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Adenylate cyclase type 5 (EC 4.6.1.1) (ATP pyrophosphate-lyase 5) (Adenylate cyclase type V) (Adenylyl cyclase 5)

 ADCY5_RAT               Reviewed;        1262 AA.
Q04400;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
23-MAY-2018, entry version 141.
RecName: Full=Adenylate cyclase type 5;
EC=4.6.1.1 {ECO:0000269|PubMed:1409703};
AltName: Full=ATP pyrophosphate-lyase 5;
AltName: Full=Adenylate cyclase type V;
AltName: Full=Adenylyl cyclase 5;
Name=Adcy5;
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].
STRAIN=Sprague-Dawley; TISSUE=Heart, Kidney, and Liver;
Premont R.T.;
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 164-1262, CATALYTIC ACTIVITY, FUNCTION,
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).
-!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP
in response to G-protein signaling (PubMed:1409703). 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. {ECO:0000250|UniProtKB:O95622,
ECO:0000269|PubMed:1409703}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
{ECO:0000269|PubMed:1409703}.
-!- 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. 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 (By similarity). Phosphorylation by RAF1
results in its activation (By similarity).
{ECO:0000250|UniProtKB:O95622, ECO:0000250|UniProtKB:P30803}.
-!- SUBUNIT: Interacts with GNAS, 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}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P30803}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P30803}. Cell projection, cilium
{ECO:0000250|UniProtKB:P84309}.
-!- TISSUE SPECIFICITY: Detected in brain and kidney.
{ECO:0000269|PubMed:1409703}.
-!- 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:P30803}.
-!- PTM: Phosphorylated by RAF1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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EMBL; M96159; AAB39764.1; -; mRNA.
RefSeq; NP_072122.1; NM_022600.1.
UniGene; Rn.6278; -.
ProteinModelPortal; Q04400; -.
SMR; Q04400; -.
BioGrid; 249116; 1.
STRING; 10116.ENSRNOP00000046488; -.
BindingDB; Q04400; -.
ChEMBL; CHEMBL2880; -.
SwissPalm; Q04400; -.
PaxDb; Q04400; -.
PRIDE; Q04400; -.
GeneID; 64532; -.
KEGG; rno:64532; -.
UCSC; RGD:71014; rat.
CTD; 111; -.
RGD; 71014; Adcy5.
eggNOG; KOG3619; Eukaryota.
eggNOG; COG2114; LUCA.
HOGENOM; HOG000006941; -.
HOVERGEN; HBG050458; -.
InParanoid; Q04400; -.
KO; K08045; -.
BRENDA; 4.6.1.1; 5301.
PRO; PR:Q04400; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005929; C:cilium; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0004016; F:adenylate cyclase activity; IDA:RGD.
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:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IMP:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0006171; P:cAMP biosynthetic process; IDA:RGD.
GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0007507; P:heart development; IEP:RGD.
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:0043278; P:response to morphine; IEP:RGD.
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; Membrane;
Metal-binding; Methylation; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix.
CHAIN 1 1262 Adenylate cyclase type 5.
/FTId=PRO_0000195697.
TOPO_DOM 1 242 Cytoplasmic. {ECO:0000255}.
TRANSMEM 243 263 Helical. {ECO:0000255}.
TRANSMEM 269 289 Helical. {ECO:0000255}.
TRANSMEM 300 320 Helical. {ECO:0000255}.
TRANSMEM 326 346 Helical. {ECO:0000255}.
TRANSMEM 351 371 Helical. {ECO:0000255}.
TRANSMEM 375 395 Helical. {ECO:0000255}.
TOPO_DOM 396 763 Cytoplasmic. {ECO:0000255}.
TRANSMEM 764 784 Helical. {ECO:0000255}.
TRANSMEM 790 810 Helical. {ECO:0000255}.
TRANSMEM 837 857 Helical. {ECO:0000255}.
TOPO_DOM 858 910 Extracellular. {ECO:0000255}.
TRANSMEM 911 931 Helical. {ECO:0000255}.
TRANSMEM 936 956 Helical. {ECO:0000255}.
TRANSMEM 985 1005 Helical. {ECO:0000255}.
TOPO_DOM 1006 1262 Cytoplasmic. {ECO:0000255}.
DOMAIN 470 597 Guanylate cyclase 1.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
DOMAIN 1072 1211 Guanylate cyclase 2.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
NP_BIND 475 480 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 517 519 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 1198 1200 ATP. {ECO:0000250|UniProtKB:P26769}.
