ADCY2_RAT
ID ADCY2_RAT Reviewed; 1090 AA.
AC P26769;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Adenylate cyclase type 2;
DE EC=4.6.1.1 {ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:1719547, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:21596131};
DE AltName: Full=ATP pyrophosphate-lyase 2;
DE AltName: Full=Adenylate cyclase type II;
DE AltName: Full=Adenylyl cyclase 2;
DE Short=AC2 {ECO:0000303|PubMed:24363043};
GN Name=Adcy2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1719547; DOI=10.1073/pnas.88.22.10173;
RA Feinstein P.G., Schrader K.A., Bakalyar H.A., Tang W.J., Krupinski J.,
RA Gilman A.G., Reed R.R.;
RT "Molecular cloning and characterization of a Ca2+/calmodulin-insensitive
RT adenylyl cyclase from rat brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10173-10177(1991).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=7761832; DOI=10.1126/science.7761832;
RA Chen J., DeVivo M., Dingus J., Harry A., Li J., Sui J., Carty D.J.,
RA Blank J.L., Exton J.H., Stoffel R.H.;
RT "A region of adenylyl cyclase 2 critical for regulation by G protein beta
RT gamma subunits.";
RL Science 268:1166-1169(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH THE G PROTEIN BETA AND GAMMA SUBUNIT COMPLEX.
RX PubMed=21596131; DOI=10.1016/j.cellsig.2011.05.002;
RA Boran A.D., Chen Y., Iyengar R.;
RT "Identification of new Gbetagamma interaction sites in adenylyl cyclase
RT 2.";
RL Cell. Signal. 23:1489-1495(2011).
RN [4]
RP PHOSPHORYLATION AT SER-490 AND SER-543, MUTAGENESIS OF SER-490 AND SER-543,
RP CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
RX PubMed=22906005; DOI=10.1042/bj20120279;
RA Shen J.X., Wachten S., Halls M.L., Everett K.L., Cooper D.M.;
RT "Muscarinic receptors stimulate AC2 by novel phosphorylation sites, whereas
RT Gbetagamma subunits exert opposing effects depending on the G-protein
RT source.";
RL Biochem. J. 447:393-405(2012).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=24363043; DOI=10.1007/s00210-013-0950-4;
RA Bogard A.S., Birg A.V., Ostrom R.S.;
RT "Non-raft adenylyl cyclase 2 defines a cAMP signaling compartment that
RT selectively regulates IL-6 expression in airway smooth muscle cells:
RT differential regulation of gene expression by AC isoforms.";
RL Naunyn Schmiedebergs Arch. Pharmacol. 387:329-339(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 871-1090 IN COMPLEX WITH
RP FORSKOLIN.
RX PubMed=9069282; DOI=10.1038/386247a0;
RA Zhang G., Liu Y., Ruoho A.E., Hurley J.H.;
RT "Structure of the adenylyl cyclase catalytic core.";
RL Nature 386:247-253(1997).
RN [8]
RP ERRATUM OF PUBMED:9069282.
RA Zhang G., Liu Y., Ruoho A.E., Hurley J.H.;
RL Nature 388:204-204(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH GNAS, INTERACTION WITH GNAS, AND DOMAIN.
RX PubMed=9417641; DOI=10.1126/science.278.5345.1907;
RA Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.;
RT "Crystal structure of the catalytic domains of adenylyl cyclase in a
RT complex with Gsalpha.GTPgammaS.";
RL Science 278:1907-1916(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH GNAS AND ATP ANALOGS, INTERACTION WITH GNAS, DOMAIN, CATALYTIC
RP ACTIVITY, FUNCTION, AND COFACTOR.
RX PubMed=10427002; DOI=10.1126/science.285.5428.756;
RA Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G.,
RA Sprang S.R.;
RT "Two-metal-ion catalysis in adenylyl cyclase.";
RL Science 285:756-760(1999).
RN [11] {ECO:0007744|PDB:1CS4, ECO:0007744|PDB:1CUL}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 874-1081 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH GNAS; MAGNESIUM AND ATP ANALOGS, INTERACTION WITH GNAS,
RP DOMAIN, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=11087399; DOI=10.1021/bi0015562;
RA Tesmer J.J., Dessauer C.W., Sunahara R.K., Murray L.D., Johnson R.A.,
RA Gilman A.G., Sprang S.R.;
RT "Molecular basis for P-site inhibition of adenylyl cyclase.";
RL Biochemistry 39:14464-14471(2000).
