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Adenylate cyclase type 5 (EC 4.6.1.1) (ATP pyrophosphate-lyase 5) (Adenylate cyclase type V) (Adenylyl cyclase 5) (AC5)

 ADCY5_HUMAN             Reviewed;        1261 AA.
O95622; B7Z8A6; Q7RTV7; Q8NFM3;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 3.
12-SEP-2018, entry version 166.
RecName: Full=Adenylate cyclase type 5;
EC=4.6.1.1 {ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:24700542, ECO:0000269|PubMed:26206488};
AltName: Full=ATP pyrophosphate-lyase 5;
AltName: Full=Adenylate cyclase type V;
AltName: Full=Adenylyl cyclase 5;
Short=AC5 {ECO:0000303|PubMed:26206488};
Name=ADCY5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 368-1261 (ISOFORM 1).
TISSUE=Heart;
PubMed=12503609; DOI=10.1081/RRS-120014589;
Ludwig M.G., Seuwen K.;
"Characterization of the human adenylyl cyclase gene family: cDNA,
gene structure, and tissue distribution of the nine isoforms.";
J. Recept. Signal Transduct. 22:79-110(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 560-664 (ISOFORM 1).
TISSUE=Heart muscle;
PubMed=10481931; DOI=10.1016/S0009-8981(99)00067-4;
Raimundo S., Giray J., Volff J.-N., Schwab M., Altenbuchner J.,
Ratge D., Wisser H.;
"Cloning and sequence of partial cDNAs encoding the human type V and
VI adenylyl cyclases and subsequent RNA-quantification in various
tissues.";
Clin. Chim. Acta 285:155-161(1999).
[5]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION,
PHOSPHORYLATION BY RAF1, INTERACTION WITH RAF1, AND ACTIVITY
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]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=24740569; DOI=10.2337/db13-1607;
Hodson D.J., Mitchell R.K., Marselli L., Pullen T.J., Gimeno Brias S.,
Semplici F., Everett K.L., Cooper D.M., Bugliani M., Marchetti P.,
Lavallard V., Bosco D., Piemonti L., Johnson P.R., Hughes S.J., Li D.,
Li W.H., Shapiro A.M., Rutter G.A.;
"ADCY5 couples glucose to insulin secretion in human islets.";
Diabetes 63:3009-3021(2014).
[7]
INTERACTION WITH GNAS; GNB1 AND GNG2, FUNCTION, CATALYTIC ACTIVITY,
ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
PubMed=26206488; DOI=10.1124/mol.115.099556;
Brand C.S., Sadana R., Malik S., Smrcka A.V., Dessauer C.W.;
"Adenylyl cyclase 5 regulation by Gbetagamma involves isoform specific
use of multiple interaction sites.";
Mol. Pharmacol. 88:758-767(2015).
[8]
VARIANT FDFM THR-726.
PubMed=22782511; DOI=10.1001/archneurol.2012.54;
Chen Y.Z., Matsushita M.M., Robertson P., Rieder M., Girirajan S.,
Antonacci F., Lipe H., Eichler E.E., Nickerson D.A., Bird T.D.,
Raskind W.H.;
"Autosomal dominant familial dyskinesia and facial myokymia: single
exome sequencing identifies a mutation in adenylyl cyclase 5.";
Arch. Neurol. 69:630-635(2012).
[9]
VARIANT FDFM TRP-418, CHARACTERIZATION OF VARIANTS FDFM TRP-418 AND
THR-726, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
PubMed=24700542; DOI=10.1002/ana.24119;
Chen Y.Z., Friedman J.R., Chen D.H., Chan G.C., Bloss C.S.,
Hisama F.M., Topol S.E., Carson A.R., Pham P.H., Bonkowski E.S.,
Scott E.R., Lee J.K., Zhang G., Oliveira G., Xu J.,
Scott-Van Zeeland A.A., Chen Q., Levy S., Topol E.J., Storm D.,
Swanson P.D., Bird T.D., Schork N.J., Raskind W.H., Torkamani A.;
"Gain-of-function ADCY5 mutations in familial dyskinesia with facial
myokymia.";
Ann. Neurol. 75:542-549(2014).