NP_BIND 1205 1209 ATP. {ECO:0000250|UniProtKB:P26769}.
COMPBIAS 64 67 Poly-Gln.
COMPBIAS 141 147 Poly-Ala.
METAL 475 475 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 475 475 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 476 476 Magnesium 2; via carbonyl oxygen;
catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
METAL 519 519 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 519 519 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
BINDING 563 563 ATP. {ECO:0000250|UniProtKB:P30803}.
BINDING 1124 1124 ATP. {ECO:0000250|UniProtKB:P26769}.
BINDING 1245 1245 ATP. {ECO:0000250|UniProtKB:P26769}.
MOD_RES 23 23 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P84309}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000250|UniProtKB:P84309}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000250|UniProtKB:P84309}.
MOD_RES 667 667 Phosphoserine.
{ECO:0000250|UniProtKB:O43306}.
MOD_RES 755 755 Phosphoserine.
{ECO:0000250|UniProtKB:Q03343}.
MOD_RES 1012 1012 Phosphothreonine.
{ECO:0000250|UniProtKB:Q03343}.
CARBOHYD 871 871 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 888 888 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 973 973 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 1262 AA; 139179 MW; 8B147E201C5DF601 CRC64;
MSGSKSVSPP GYAAQTAASP APRGGPEHRA AWGEADSRAN GYPHAPGGST RGSTKRSGGA
VTPQQQQRLA SRWRGGDDDE DPPLSGDDPL VGGFGFSFRS KSAWQERGGD DGGRGSRRQR
RGAAGGGSTR APPAGGSGSS AAAAAAAGGT EVRPRSVEVG LEERRGKGRA AEELEPGTGT
VEDGDGSEDG GSSVASGSGT GTVLSLGACC LALLQIFRSK KFPSDKLERL YQRYFFRLNQ
SSLTMLMAVL VLVCLVMLAF HAARPPLQVV YLAVLAAAVG VILIMAVLCN RAAFHQDHMG
LACYALIAVV LAVQVVGLLL PQPRSASEGI WWTVFFIYTI YTLLPVRMRA AVLSGVLLSA
LHLAISLHTN AQDQFLLKQL VSNVLIFSCT NIVGVCTHYP AEVSQRQAFQ ETRECIQARL
HSQRENQQQE RLLLSVLPRH VAMEMKADIN AKQEDMMFHK IYIQKHDNVS ILFADIEGFT
SLASQCTAQE LVMTLNELFA RFDKLAAENH CLRIKILGDC YYCVSGLPEA RADHAHCCVE
MGMDMIEAIS SVREVTGVNV NMRVGIHSGR VHCGVLGLRK WQFDVWSNDV TLANHMEAGG
KAGRIHITKA TLNYLNGDYE VEPGCGGERN AYLKEHSIET FLILRCTQKR KEEKAMIAKM
NRQRTNSIGH NPPHWGAERP FYNHLGGNQV SKEMKRMGFE DPKDKNAQES ANPEDEVDEF
LGRAIDARSI DRLRSEHVRK FLLTFREPDL EKKYSKQVDD RFGAYVACAS LVFLFICFVQ
ITIVPHSLFM LSFYLSCFLL LALVVFISVI YACVKLFPTP LQTLSRKIVR SKKNSTLVGV
FTITLVFLSA FVNMFMCNSK NLVGCLAEEH NITVNQVNAC HVMESAFNYS LGDEQGFCGS
PQSNCNFPEY FTYSVLLSLL ACSVFLQISC IGKLVLMLAI ELIYVLIVEV PGVTLFDNAD
LLVTANAIDF SNNGTSQCPE HATKVALKVV TPIIISVFVL ALYLHAQQVE STARLDFLWK
LQATEEKEEM EELQAYNRRL LHNILPKDVA AHFLARERRN DELYYQSCEC VAVMFASIAN
FSEFYVELEA NNEGVECLRL LNEIIADFDE IISEDRFRQL EKIKTIGSTY MAASGLNDST
YDKAGKTHIK ALADFAMKLM DQMKYINEHS FNNFQMKIGL NIGPVVAGVI GARKPQYDIW
GNTVNVASRM DSTGVPDRIQ VTTDMYQVLA ANTYQLECRG VVKVKGKGEM MTYFLNGGPP
LS


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