates in signaling
cascades triggered by odorant receptors via its function in cAMP
biosynthesis (PubMed:9768837, PubMed:11055432). Required for the
perception of odorants (PubMed:11055432). Required for normal
sperm motility and normal male fertility (PubMed:15705663). Plays
a role in regulating insulin levels and body fat accumulation in
response to a high fat diet (PubMed:25329148).
{ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:15705663,
ECO:0000269|PubMed:9768837}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
{ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:25329148,
ECO:0000269|PubMed:9768837}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P30803};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:P30803};
Note=Binds 2 magnesium ions per subunit. Is also active with
manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
-!- ENZYME REGULATION: Activated by forskolin (PubMed:11055432,
PubMed:25329148). After forskolin treatment, activity is further
increased by calcium/calmodulin. In the absence of forskolin,
calcium/calmodulin has little effect on enzyme activity (By
similarity). {ECO:0000250|UniProtKB:P21932,
ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:25329148}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11055432};
Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium
{ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:9768837}. Golgi
apparatus {ECO:0000250|UniProtKB:P21932}. Cytoplasm
{ECO:0000250|UniProtKB:O60266}.
-!- TISSUE SPECIFICITY: Detected in the acrosomal region of epididymal
spermatozoa, the acrosomal region of round spermatids and in
elongating spermatids (PubMed:15705663). Detected in cilia in the
olfactory epithelium (at protein level) (PubMed:9768837,
PubMed:11055432, PubMed:25908845). Detected in olfactory
epithelium neurons (PubMed:11055432). Detected in brain, testis,
late pachytene spermatocytes, round spermatids and elongating
spermatids (PubMed:15705663). {ECO:0000269|PubMed:11055432,
ECO:0000269|PubMed:15705663}.
-!- DOMAIN: The protein contains two modules with six transmembrane
helices each; both are required for catalytic activity. Isolated
N-terminal or C-terminal modules have no catalytic activity, but
when they are brought together, enzyme activity is restored. The
active site is at the interface of the two modules.
{ECO:0000250|UniProtKB:P30803}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:9768837}.
-!- PTM: Rapidly phosphorylated after stimulation by odorants or
forskolin. Phosphorylation by CaMK2 at Ser-1077 down-regulates
enzyme activity. {ECO:0000269|PubMed:9768837}.
-!- PTM: Sumoylated (PubMed:25908845). Sumoylation is required for
targeting of olfactory cilia. {ECO:0000250|UniProtKB:P21932,
ECO:0000269|PubMed:25908845}.
-!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected
Mendelian rate, but up to 80% of the pups die within 48 h after
birth. Survival is improved by paring down the litter size shortly
after birth. Mutant mice are initially smaller than wild-type, but
achieve normal size within three months. Mutant mice do not
display the normal electrophysiological responses to odorants that
stimulate production of cAMP or inositoltrisphosphate (IP3).
Likewise, behavorial responses to smells are abolished
(PubMed:11055432). In spite of normal mating behavior, they do not
produce any offspring (PubMed:11055432, PubMed:15705663). Male
mice have strongly reduced fertility due to defects in sperm
motility, an increased rate of spontaneous acrosome reactions and
an impaired ability to penetrate the oocyte zona
(PubMed:15705663). {ECO:0000269|PubMed:11055432,
ECO:0000269|PubMed:15705663}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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EMBL; AF458089; AAL59384.1; -; mRNA.
EMBL; CT572999; CAX15321.1; -; Genomic_DNA.
EMBL; CH466623; EDL01374.1; -; Genomic_DNA.
CCDS; CCDS25787.1; -.
RefSeq; NP_612178.2; NM_138305.3.
RefSeq; XP_006514995.1; XM_006514932.2.
RefSeq; XP_006514996.1; XM_006514933.2.
RefSeq; XP_006514997.1; XM_006514934.3.
RefSeq; XP_006514998.1; XM_006514935.3.
UniGene; Mm.489807; -.
ProteinModelPortal; Q8VHH7; -.
SMR; Q8VHH7; -.
BioGrid; 222368; 2.
IntAct; Q8VHH7; 1.
MINT; MINT-7290275; -.
STRING; 10090.ENSMUSP00000020984; -.
iPTMnet; Q8VHH7; -.