RN [12] {ECO:0007744|PDB:1TL7, ECO:0007744|PDB:1U0H}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH GNAS AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, INTERACTION
RP WITH GNAS, AND DOMAIN.
RX PubMed=15591060; DOI=10.1074/jbc.m409076200;
RA Mou T.C., Gille A., Fancy D.A., Seifert R., Sprang S.R.;
RT "Structural basis for the inhibition of mammalian membrane adenylyl cyclase
RT by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate.";
RL J. Biol. Chem. 280:7253-7261(2005).
RN [13] {ECO:0007744|PDB:2GVD, ECO:0007744|PDB:2GVZ}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH GNAS AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP INTERACTION WITH GNAS, AND DOMAIN.
RX PubMed=16766715; DOI=10.1124/mol.106.026427;
RA Mou T.C., Gille A., Suryanarayana S., Richter M., Seifert R., Sprang S.R.;
RT "Broad specificity of mammalian adenylyl cyclase for interaction with
RT 2',3'-substituted purine- and pyrimidine nucleotide inhibitors.";
RL Mol. Pharmacol. 70:878-886(2006).
RN [14] {ECO:0007744|PDB:3C14, ECO:0007744|PDB:3C15, ECO:0007744|PDB:3C16, ECO:0007744|PDB:3MAA}
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH GNAS; FORSKOLIN; MAGNESIUM IONS AND ATP ANALOG, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GNAS, AND DOMAIN.
RX PubMed=19243146; DOI=10.1021/bi802122k;
RA Mou T.C., Masada N., Cooper D.M., Sprang S.R.;
RT "Structural basis for inhibition of mammalian adenylyl cyclase by
RT calcium.";
RL Biochemistry 48:3387-3397(2009).
CC -!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP in
CC response to G-protein signaling (PubMed:22906005, PubMed:24363043,
CC PubMed:10427002, PubMed:1719547, PubMed:7761832, PubMed:21596131,
CC PubMed:11087399, PubMed:15591060, PubMed:19243146, PubMed:16766715).
CC Down-stream signaling cascades mediate changes in gene expression
CC patterns and lead to increased IL6 production (PubMed:24363043).
CC Functions in signaling cascades downstream of the muscarinic
CC acetylcholine receptors (PubMed:22906005).
CC {ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399,
CC ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:16766715,
CC ECO:0000269|PubMed:1719547, ECO:0000269|PubMed:19243146,
CC ECO:0000269|PubMed:21596131, ECO:0000269|PubMed:22906005,
CC ECO:0000269|PubMed:24363043, ECO:0000269|PubMed:7761832}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC Evidence={ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399,
CC ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:16766715,
CC ECO:0000269|PubMed:1719547, ECO:0000269|PubMed:19243146,
CC ECO:0000269|PubMed:21596131, ECO:0000269|PubMed:22906005,
CC ECO:0000269|PubMed:24363043, ECO:0000269|PubMed:7761832};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399,
CC ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:1719547,
CC ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:7761832};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399,
CC ECO:0000269|PubMed:16766715};
CC Note=Binds 2 magnesium ions per subunit. Is also active with manganese
CC (in vitro). {ECO:0000269|PubMed:16766715, ECO:0000305|PubMed:10427002};
CC -!- ACTIVITY REGULATION: Activated by forskolin (PubMed:1719547,
CC PubMed:22906005, PubMed:24363043). Is not activated by calmodulin
CC (PubMed:1719547). Inhibited by calcium ions, already at micromolar
CC concentration. Activated by the G protein alpha subunit GNAS
CC (PubMed:1719547, PubMed:7761832, PubMed:21596131). Activated by the G
CC protein beta and gamma subunit complex (PubMed:7761832,
CC PubMed:21596131, PubMed:22906005). Phosphorylation by RAF1 results in
CC its activation (By similarity). Phosphorylation by PKC activates the
CC enzyme (PubMed:22906005). {ECO:0000250|UniProtKB:Q08462,
CC ECO:0000269|PubMed:1719547, ECO:0000269|PubMed:21596131,
CC ECO:0000269|PubMed:22906005, ECO:0000269|PubMed:24363043,
CC ECO:0000269|PubMed:7761832}.
