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Adenylate cyclase type 2 (EC 4.6.1.1) (ATP pyrophosphate-lyase 2) (Adenylate cyclase type II) (Adenylyl cyclase 2) (AC2)

 ADCY2_RAT               Reviewed;        1090 AA.
P26769;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
20-JUN-2018, entry version 158.
RecName: Full=Adenylate cyclase type 2;
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};
AltName: Full=ATP pyrophosphate-lyase 2;
AltName: Full=Adenylate cyclase type II;
AltName: Full=Adenylyl cyclase 2;
Short=AC2 {ECO:0000303|PubMed:24363043};
Name=Adcy2;
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, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=1719547; DOI=10.1073/pnas.88.22.10173;
Feinstein P.G., Schrader K.A., Bakalyar H.A., Tang W.J., Krupinski J.,
Gilman A.G., Reed R.R.;
"Molecular cloning and characterization of a Ca2+/calmodulin-
insensitive adenylyl cyclase from rat brain.";
Proc. Natl. Acad. Sci. U.S.A. 88:10173-10177(1991).
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, AND
SUBCELLULAR LOCATION.
PubMed=7761832; DOI=10.1126/science.7761832;
Chen J., DeVivo M., Dingus J., Harry A., Li J., Sui J., Carty D.J.,
Blank J.L., Exton J.H., Stoffel R.H.;
"A region of adenylyl cyclase 2 critical for regulation by G protein
beta gamma subunits.";
Science 268:1166-1169(1995).
[3]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION,
AND INTERACTION WITH THE G PROTEIN BETA AND GAMMA SUBUNIT COMPLEX.
PubMed=21596131; DOI=10.1016/j.cellsig.2011.05.002;
Boran A.D., Chen Y., Iyengar R.;
"Identification of new Gbetagamma interaction sites in adenylyl
cyclase 2.";
Cell. Signal. 23:1489-1495(2011).
[4]
PHOSPHORYLATION AT SER-490 AND SER-543, MUTAGENESIS OF SER-490 AND
SER-543, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND
ENZYME REGULATION.
PubMed=22906005; DOI=10.1042/BJ20120279;
Shen J.X., Wachten S., Halls M.L., Everett K.L., Cooper D.M.;
"Muscarinic receptors stimulate AC2 by novel phosphorylation sites,
whereas Gbetagamma subunits exert opposing effects depending on the G-
protein source.";
Biochem. J. 447:393-405(2012).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[6]
FUNCTION, CATALYTIC ACTIVITY, 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).
[7]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 871-1090 IN COMPLEX WITH
FORSKOLIN.
PubMed=9069282; DOI=10.1038/386247a0;
Zhang G., Liu Y., Ruoho A.E., Hurley J.H.;
"Structure of the adenylyl cyclase catalytic core.";
Nature 386:247-253(1997).
[8]
ERRATUM.
Zhang G., Liu Y., Ruoho A.E., Hurley J.H.;
Nature 388:204-204(1997).
[9]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 870-1081 OF CHIMERA WITH
ADCY5 IN COMPLEX WITH GNAS, INTERACTION WITH GNAS, AND DOMAIN.
PubMed=9417641; DOI=10.1126/science.278.5345.1907;
Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.;
"Crystal structure of the catalytic domains of adenylyl cyclase in a
complex with Gsalpha.GTPgammaS.";
Science 278:1907-1916(1997).
[10]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF CHIMERA WITH
ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOGS, INTERACTION WITH GNAS,
DOMAIN, CATALYTIC ACTIVITY, FUNCTION, AND COFACTOR.
PubMed=10427002; DOI=10.1126/science.285.5428.756;
Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G.,
Sprang S.R.;
"Two-metal-ion catalysis in adenylyl cyclase.";
Science 285:756-760(1999).
[11] {ECO:0000244|PDB:1CS4, ECO:0000244|PDB:1CUL}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 874-1081 OF CHIMERA WITH
ADCY5 IN COMPLEX WITH GNAS; MAGNESIUM AND ATP ANALOGS, INTERACTION
WITH GNAS, DOMAIN, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=11087399; DOI=10.1021/bi0015562;
Tesmer J.J., Dessauer C.W., Sunahara R.K., Murray L.D., Johnson R.A.,
Gilman A.G., Sprang S.R.;
"Molecular basis for P-site inhibition of adenylyl cyclase.";
Biochemistry 39:14464-14471(2000).
[12] {ECO:0000244|PDB:1TL7, ECO:0000244|PDB:1U0H}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 870-1081 OF CHIMERA WITH
ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOG, FUNCTION, CATALYTIC
ACTIVITY, INTERACTION WITH GNAS, AND DOMAIN.