PhosphoSitePlus; Q8VHH7; -.
EPD; Q8VHH7; -.
MaxQB; Q8VHH7; -.
PaxDb; Q8VHH7; -.
PRIDE; Q8VHH7; -.
Ensembl; ENSMUST00000020984; ENSMUSP00000020984; ENSMUSG00000020654.
Ensembl; ENSMUST00000127756; ENSMUSP00000115406; ENSMUSG00000020654.
GeneID; 104111; -.
KEGG; mmu:104111; -.
UCSC; uc007mxm.2; mouse.
CTD; 109; -.
MGI; MGI:99675; Adcy3.
eggNOG; KOG3619; Eukaryota.
eggNOG; COG2114; LUCA.
GeneTree; ENSGT00760000119042; -.
HOGENOM; HOG000006941; -.
HOVERGEN; HBG050458; -.
InParanoid; Q8VHH7; -.
KO; K08043; -.
OMA; DEHELNQ; -.
OrthoDB; EOG091G05JR; -.
PhylomeDB; Q8VHH7; -.
BRENDA; 4.6.1.1; 3474.
Reactome; R-MMU-163359; Glucagon signaling in metabolic regulation.
Reactome; R-MMU-163615; PKA activation.
Reactome; R-MMU-164378; PKA activation in glucagon signalling.
Reactome; R-MMU-170660; Adenylate cyclase activating pathway.
Reactome; R-MMU-170670; Adenylate cyclase inhibitory pathway.
Reactome; R-MMU-418555; G alpha (s) signalling events.
Reactome; R-MMU-418597; G alpha (z) signalling events.
Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-MMU-442720; CREB phosphorylation through the activation of Adenylate Cyclase.
Reactome; R-MMU-5610787; Hedgehog 'off' state.
ChiTaRS; Adcy3; mouse.
PRO; PR:Q8VHH7; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000020654; -.
CleanEx; MM_ADCY3; -.
ExpressionAtlas; Q8VHH7; baseline and differential.
Genevisible; Q8VHH7; MM.
GO; GO:0005929; C:cilium; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0004016; F:adenylate cyclase activity; IMP:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin 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:0007340; P:acrosome reaction; IMP:UniProtKB.
GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:MGI.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0006171; P:cAMP biosynthetic process; IMP:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; IMP:UniProtKB.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
GO; GO:0008355; P:olfactory learning; IMP:UniProtKB.
GO; GO:0007608; P:sensory perception of smell; IDA:MGI.
GO; GO:0007338; P:single fertilization; IMP:UniProtKB.
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; IPR029787; Nucleotide_cyclase.
Pfam; PF16214; AC_N; 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; Calmodulin-binding; cAMP biosynthesis; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Glycoprotein;
Golgi apparatus; Isopeptide bond; Lyase; Magnesium; Manganese;
Membrane; Metal-binding; Nucleotide-binding; Olfaction;
Phosphoprotein; Reference proteome; Repeat; Sensory transduction;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 1145 Adenylate cyclase type 3.
/FTId=PRO_0000195688.
TOPO_DOM 1 79 Cytoplasmic. {ECO:0000255}.
TRANSMEM 80 100 Helical. {ECO:0000255}.
TRANSMEM 105 125 Helical. {ECO:0000255}.
TRANSMEM 139 159 Helical. {ECO:0000255}.
TRANSMEM 173 193 Helical. {ECO:0000255}.
TRANSMEM 226 246 Helical. {ECO:0000255}.
TRANSMEM 381 401 Helical. {ECO:0000255}.
TOPO_DOM 402 631 Cytoplasmic. {ECO:0000255}.
TRANSMEM 632 652 Helical. {ECO:0000255}.
TRANSMEM 663 683 Helical. {ECO:0000255}.
TRANSMEM 707 727 Helical. {ECO:0000255}.
TRANSMEM 753 773 Helical. {ECO:0000255}.
TRANSMEM 774 794 Helical. {ECO:0000255}.
TRANSMEM 834 854 Helical. {ECO:0000255}.
TOPO_DOM 855 1145 Cytoplasmic. {ECO:0000255}.
NP_BIND 324 329 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 366 368 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 1063 1065 ATP. {ECO:0000250|UniProtKB:P26769}.