CC -!- SUBUNIT: Interacts with RAF1 (By similarity). Interacts with GNAS
CC (PubMed:9417641, PubMed:10427002, PubMed:11087399, PubMed:15591060,
CC PubMed:16766715, PubMed:19243146). Interacts with the G protein beta
CC and gamma subunit complex (PubMed:21596131).
CC {ECO:0000250|UniProtKB:Q08462, ECO:0000269|PubMed:10427002,
CC ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060,
CC ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146,
CC ECO:0000269|PubMed:21596131, ECO:0000269|PubMed:9417641}.
CC -!- INTERACTION:
CC P26769; Q99996-4: AKAP9; Xeno; NbExp=3; IntAct=EBI-1027877, EBI-15676518;
CC P26769; Q08499-2: PDE4D; Xeno; NbExp=3; IntAct=EBI-1027877, EBI-8095525;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:1719547,
CC ECO:0000269|PubMed:22906005}; Multi-pass membrane protein
CC {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:1719547,
CC ECO:0000269|PubMed:7761832}; Multi-pass membrane protein {ECO:0000305}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q08462}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, olfactory epithelium and lung.
CC {ECO:0000269|PubMed:1719547}.
CC -!- DOMAIN: The protein contains two modules with six transmembrane helices
CC each; both are required for catalytic activity. Isolated N-terminal or
CC C-terminal guanylate cyclase domains have no catalytic activity, but
CC when they are brought together, enzyme activity is restored. The active
CC site is at the interface of the two domains. Both contribute substrate-
CC binding residues, but the catalytic metal ions are bound exclusively
CC via the N-terminal guanylate cyclase domain.
CC {ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399,
CC ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:16766715,
CC ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9417641}.
CC -!- PTM: Phosphorylated by RAF1 (By similarity).
CC {ECO:0000250|UniProtKB:Q08462}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; M80550; AAA40682.1; -; mRNA.
DR PIR; A41541; A41541.
DR RefSeq; NP_112269.1; NM_031007.1.
DR PDB; 1AB8; X-ray; 2.20 A; A/B=871-1090.
DR PDB; 1AZS; X-ray; 2.30 A; B=870-1081.
DR PDB; 1CJK; X-ray; 3.00 A; B=870-1081.
DR PDB; 1CJT; X-ray; 2.80 A; B=870-1081.
DR PDB; 1CJU; X-ray; 2.80 A; B=870-1081.
DR PDB; 1CJV; X-ray; 3.00 A; B=870-1081.
DR PDB; 1CS4; X-ray; 2.50 A; B=870-1081.
DR PDB; 1CUL; X-ray; 2.40 A; B=874-1081.
DR PDB; 1TL7; X-ray; 2.80 A; B=870-1081.
DR PDB; 1U0H; X-ray; 2.90 A; B=870-1081.
DR PDB; 2GVD; X-ray; 2.90 A; B=870-1081.
DR PDB; 2GVZ; X-ray; 3.27 A; B=870-1081.
DR PDB; 3C14; X-ray; 2.68 A; B=870-1081.
DR PDB; 3C15; X-ray; 2.78 A; B=870-1081.
DR PDB; 3C16; X-ray; 2.87 A; B=870-1081.
DR PDB; 3G82; X-ray; 3.11 A; B=870-1081.
DR PDB; 3MAA; X-ray; 3.00 A; B=870-1081.
DR PDBsum; 1AB8; -.
DR PDBsum; 1AZS; -.
DR PDBsum; 1CJK; -.
DR PDBsum; 1CJT; -.
DR PDBsum; 1CJU; -.
DR PDBsum; 1CJV; -.
DR PDBsum; 1CS4; -.
DR PDBsum; 1CUL; -.
DR PDBsum; 1TL7; -.
DR PDBsum; 1U0H; -.
DR PDBsum; 2GVD; -.
DR PDBsum; 2GVZ; -.
DR PDBsum; 3C14; -.
