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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_RAT               Reviewed;        1144 AA.
P21932;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
22-NOV-2017, entry version 140.
RecName: Full=Adenylate cyclase type 3;
EC=4.6.1.1 {ECO:0000269|PubMed:1633161, ECO:0000269|PubMed:2255909, ECO:0000269|PubMed:24363043};
AltName: Full=ATP pyrophosphate-lyase 3;
AltName: Full=Adenylate cyclase type III {ECO:0000303|PubMed:2255909};
Short=AC-III;
AltName: Full=Adenylate cyclase, olfactive type;
AltName: Full=Adenylyl cyclase 3;
Short=AC3;
Name=Adcy3;
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], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
ENZYME REGULATION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
TISSUE=Olfactory epithelium;
PubMed=2255909; DOI=10.1126/science.2255909;
Bakalyar H.A., Reed R.R.;
"Identification of a specialized adenylyl cyclase that may mediate
odorant detection.";
Science 250:1403-1406(1990).
[2]
CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, AND SUBCELLULAR
LOCATION.
PubMed=1633161; DOI=10.1021/bi00143a019;
Choi E.J., Xia Z., Storm D.R.;
"Stimulation of the type III olfactory adenylyl cyclase by calcium and
calmodulin.";
Biochemistry 31:6492-6498(1992).
[3]
SUBCELLULAR LOCATION.
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).
[4]
CATALYTIC ACTIVITY, FUNCTION, AND ENZYME REGULATION.
PubMed=24363043; DOI=10.1007/s00210-013-0950-4;
Bogard A.S., Birg A.V., Ostrom R.S.;
"Non-raft adenylyl cyclase 2 defines a cAMP signaling compartment that
selectively regulates IL-6 expression in airway smooth muscle cells:
differential regulation of gene expression by AC isoforms.";
Naunyn Schmiedebergs Arch. Pharmacol. 387:329-339(2014).
[5]
SUMOYLATION, MUTAGENESIS OF LYS-465, SUBCELLULAR LOCATION, 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:2255909,
PubMed:1633161, PubMed:24363043). Participates in signaling
cascades triggered by odorant receptors via its function in cAMP
biosynthesis (PubMed:2255909). Required for the perception of
odorants. Required for normal sperm motility and normal male
fertility. Plays a role in regulating insulin levels and body fat
accumulation in response to a high fat diet (By similarity).
{ECO:0000250|UniProtKB:Q8VHH7, ECO:0000269|PubMed:1633161,
ECO:0000269|PubMed:2255909, ECO:0000269|PubMed:24363043}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
{ECO:0000269|PubMed:1633161, ECO:0000269|PubMed:2255909,
ECO:0000269|PubMed:24363043}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:2255909};
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:2255909,
PubMed:1633161, PubMed:24363043). After forskolin treatment,
activity is further increased by calcium/calmodulin
(PubMed:1633161). In the absence of forskolin, calcium/calmodulin
has little effect on enzyme activity (PubMed:1633161).
{ECO:0000269|PubMed:1633161, ECO:0000269|PubMed:2255909,
ECO:0000269|PubMed:24363043}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15705663,
ECO:0000269|PubMed:1633161}; Multi-pass membrane protein
{ECO:0000305}. Golgi apparatus {ECO:0000269|PubMed:15705663}. Cell
projection, cilium {ECO:0000269|PubMed:2255909,
ECO:0000269|PubMed:25908845}. Cytoplasm
{ECO:0000250|UniProtKB:O60266}.
-!- TISSUE SPECIFICITY: Detected on cilia on the olfactory epithelium
(at protein level) (PubMed:2255909, PubMed:25908845). Detected on
cilia on the olfactory epithelium. {ECO:0000269|PubMed:2255909}.
-!- 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:2255909}.
-!- PTM: Sumoylated. Sumoylation is required for targeting ot
olfactory cilia. {ECO:0000269|PubMed:25908845}.
-!- PTM: Rapidly phosphorylated after stimulation by odorants or
forskolin. Phosphorylation by CaMK2 at Ser-1076 down-regulates
enzyme activity. {ECO:0000250|UniProtKB:Q8VHH7}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
-----------------------------------------------------------------------
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EMBL; M55075; AAA40677.1; -; mRNA.
PIR; A39833; A39833.
RefSeq; NP_570135.2; NM_130779.2.
UniGene; Rn.87800; -.
ProteinModelPortal; P21932; -.
SMR; P21932; -.
BioGrid; 249093; 1.
STRING; 10116.ENSRNOP00000005389; -.
BindingDB; P21932; -.