PubMed=15591060; DOI=10.1074/jbc.M409076200;
Mou T.C., Gille A., Fancy D.A., Seifert R., Sprang S.R.;
"Structural basis for the inhibition of mammalian membrane adenylyl
cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-
triphosphate.";
J. Biol. Chem. 280:7253-7261(2005).
[13] {ECO:0000244|PDB:2GVD, ECO:0000244|PDB:2GVZ}
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 870-1081 OF CHIMERA WITH
ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOG, FUNCTION, CATALYTIC
ACTIVITY, COFACTOR, INTERACTION WITH GNAS, AND DOMAIN.
PubMed=16766715; DOI=10.1124/mol.106.026427;
Mou T.C., Gille A., Suryanarayana S., Richter M., Seifert R.,
Sprang S.R.;
"Broad specificity of mammalian adenylyl cyclase for interaction with
2',3'-substituted purine- and pyrimidine nucleotide inhibitors.";
Mol. Pharmacol. 70:878-886(2006).
[14] {ECO:0000244|PDB:3C14, ECO:0000244|PDB:3C15, ECO:0000244|PDB:3C16, ECO:0000244|PDB:3MAA}
X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 870-1081 OF CHIMERA WITH
ADCY5 IN COMPLEX WITH GNAS; FORSKOLIN; MAGNESIUM IONS AND ATP ANALOG,
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GNAS, AND
DOMAIN.
PubMed=19243146; DOI=10.1021/bi802122k;
Mou T.C., Masada N., Cooper D.M., Sprang S.R.;
"Structural basis for inhibition of mammalian adenylyl cyclase by
calcium.";
Biochemistry 48:3387-3397(2009).
-!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP
in response to G-protein signaling (PubMed:22906005,
PubMed:24363043, PubMed:10427002, PubMed:1719547, PubMed:7761832,
PubMed:21596131, PubMed:11087399, PubMed:15591060,
PubMed:19243146, PubMed:16766715). Down-stream signaling cascades
mediate changes in gene expression patterns and lead to increased
IL6 production (PubMed:24363043). Functions in signaling cascades
downstream of the muscarinic acetylcholine receptors
(PubMed:22906005). {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,
ECO:0000269|PubMed:22906005, ECO:0000269|PubMed:24363043,
ECO:0000269|PubMed:7761832}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
{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, ECO:0000269|PubMed:22906005,
ECO:0000269|PubMed:24363043, ECO:0000269|PubMed:7761832}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10427002,
ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:16766715,
ECO:0000269|PubMed:1719547, ECO:0000269|PubMed:19243146,
ECO:0000269|PubMed:7761832};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:10427002,
ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:16766715};
Note=Binds 2 magnesium ions per subunit. Is also active with
manganese (in vitro). {ECO:0000269|PubMed:16766715,
ECO:0000305|PubMed:10427002};
-!- ENZYME REGULATION: Activated by forskolin (PubMed:1719547,
PubMed:22906005, PubMed:24363043). Is not activated by calmodulin
(PubMed:1719547). Inhibited by calcium ions, already at micromolar
concentration. Activated by the G protein alpha subunit GNAS
(PubMed:1719547, PubMed:7761832, PubMed:21596131). Activated by
the G protein beta and gamma subunit complex (PubMed:7761832,
PubMed:21596131, PubMed:22906005). Phosphorylation by RAF1 results
in its activation (By similarity). Phosphorylation by PKC
activates the enzyme (PubMed:22906005).
{ECO:0000250|UniProtKB:Q08462, ECO:0000269|PubMed:1719547,
ECO:0000269|PubMed:21596131, ECO:0000269|PubMed:22906005,
ECO:0000269|PubMed:24363043, ECO:0000269|PubMed:7761832}.
-!- SUBUNIT: Interacts with RAF1 (By similarity). Interacts with GNAS
(PubMed:9417641, PubMed:10427002, PubMed:11087399,
PubMed:15591060, PubMed:16766715, PubMed:19243146). Interacts with
the G protein beta and gamma subunit complex (PubMed:21596131).
{ECO:0000250|UniProtKB:Q08462, ECO:0000269|PubMed:10427002,
ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060,
ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146,
ECO:0000269|PubMed:21596131, ECO:0000269|PubMed:9417641}.
-!- INTERACTION:
Q99996-4:AKAP9 (xeno); NbExp=3; IntAct=EBI-1027877, EBI-15676518;
Q08499-2:PDE4D (xeno); NbExp=3; IntAct=EBI-1027877, EBI-8095525;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:1719547,
ECO:0000269|PubMed:22906005}; Multi-pass membrane protein
{ECO:0000305}. Cell membrane {ECO:0000269|PubMed:1719547,
ECO:0000269|PubMed:7761832}; Multi-pass membrane protein
{ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q08462}.