-!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP
in response to G-protein signaling (PubMed:15385642,
PubMed:26206488, PubMed:24700542). Mediates signaling downstream
of ADRB1 (PubMed:24700542). 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 (PubMed:24740569). {ECO:0000269|PubMed:15385642,
ECO:0000269|PubMed:24700542, ECO:0000269|PubMed:24740569,
ECO:0000269|PubMed:26206488}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
{ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:24700542,
ECO:0000269|PubMed:26206488}.
-!- 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};
Note=Binds 2 magnesium ions per subunit. Is also active with
manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
-!- ACTIVITY REGULATION: Activated by forskolin (PubMed:24700542).
Activated by GNAS. Activity is further increased by interaction
with the G-protein beta and gamma subunit complex formed by GNB1
and GNG2 (PubMed:26206488). 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
(PubMed:15385642). {ECO:0000250|UniProtKB:P30803,
ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:26206488}.
-!- SUBUNIT: Interacts with GNAS, GNB1 and GNG2 (PubMed:26206488).
Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2 (By
similarity). Interacts with RAF1 (PubMed:15385642).
{ECO:0000250|UniProtKB:P84309, ECO:0000269|PubMed:15385642,
ECO:0000269|PubMed:26206488}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15385642,
ECO:0000305|PubMed:26206488}; Multi-pass membrane protein. Cell
projection, cilium {ECO:0000250|UniProtKB:P84309}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O95622-1; Sequence=Displayed;
Name=2;
IsoId=O95622-2; Sequence=VSP_042914, VSP_042915;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in pancreas islets (at protein
level). Detected in pancreas islets.
{ECO:0000269|PubMed:24740569}.
-!- 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:0000269|PubMed:15385642}.
-!- DISEASE: Dyskinesia, familial, with facial myokymia (FDFM)
[MIM:606703]: A disorder characterized by predominantly perioral
and periorbital myokymia, and face, neck and upper limb
dystonic/choreic movements. Initially paroxysmal and worsened by
stress, the dyskinetic episodes become nearly constant by the end
of the third decade of life, but in some individuals, they may
diminish in frequency and severity at older ages.
{ECO:0000269|PubMed:22782511, ECO:0000269|PubMed:24700542}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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EMBL; AK303070; BAH13892.1; -; mRNA.
EMBL; AC025571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF497517; AAM94374.1; -; mRNA.
EMBL; U65473; AAD00121.1; -; mRNA.
EMBL; BK000371; DAA00057.1; -; mRNA.
CCDS; CCDS3022.1; -. [O95622-1]
CCDS; CCDS56274.1; -. [O95622-2]
RefSeq; NP_001186571.1; NM_001199642.1. [O95622-2]
RefSeq; NP_899200.1; NM_183357.2. [O95622-1]
UniGene; Hs.593292; -.
ProteinModelPortal; O95622; -.
SMR; O95622; -.
BioGrid; 106624; 14.
STRING; 9606.ENSP00000419361; -.
BindingDB; O95622; -.
ChEMBL; CHEMBL3189; -.
DrugBank; DB02587; Colforsin.
GuidetoPHARMACOLOGY; 1282; -.
iPTMnet; O95622; -.
PhosphoSitePlus; O95622; -.
BioMuta; ADCY5; -.
EPD; O95622; -.
MaxQB; O95622; -.
PaxDb; O95622; -.
PeptideAtlas; O95622; -.
PRIDE; O95622; -.
ProteomicsDB; 50954; -.
ProteomicsDB; 50955; -. [O95622-2]
DNASU; 111; -.
Ensembl; ENST00000309879; ENSP00000308685; ENSG00000173175. [O95622-2]
Ensembl; ENST00000462833; ENSP00000419361; ENSG00000173175. [O95622-1]
GeneID; 111; -.
KEGG; hsa:111; -.
UCSC; uc003egh.3; human. [O95622-1]
CTD; 111; -.
DisGeNET; 111; -.
EuPathDB; HostDB:ENSG00000173175.14; -.
GeneCards; ADCY5; -.
H-InvDB; HIX0003612; -.
HGNC; HGNC:236; ADCY5.
HPA; HPA017730; -.
HPA; HPA077682; -.
MalaCards; ADCY5; -.
MIM; 600293; gene.
MIM; 606703; phenotype.
neXtProt; NX_O95622; -.
OpenTargets; ENSG00000173175; -.