ChEMBL; CHEMBL2095179; -.
PhosphoSitePlus; P21932; -.
PaxDb; P21932; -.
PRIDE; P21932; -.
GeneID; 64508; -.
KEGG; rno:64508; -.
CTD; 109; -.
RGD; 71009; Adcy3.
eggNOG; KOG3619; Eukaryota.
eggNOG; COG2114; LUCA.
HOGENOM; HOG000006941; -.
HOVERGEN; HBG050458; -.
InParanoid; P21932; -.
KO; K08043; -.
PhylomeDB; P21932; -.
BRENDA; 4.6.1.1; 5301.
PRO; PR:P21932; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005929; C:cilium; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008294; F:calcium- and calmodulin-responsive adenylate cyclase activity; IDA:RGD.
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; ISS:UniProtKB.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; IDA:UniProtKB.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0007143; P:female meiotic nuclear division; IEP:RGD.
GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
GO; GO:0008355; P:olfactory learning; ISS:UniProtKB.
GO; GO:0007608; P:sensory perception of smell; IDA:RGD.
GO; GO:0007338; P:single fertilization; ISS: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 1144 Adenylate cyclase type 3.
/FTId=PRO_0000195689.
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 402 630 Cytoplasmic. {ECO:0000255}.
TRANSMEM 631 651 Helical. {ECO:0000255}.
TRANSMEM 662 682 Helical. {ECO:0000255}.
TRANSMEM 706 726 Helical. {ECO:0000255}.
TRANSMEM 755 775 Helical. {ECO:0000255}.
TRANSMEM 777 797 Helical. {ECO:0000255}.
TRANSMEM 833 853 Helical. {ECO:0000255}.
TOPO_DOM 854 1144 Cytoplasmic. {ECO:0000255}.
NP_BIND 324 329 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 366 368 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 1062 1064 ATP. {ECO:0000250|UniProtKB:P26769}.
NP_BIND 1069 1073 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 975 975 ATP. {ECO:0000250|UniProtKB:P26769}.
BINDING 1109 1109 ATP. {ECO:0000250|UniProtKB:P26769}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000250|UniProtKB:O60266}.
MOD_RES 578 578 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VHH7}.
MOD_RES 1076 1076 Phosphoserine; by CaMK2.
{ECO:0000250|UniProtKB:Q8VHH7}.
CARBOHYD 734 734 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 465 465 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO3).
{ECO:0000269|PubMed:25908845}.
MUTAGEN 465 465 K->R: Abolishes sumoylation. Abolishes
location at cilia in the olfactory
epithelium.
{ECO:0000269|PubMed:25908845}.
SEQUENCE 1144 AA; 128936 MW; 21098D028DDBAB55 CRC64;
MTEDQGFSDP EYSAEYSAEY SVSLPSDPDR GVGRTHEISV RNSGSCLCLP RFMRLTFVPE
SLENLYQTYF KRQRHETLLV LVVFAALFDC YVVVMCAVVF SSDKLAPLMV AGVGLVLDII
LFVLCKKGLL PDRVSRKVVP YLLWLLITAQ 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 ALPNGAPASK PSSPALIETK EPNGSAHASG
STSEEAEEQE AQADNPSFPN PRRRLRLQDL ADRVVDASED EHELNQLLNE ALLERESAQV
VKKRNTFLLT MRFMDPEMET RYSVEKEKQS GAAFSCSCVV LFCTAMVEIL IDPWLMTNYV
TFVVGEVLLL ILTICSMAAI FPRAFPKKLV AFSSWIDRTR WARNTWAMLA IFILVMANVV
DMLSCLQYYM GPYNVTTGIE LDGGCMENPK YYNYVAVLSL IATIMLVQVS HMVKLTLMLL
VTGAVTAINL YAWCPVFDEY DHKRFQEKDS PMVALEKMQV LSTPGLNGTD SRLPLVPSKY
SMTVMMFVMM LSFYYFSRHV EKLARTLFLW KIEVHDQKER VYEMRRWNEA LVTNMLPEHV
ARHFLGSKKR DEELYSQSYD EIGVMFASLP NFADFYTEES INNGGIECLR FLNEIISDFD
SLLDNPKFRV ITKIKTIGST YMAASGVTPD VNTNGFTSSS KEEKSDKERW QHLADLADFA
LAMKDTLTNI NNQSFNNFML RIGMNKGGVL AGVIGARKPH YDIWGNTVNV ASRMESTGVM
GNIQVVEETQ VILREYGFRF VRRGPIFVKG KGELLTFFLK GRDRPAAFPN GSSVTLPHQV
VDNP


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