NP_BIND 1070 1074 ATP. {ECO:0000250|UniProtKB:P26769}.
METAL 324 324 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 324 324 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 325 325 Magnesium 2; via carbonyl oxygen;
catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
METAL 368 368 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 368 368 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
BINDING 412 412 ATP. {ECO:0000250|UniProtKB:P30803}.
BINDING 976 976 ATP. {ECO:0000250|UniProtKB:P26769}.
BINDING 1110 1110 ATP. {ECO:0000250|UniProtKB:P26769}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:O60266}.
MOD_RES 579 579 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1077 1077 Phosphoserine; by CaMK2.
{ECO:0000269|PubMed:9768837}.
CARBOHYD 735 735 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 465 465 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO3).
{ECO:0000250|UniProtKB:P21932}.
MUTAGEN 279 279 M->I: In Jll; dominant allele that
increases enzyme activity, and decreases
fasting insulin levels, fasting leptin
levels, weight gain and fat accumulation
when mice are kept on a high fat diet.
{ECO:0000269|PubMed:25329148}.
CONFLICT 152 152 F -> L (in Ref. 1; AAL59384).
{ECO:0000305}.
CONFLICT 833 835 RLP -> MLL (in Ref. 1; AAL59384).
{ECO:0000305}.
SEQUENCE 1145 AA; 129085 MW; 09195176F4B3D61F CRC64;
MPRNQGFSDP EYSAEYSAEY SVSLPSDPDR GVGRTHEISV RNSGSCLCLP RFMRLTFVPE
SLENLYQTYF KRQRHETLLV LVVFAALFDC YVVVMCAVVF SSDKLAPLMV AGFGLVLDII
LFVLCKKGLL PDRVSRKVVP YLLWLLISAQ IFSYLGLNFS RAHAASDTVG WQAFFVFSFF
ITLPLSLSPI VIISVVSCVV HTLVLGVTVA QQQQDELEGM QLLREILANV FLYLCAIIVG
IMSYYMADRK HRKAFLEARQ SLEVKMNLEE QSQQQENLML SILPKHVADE MLKDMKKDES
QKDQQQFNTM YMYRHENVSI LFADIVGFTQ LSSACSAQEL VKLLNELFAR FDKLAAKYHQ
LRIKILGDCY YCICGLPDYR EDHAVCSILM GLAMVEAISY VREKTKTGVD MRVGVHTGTV
LGGVLGQKRW QYDVWSTDVT VANKMEAGGI PGRVHISQST MDCLKGEFDV EPGDGGSRCD
YLDEKGIETY LIIASKPEVK KTAQNGLNGS AVPNGAPASS KPSSPALIET KEPNGSAHAS
GSTSEEAEEQ EAQADNPSFP NPRRRLRLQD LADRVVDASE DEHELNQLLN EALLERESAQ
VVKKRNTFLL TMRFMDPEME TRYSVEKEKQ SGAAFSCSCV VLFCTAMVEI LIDPWLMTNY
VTFVVGEVLL LILTICSMAA IFPRSFPKKL VAFSSWIDRT RWARNTWAML AIFILVMANV
VDMLSCLQYY MGPYNMTAGM ELDGGCMENP KYYNYVAVLS LIATIMLVQV SHMVKLTLML
LVTGAVTALN LYAWCPVFDE YDHKRFQEKD SPMVALEKMQ VLATPGLNGT DSRLPLVPSK
YSMTVMMFVM MLSFYYFSRH VEKLARTLFL WKIEVHDQKE RVYEMRRWNE ALVTNMLPEH
VARHFLGSKK RDEELYSQSY DEIGVMFASL PNFADFYTEE SINNGGIECL RFLNEIISDF
DSLLDNPKFR VITKIKTIGS TYMAASGVTP DVNTNGFTSS SKEEKSDKER WQHLADLADF
ALAMKDTLTN INNQSFNNFM LRIGMNKGGV LAGVIGARKP HYDIWGNTVN VASRMESTGV
MGNIQVVEET QVILREYGFR FVRRGPIFVK GKGELLTFFL KGRDRPAAFP NGSSVTLPHQ
VVDNP


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U1348r CLIA 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
E1348r ELISA kit 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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