Orphanet; 324588; Familial dyskinesia and facial myokymia.
PharmGKB; PA24563; -.
eggNOG; KOG3619; Eukaryota.
eggNOG; COG2114; LUCA.
GeneTree; ENSGT00760000119042; -.
HOGENOM; HOG000006941; -.
HOVERGEN; HBG050458; -.
InParanoid; O95622; -.
KO; K08045; -.
OMA; VRSKMNS; -.
OrthoDB; EOG091G05JR; -.
PhylomeDB; O95622; -.
TreeFam; TF313845; -.
BRENDA; 4.6.1.1; 2681.
Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
Reactome; R-HSA-163615; PKA activation.
Reactome; R-HSA-164378; PKA activation in glucagon signalling.
Reactome; R-HSA-170660; Adenylate cyclase activating pathway.
Reactome; R-HSA-170670; Adenylate cyclase inhibitory pathway.
Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-418597; G alpha (z) signalling events.
Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-HSA-5610787; Hedgehog 'off' state.
SIGNOR; O95622; -.
ChiTaRS; ADCY5; human.
GeneWiki; ADCY5; -.
GenomeRNAi; 111; -.
PRO; PR:O95622; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000173175; Expressed in 139 organ(s), highest expression level in lower esophagus.
CleanEx; HS_ADCY5; -.
ExpressionAtlas; O95622; baseline and differential.
Genevisible; O95622; HS.
GO; GO:0005929; C:cilium; 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:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
GO; GO:0008179; F:adenylate cyclase binding; ISS:BHF-UCL.
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:0046982; F:protein heterodimerization activity; ISS:BHF-UCL.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0001973; P:adenosine receptor signaling pathway; IEA:Ensembl.
GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IEA:Ensembl.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IEA:Ensembl.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; IDA:UniProtKB.
GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:UniProtKB.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
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;
Alternative splicing; ATP-binding; cAMP biosynthesis; Cell membrane;
Cell projection; Cilium; Complete proteome; Disease mutation;
Glycoprotein; Lyase; Magnesium; Membrane; Metal-binding; Methylation;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Transmembrane; Transmembrane helix.
CHAIN 1 1261 Adenylate cyclase type 5.
/FTId=PRO_0000195694.
TOPO_DOM 1 195 Cytoplasmic. {ECO:0000255}.
TRANSMEM 196 216 Helical. {ECO:0000255}.
TRANSMEM 242 262 Helical. {ECO:0000255}.
TRANSMEM 268 288 Helical. {ECO:0000255}.
TRANSMEM 299 319 Helical. {ECO:0000255}.
TRANSMEM 325 345 Helical. {ECO:0000255}.
TRANSMEM 374 394 Helical. {ECO:0000255}.
TOPO_DOM 395 769 Cytoplasmic. {ECO:0000255}.
TRANSMEM 770 790 Helical. {ECO:0000255}.
TRANSMEM 792 812 Helical. {ECO:0000255}.
TRANSMEM 836 856 Helical. {ECO:0000255}.
TOPO_DOM 857 909 Extracellular. {ECO:0000255}.
TRANSMEM 910 930 Helical. {ECO:0000255}.
TRANSMEM 935 955 Helical. {ECO:0000255}.
TRANSMEM 984 1004 Helical. {ECO:0000255}.
TOPO_DOM 1005 1261 Cytoplasmic. {ECO:0000255}.
DOMAIN 469 596 Guanylate cyclase 1.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
DOMAIN 1071 1210 Guanylate cyclase 2.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
NP_BIND 474 479 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 516 518 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 1197 1199 ATP. {ECO:0000250|UniProtKB:P26769}.
NP_BIND 1204 1208 ATP. {ECO:0000250|UniProtKB:P26769}.
METAL 474 474 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 474 474 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 475 475 Magnesium 2; via carbonyl oxygen;
catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
METAL 518 518 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 518 518 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
BINDING 562 562 ATP. {ECO:0000250|UniProtKB:P30803}.
BINDING 1123 1123 ATP. {ECO:0000250|UniProtKB:P26769}.
BINDING 1244 1244 ATP. {ECO:0000250|UniProtKB:P26769}.
MOD_RES 23 23 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P84309}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000250|UniProtKB:P84309}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000250|UniProtKB:P84309}.