DR PDBsum; 3C15; -.
DR PDBsum; 3C16; -.
DR PDBsum; 3G82; -.
DR PDBsum; 3MAA; -.
DR AlphaFoldDB; P26769; -.
DR SMR; P26769; -.
DR BioGRID; 249536; 1.
DR DIP; DIP-164N; -.
DR IntAct; P26769; 8.
DR MINT; P26769; -.
DR STRING; 10116.ENSRNOP00000038994; -.
DR BindingDB; P26769; -.
DR ChEMBL; CHEMBL2958; -.
DR DrugCentral; P26769; -.
DR GlyGen; P26769; 2 sites.
DR iPTMnet; P26769; -.
DR PhosphoSitePlus; P26769; -.
DR PaxDb; P26769; -.
DR PRIDE; P26769; -.
DR GeneID; 81636; -.
DR KEGG; rno:81636; -.
DR UCSC; RGD:619965; rat.
DR CTD; 108; -.
DR RGD; 619965; Adcy2.
DR eggNOG; KOG3619; Eukaryota.
DR InParanoid; P26769; -.
DR OrthoDB; 363718at2759; -.
DR PhylomeDB; P26769; -.
DR BRENDA; 4.6.1.1; 5301.
DR Reactome; R-RNO-163615; PKA activation.
DR Reactome; R-RNO-170660; Adenylate cyclase activating pathway.
DR Reactome; R-RNO-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-RNO-418597; G alpha (z) signalling events.
DR Reactome; R-RNO-5610787; Hedgehog 'off' state.
DR EvolutionaryTrace; P26769; -.
DR PRO; PR:P26769; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0008179; F:adenylate cyclase binding; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IPI:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB.
DR GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; IDA:UniProtKB.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; -; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR032628; AC_N.
DR InterPro; IPR030672; Adcy.
DR InterPro; IPR009398; Adcy_conserved_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF16214; AC_N; 1.
DR Pfam; PF06327; DUF1053; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR PIRSF; PIRSF039050; Ade_cyc; 1.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; SSF55073; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; cAMP biosynthesis; Cell membrane; Cytoplasm;
KW Glycoprotein; Lyase; Magnesium; Manganese; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1090
FT /note="Adenylate cyclase type 2"
FT /id="PRO_0000195686"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 763..783
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 800..820
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 821..1090
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000305"
FT REGION 904..921
FT /note="Interaction with GNAS"
FT /evidence="ECO:0000269|PubMed:11087399"
FT REGION 989..992
FT /note="Interaction with GNAS"
FT /evidence="ECO:0000269|PubMed:11087399"
FT BINDING 294..299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099,
FT ECO:0000305"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099,
FT ECO:0000269|PubMed:11087399, ECO:0000305"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099,
FT ECO:0000269|PubMed:11087399, ECO:0000305"
FT BINDING 336..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099,
FT ECO:0000305"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099,
FT ECO:0000269|PubMed:11087399, ECO:0000305"
FT BINDING 382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 938
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:10427002,
FT ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060,
FT ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146"
FT BINDING 1018..1020
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:10427002,
FT ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060,
FT ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146"
FT BINDING 1025..1029
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10427002,
FT ECO:0007744|PDB:1CJK, ECO:0007744|PDB:3MAA"
FT BINDING 1065
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:10427002,
FT ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060,
FT ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146"
FT MOD_RES 490
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:22906005"
FT MOD_RES 543
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:22906005"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 490
FT /note="S->A: Reduces activation by PKC. Abolishes
FT activation by PKC; when associated with A-543."
FT /evidence="ECO:0000269|PubMed:22906005"
FT MUTAGEN 490
FT /note="S->D: Increases basal level of enzyme activity.
FT Abolishes activation by PKC; when associated with D-543."
FT /evidence="ECO:0000269|PubMed:22906005"
FT MUTAGEN 543
FT /note="S->A: Reduces activation by PKC. Abolishes
FT activation by PKC; when associated with A-490."
FT /evidence="ECO:0000269|PubMed:22906005"
FT MUTAGEN 543
FT /note="S->D: Increases basal level of enzyme activity.
FT Abolishes activation by PKC; when associated with D-490."