-!- TISSUE SPECIFICITY: Expressed in brain, olfactory epithelium and
lung. {ECO:0000269|PubMed:1719547}.
-!- 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:0000269|PubMed:10427002,
ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060,
ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146,
ECO:0000269|PubMed:9417641}.
-!- PTM: Phosphorylated by RAF1 (By similarity).
{ECO:0000250|UniProtKB:Q08462}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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EMBL; M80550; AAA40682.1; -; mRNA.
PIR; A41541; A41541.
RefSeq; NP_112269.1; NM_031007.1.
UniGene; Rn.10731; -.
PDB; 1AB8; X-ray; 2.20 A; A/B=871-1090.
PDB; 1AZS; X-ray; 2.30 A; B=870-1081.
PDB; 1CJK; X-ray; 3.00 A; B=870-1081.
PDB; 1CJT; X-ray; 2.80 A; B=870-1081.
PDB; 1CJU; X-ray; 2.80 A; B=870-1081.
PDB; 1CJV; X-ray; 3.00 A; B=870-1081.
PDB; 1CS4; X-ray; 2.50 A; B=870-1081.
PDB; 1CUL; X-ray; 2.40 A; B=874-1081.
PDB; 1TL7; X-ray; 2.80 A; B=870-1081.
PDB; 1U0H; X-ray; 2.90 A; B=870-1081.
PDB; 2GVD; X-ray; 2.90 A; B=870-1081.
PDB; 2GVZ; X-ray; 3.27 A; B=870-1081.
PDB; 3C14; X-ray; 2.68 A; B=870-1081.
PDB; 3C15; X-ray; 2.78 A; B=870-1081.
PDB; 3C16; X-ray; 2.87 A; B=870-1081.
PDB; 3G82; X-ray; 3.11 A; B=870-1081.
PDB; 3MAA; X-ray; 3.00 A; B=870-1081.
PDBsum; 1AB8; -.
PDBsum; 1AZS; -.
PDBsum; 1CJK; -.
PDBsum; 1CJT; -.
PDBsum; 1CJU; -.
PDBsum; 1CJV; -.
PDBsum; 1CS4; -.
PDBsum; 1CUL; -.
PDBsum; 1TL7; -.
PDBsum; 1U0H; -.
PDBsum; 2GVD; -.
PDBsum; 2GVZ; -.
PDBsum; 3C14; -.
PDBsum; 3C15; -.
PDBsum; 3C16; -.
PDBsum; 3G82; -.
PDBsum; 3MAA; -.
ProteinModelPortal; P26769; -.
SMR; P26769; -.
BioGrid; 249536; 1.
DIP; DIP-164N; -.
IntAct; P26769; 8.
MINT; P26769; -.
STRING; 10116.ENSRNOP00000038994; -.
BindingDB; P26769; -.
ChEMBL; CHEMBL2958; -.
iPTMnet; P26769; -.
PhosphoSitePlus; P26769; -.
PaxDb; P26769; -.
PRIDE; P26769; -.
GeneID; 81636; -.
KEGG; rno:81636; -.
UCSC; RGD:619965; rat.
CTD; 108; -.
RGD; 619965; Adcy2.
eggNOG; KOG3619; Eukaryota.
eggNOG; COG2114; LUCA.
HOGENOM; HOG000006941; -.
HOVERGEN; HBG050458; -.
InParanoid; P26769; -.
KO; K08042; -.
PhylomeDB; P26769; -.
BRENDA; 4.6.1.1; 5301.
EvolutionaryTrace; P26769; -.
PRO; PR:P26769; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
GO; GO:0008179; F:adenylate cyclase binding; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IPI:RGD.
GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:BHF-UCL.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; IDA:UniProtKB.
GO; GO:0006182; P:cGMP biosynthetic process; 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;
3D-structure; ATP-binding; cAMP biosynthesis; Cell membrane;
Complete proteome; Cytoplasm; Glycoprotein; Lyase; Magnesium;
Manganese; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat; Transmembrane;
Transmembrane helix.
CHAIN 1 1090 Adenylate cyclase type 2.
/FTId=PRO_0000195686.
TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.
TRANSMEM 45 65 Helical. {ECO:0000255}.
TRANSMEM 75 95 Helical. {ECO:0000255}.
TRANSMEM 107 127 Helical. {ECO:0000255}.
TRANSMEM 132 152 Helical. {ECO:0000255}.
TRANSMEM 157 177 Helical. {ECO:0000255}.
TRANSMEM 186 206 Helical. {ECO:0000255}.
TOPO_DOM 207 600 Cytoplasmic. {ECO:0000255}.