MOD_RES 666 666 Phosphoserine.
{ECO:0000250|UniProtKB:O43306}.
MOD_RES 754 754 Phosphoserine.
{ECO:0000250|UniProtKB:Q03343}.
MOD_RES 1011 1011 Phosphothreonine.
{ECO:0000250|UniProtKB:Q03343}.
CARBOHYD 870 870 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 887 887 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 28 MSGSKSVSPPGYAAQKTAAPAPRGGPEH -> MKSQKEGCC
SRGDLSIQTGPGGEWAPRR (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042914.
VAR_SEQ 29 378 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042915.
VARIANT 418 418 R -> W (in FDFM; increases cAMP
production upon activation of ADRB1;
dbSNP:rs864309483).
{ECO:0000269|PubMed:24700542}.
/FTId=VAR_073778.
VARIANT 726 726 A -> T (in FDFM; increases cAMP
production upon activation of ADRB1;
dbSNP:rs796065306).
{ECO:0000269|PubMed:22782511,
ECO:0000269|PubMed:24700542}.
/FTId=VAR_068821.
SEQUENCE 1261 AA; 138908 MW; C50492A0B053694F CRC64;
MSGSKSVSPP GYAAQKTAAP APRGGPEHRS AWGEADSRAN GYPHAPGGSA RGSTKKPGGA
VTPQQQQRLA SRWRSDDDDD PPLSGDDPLA GGFGFSFRSK SAWQERGGDD CGRGSRRQRR
GAASGGSTRA PPAGGGGGSA AAAASAGGTE VRPRSVEVGL EERRGKGRAA DELEAGAVEG
GEGSGDGGSS ADSGSGAGPG AVLSLGACCL ALLQIFRSKK FPSDKLERLY QRYFFRLNQS
SLTMLMAVLV LVCLVMLAFH AARPPLQLPY LAVLAAAVGV ILIMAVLCNR AAFHQDHMGL
ACYALIAVVL AVQVVGLLLP QPRSASEGIW WTVFFIYTIY TLLPVRMRAA VLSGVLLSAL
HLAIALRTNA QDQFLLKQLV SNVLIFSCTN IVGVCTHYPA EVSQRQAFQE TRECIQARLH
SQRENQQQER LLLSVLPRHV AMEMKADINA KQEDMMFHKI YIQKHDNVSI LFADIEGFTS
LASQCTAQEL VMTLNELFAR FDKLAAENHC LRIKILGDCY YCVSGLPEAR ADHAHCCVEM
GMDMIEAISL VREVTGVNVN MRVGIHSGRV HCGVLGLRKW QFDVWSNDVT LANHMEAGGK
AGRIHITKAT LNYLNGDYEV EPGCGGERNA YLKEHSIETF LILRCTQKRK EEKAMIAKMN
RQRTNSIGHN PPHWGAERPF YNHLGGNQVS KEMKRMGFED PKDKNAQESA NPEDEVDEFL
GRAIDARSID RLRSEHVRKF LLTFREPDLE KKYSKQVDDR FGAYVACASL VFLFICFVQI
TIVPHSIFML SFYLTCSLLL TLVVFVSVIY SCVKLFPSPL QTLSRKIVRS KMNSTLVGVF
TITLVFLAAF VNMFTCNSRD LLGCLAQEHN ISASQVNACH VAESAVNYSL GDEQGFCGSP
WPNCNFPEYF TYSVLLSLLA CSVFLQISCI GKLVLMLAIE LIYVLIVEVP GVTLFDNADL
LVTANAIDFF NNGTSQCPEH ATKVALKVVT PIIISVFVLA LYLHAQQVES TARLDFLWKL
QATEEKEEME ELQAYNRRLL HNILPKDVAA HFLARERRND ELYYQSCECV AVMFASIANF
SEFYVELEAN NEGVECLRLL NEIIADFDEI ISEDRFRQLE KIKTIGSTYM AASGLNDSTY
DKVGKTHIKA LADFAMKLMD QMKYINEHSF NNFQMKIGLN IGPVVAGVIG ARKPQYDIWG
NTVNVASRMD STGVPDRIQV TTDMYQVLAA NTYQLECRGV VKVKGKGEMM TYFLNGGPPL
S


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