FT /evidence="ECO:0000269|PubMed:22906005"
FT STRAND 879..891
FT /evidence="ECO:0007829|PDB:1AB8"
FT HELIX 895..898
FT /evidence="ECO:0007829|PDB:1AB8"
FT TURN 903..908
FT /evidence="ECO:0007829|PDB:1AB8"
FT HELIX 909..923
FT /evidence="ECO:0007829|PDB:1AB8"
FT HELIX 924..927
FT /evidence="ECO:0007829|PDB:1AB8"
FT HELIX 929..931
FT /evidence="ECO:0007829|PDB:1AB8"
FT STRAND 934..940
FT /evidence="ECO:0007829|PDB:1AB8"
FT STRAND 943..948
FT /evidence="ECO:0007829|PDB:1AB8"
FT HELIX 967..987
FT /evidence="ECO:0007829|PDB:1AB8"
FT TURN 988..991
FT /evidence="ECO:0007829|PDB:1AB8"
FT STRAND 997..1010
FT /evidence="ECO:0007829|PDB:1AB8"
FT STRAND 1012..1014
FT /evidence="ECO:0007829|PDB:1AB8"
FT STRAND 1016..1021
FT /evidence="ECO:0007829|PDB:1AB8"
FT HELIX 1022..1032
FT /evidence="ECO:0007829|PDB:1AB8"
FT STRAND 1039..1041
FT /evidence="ECO:0007829|PDB:1AB8"
FT HELIX 1043..1052
FT /evidence="ECO:0007829|PDB:1AB8"
FT STRAND 1056..1064
FT /evidence="ECO:0007829|PDB:1AZS"
FT TURN 1065..1067
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 1068..1075
FT /evidence="ECO:0007829|PDB:1AZS"
SQ SEQUENCE 1090 AA; 123316 MW; 935CE44DF73199B3 CRC64;
MRRRRYLRDR AEAAAAAAAG GGEGLQRSRD WLYESYYCMS QQHPLIVFLL LIVMGACLAL
LAVFFALGLE VEDHVAFLIT VPTALAIFFA IFILVCIESV FKKLLRVFSL VIWICLVAMG
YLFMCFGGTV SAWDQVSFFL FIIFVVYTML PFNMRDAIIA SILTSSSHTI VLSVYLSATP
GAKEHLFWQI LANVIIFICG NLAGAYHKHL MELALQQTYR DTCNCIKSRI KLEFEKRQQE
RLLLSLLPAH IAMEMKAEII QRLQGPKAGQ MENTNNFHNL YVKRHTNVSI LYADIVGFTR
LASDCSPGEL VHMLNELFGK FDQIAKENEC MRIKILGDCY YCVSGLPISL PNHAKNCVKM
GLDMCEAIKK VRDATGVDIN MRVGVHSGNV LCGVIGLQKW QYDVWSHDVT LANHMEAGGV
PGRVHISSVT LEHLNGAYKV EEGDGEIRDP YLKQHLVKTY FVINPKGERR SPQHLFRPRH
TLDGAKMRAS VRMTRYLESW GAAKPFAHLH HRDSMTTENG KISTTDVPMG QHNFQNRTLR
TKSQKKRFEE ELNERMIQAI DGINAQKQWL KSEDIQRISL LFYNKNIEKE YRATALPAFK
YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL LQCSKKASTS
LMWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL SNSEETTLPT ANTSNANVSV
PDNQASILHA RNLFFLPYFI YSCILGLISC SVFLRVNYEL KMLIMMVALV GYNTILLHTH
AHVLDAYSQV LFQRPGIWKD LKTMGSVSLS IFFITLLVLG RQSEYYCRLD FLWKNKFKKE
REEIETMENL NRVLLENVLP AHVAEHFLAR SLKNEELYHQ SYDCVCVMFA SIPDFKEFYT
ESDVNKEGLE CLRLLNEIIA DFDDLLSKPK FSGVEKIKTI GSTYMAATGL SAIPSQEHAQ
EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI NHGPVIAGVI GAQKPQYDIW
GNTVNVASRM DSTGVLDKIQ VTEETSLILQ TLGYTCTCRG IINVKGKGDL KTYFVNTEMS
RSLSQSNLAS