TRANSMEM 601 621 Helical. {ECO:0000255}.
TRANSMEM 626 646 Helical. {ECO:0000255}.
TRANSMEM 679 699 Helical. {ECO:0000255}.
TRANSMEM 734 754 Helical. {ECO:0000255}.
TRANSMEM 763 783 Helical. {ECO:0000255}.
TRANSMEM 800 820 Helical. {ECO:0000255}.
TOPO_DOM 821 1090 Cytoplasmic. {ECO:0000255, ECO:0000305}.
NP_BIND 294 299 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 336 338 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 1018 1020 ATP. {ECO:0000305|PubMed:10427002,
ECO:0000305|PubMed:11087399,
ECO:0000305|PubMed:15591060,
ECO:0000305|PubMed:16766715,
ECO:0000305|PubMed:19243146}.
NP_BIND 1025 1029 ATP. {ECO:0000244|PDB:1CJK,
ECO:0000244|PDB:3MAA,
ECO:0000269|PubMed:10427002}.
REGION 904 921 Interaction with GNAS.
{ECO:0000269|PubMed:11087399}.
REGION 989 992 Interaction with GNAS.
{ECO:0000269|PubMed:11087399}.
METAL 294 294 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099,
ECO:0000305}.
METAL 294 294 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099,
ECO:0000269|PubMed:11087399,
ECO:0000305}.
METAL 295 295 Magnesium 2; via carbonyl oxygen;
catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00099,
ECO:0000269|PubMed:11087399,
ECO:0000305}.
METAL 338 338 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099,
ECO:0000305}.
METAL 338 338 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099,
ECO:0000269|PubMed:11087399,
ECO:0000305}.
BINDING 382 382 ATP. {ECO:0000250|UniProtKB:P30803}.
BINDING 938 938 ATP. {ECO:0000305|PubMed:10427002,
ECO:0000305|PubMed:11087399,
ECO:0000305|PubMed:15591060,
ECO:0000305|PubMed:16766715,
ECO:0000305|PubMed:19243146}.
BINDING 1065 1065 ATP. {ECO:0000305|PubMed:10427002,
ECO:0000305|PubMed:11087399,
ECO:0000305|PubMed:15591060,
ECO:0000305|PubMed:16766715,
ECO:0000305|PubMed:19243146}.
MOD_RES 490 490 Phosphoserine; by PKC.
{ECO:0000269|PubMed:22906005}.
MOD_RES 543 543 Phosphoserine; by PKC.
{ECO:0000269|PubMed:22906005}.
CARBOHYD 712 712 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 717 717 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 490 490 S->A: Reduces activation by PKC.
Abolishes activation by PKC; when
associated with A-543.
{ECO:0000269|PubMed:22906005}.
MUTAGEN 490 490 S->D: Increases basal level of enzyme
activity. Abolishes activation by PKC;
when associated with D-543.
{ECO:0000269|PubMed:22906005}.
MUTAGEN 543 543 S->A: Reduces activation by PKC.
Abolishes activation by PKC; when
associated with A-490.
{ECO:0000269|PubMed:22906005}.
MUTAGEN 543 543 S->D: Increases basal level of enzyme
activity. Abolishes activation by PKC;
when associated with D-490.
{ECO:0000269|PubMed:22906005}.
STRAND 879 891 {ECO:0000244|PDB:1AB8}.
HELIX 895 898 {ECO:0000244|PDB:1AB8}.
TURN 903 908 {ECO:0000244|PDB:1AB8}.
HELIX 909 923 {ECO:0000244|PDB:1AB8}.
HELIX 924 927 {ECO:0000244|PDB:1AB8}.
HELIX 929 931 {ECO:0000244|PDB:1AB8}.
STRAND 934 940 {ECO:0000244|PDB:1AB8}.
STRAND 943 948 {ECO:0000244|PDB:1AB8}.
HELIX 967 987 {ECO:0000244|PDB:1AB8}.
TURN 988 991 {ECO:0000244|PDB:1AB8}.
STRAND 997 1010 {ECO:0000244|PDB:1AB8}.
STRAND 1012 1014 {ECO:0000244|PDB:1AB8}.
STRAND 1016 1021 {ECO:0000244|PDB:1AB8}.
HELIX 1022 1032 {ECO:0000244|PDB:1AB8}.
STRAND 1039 1041 {ECO:0000244|PDB:1AB8}.
HELIX 1043 1052 {ECO:0000244|PDB:1AB8}.
STRAND 1056 1064 {ECO:0000244|PDB:1AZS}.
TURN 1065 1067 {ECO:0000244|PDB:1AZS}.
STRAND 1068 1075 {ECO:0000244|PDB:1AZS}.
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


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