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Database: UniProt
Entry: P54645
LinkDB: P54645
Original site: P54645 
ID   AAPK1_RAT               Reviewed;         559 AA.
AC   P54645;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   17-JUN-2020, entry version 193.
DE   RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-1;
DE            Short=AMPK subunit alpha-1;
DE            EC=2.7.11.1 {ECO:0000269|PubMed:2369897, ECO:0000269|PubMed:9029219};
DE   AltName: Full=Acetyl-CoA carboxylase kinase;
DE            Short=ACACA kinase;
DE            EC=2.7.11.27 {ECO:0000269|PubMed:9029219};
DE   AltName: Full=Hydroxymethylglutaryl-CoA reductase kinase;
DE            Short=HMGCR kinase;
DE            EC=2.7.11.31 {ECO:0000269|PubMed:2369897};
DE   AltName: Full=Tau-protein kinase PRKAA1;
DE            EC=2.7.11.26 {ECO:0000305|PubMed:21204788};
GN   Name=Prkaa1; Synonyms=Ampk1;
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 [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-559, AND PROTEIN SEQUENCE OF 24-40;
RP   90-115; 129-140; 150-160; 166-182; 236-257; 272-276; 286-305; 326-341;
RP   350-367; 375-384; 409-426; 437-446; 458-475 AND 507-517.
RC   STRAIN=Sprague-Dawley; TISSUE=Hypothalamus, and Liver;
RX   PubMed=8557660; DOI=10.1074/jbc.271.2.611;
RA   Stapleton D., Mitchelhill K.I., Gao G., Widmer J., Michell B.J., Teh T.,
RA   House C.M., Fernandez C.S., Cox T., Witters L.A., Kemp B.E.;
RT   "Mammalian AMP-activated protein kinase subfamily.";
RL   J. Biol. Chem. 271:611-614(1996).
RN   [3]
RP   CATALYTIC ACTIVITY, AND FUNCTION IN PHOSPHORYLATION OF HMGCR.
RX   PubMed=2369897; DOI=10.1002/j.1460-2075.1990.tb07420.x;
RA   Clarke P.R., Hardie D.G.;
RT   "Regulation of HMG-CoA reductase: identification of the site phosphorylated
RT   by the AMP-activated protein kinase in vitro and in intact rat liver.";
RL   EMBO J. 9:2439-2446(1990).
RN   [4]
RP   IDENTIFICATION IN THE AMPK COMPLEX.
RC   STRAIN=Sprague-Dawley; TISSUE=Hypothalamus, and Liver;
RX   PubMed=7961907;
RA   Stapleton D., Gao G., Michell B.J., Widmer J., Mitchelhill K.I., Teh T.,
RA   House C.M., Witters L.A., Kemp B.E.;
RT   "Mammalian 5'-AMP-activated protein kinase non-catalytic subunits are
RT   homologs of proteins that interact with yeast Snf1 protein kinase.";
RL   J. Biol. Chem. 269:29343-29346(1994).
RN   [5]
RP   PHOSPHORYLATION AT THR-183, AND ACTIVITY REGULATION.
RX   PubMed=8910387; DOI=10.1074/jbc.271.44.27879;
RA   Hawley S.A., Davison M., Woods A., Davies S.P., Beri R.K., Carling D.,
RA   Hardie D.G.;
RT   "Characterization of the AMP-activated protein kinase kinase from rat liver
RT   and identification of threonine 172 as the major site at which it
RT   phosphorylates AMP-activated protein kinase.";
RL   J. Biol. Chem. 271:27879-27887(1996).
RN   [6]
RP   CATALYTIC ACTIVITY, AND FUNCTION IN PHOSPHORYLATION OF ACACA AND ACACB.
RX   PubMed=9029219; DOI=10.1152/jappl.1997.82.1.219;
RA   Winder W.W., Wilson H.A., Hardie D.G., Rasmussen B.B., Hutber C.A.,
RA   Call G.B., Clayton R.D., Conley L.M., Yoon S., Zhou B.;
RT   "Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated
RT   protein kinase and protein kinase A.";
RL   J. Appl. Physiol. 82:219-225(1997).
RN   [7]
RP   FUNCTION IN PHOSPHORYLATION OF NOS3.
RX   PubMed=10025949; DOI=10.1016/s0014-5793(98)01705-0;
RA   Chen Z.P., Mitchelhill K.I., Michell B.J., Stapleton D.,
RA   Rodriguez-Crespo I., Witters L.A., Power D.A., Ortiz de Montellano P.R.,
RA   Kemp B.E.;
RT   "AMP-activated protein kinase phosphorylation of endothelial NO synthase.";
RL   FEBS Lett. 443:285-289(1999).
RN   [8]
RP   FUNCTION IN PHOSPHORYLATION OF PFKFB2.
RX   PubMed=11069105; DOI=10.1016/s0960-9822(00)00742-9;
RA   Marsin A.S., Bertrand L., Rider M.H., Deprez J., Beauloye C., Vincent M.F.,
RA   Van den Berghe G., Carling D., Hue L.;
RT   "Phosphorylation and activation of heart PFK-2 by AMPK has a role in the
RT   stimulation of glycolysis during ischaemia.";
RL   Curr. Biol. 10:1247-1255(2000).
RN   [9]
RP   FUNCTION IN PHOSPHORYLATION OF IRS1.
RX   PubMed=11598104; DOI=10.1074/jbc.c100483200;
RA   Jakobsen S.N., Hardie D.G., Morrice N., Tornqvist H.E.;
RT   "5'-AMP-activated protein kinase phosphorylates IRS-1 on Ser-789 in mouse
RT   C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide riboside.";
RL   J. Biol. Chem. 276:46912-46916(2001).
RN   [10]
RP   FUNCTION IN PHOSPHORYLATION OF MLXIPL.
RX   PubMed=11724780; DOI=10.1074/jbc.m107895200;
RA   Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.;
RT   "Mechanism for fatty acid 'sparing' effect on glucose-induced
RT   transcription: regulation of carbohydrate-responsive element-binding
RT   protein by AMP-activated protein kinase.";
RL   J. Biol. Chem. 277:3829-3835(2002).
RN   [11]
RP   FUNCTION IN PHOSPHORYLATION OF PFKFB3.
RX   PubMed=12065600; DOI=10.1074/jbc.m205213200;
RA   Marsin A.S., Bouzin C., Bertrand L., Hue L.;
RT   "The stimulation of glycolysis by hypoxia in activated monocytes is
RT   mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-
RT   kinase.";
RL   J. Biol. Chem. 277:30778-30783(2002).
RN   [12]
RP   PHOSPHORYLATION AT THR-183, AND ACTIVITY REGULATION.
RX   PubMed=14614828; DOI=10.1016/j.cub.2003.10.031;
RA   Woods A., Johnstone S.R., Dickerson K., Leiper F.C., Fryer L.G.,
RA   Neumann D., Schlattner U., Wallimann T., Carlson M., Carling D.;
RT   "LKB1 is the upstream kinase in the AMP-activated protein kinase cascade.";
RL   Curr. Biol. 13:2004-2008(2003).
RN   [13]
RP   FUNCTION, ACTIVITY REGULATION, AND PHOSPHORYLATION AT THR-183.
RX   PubMed=14511394; DOI=10.1186/1475-4924-2-28;
RA   Hawley S.A., Boudeau J., Reid J.L., Mustard K.J., Udd L., Makela T.P.,
RA   Alessi D.R., Hardie D.G.;
RT   "Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25
RT   alpha/beta are upstream kinases in the AMP-activated protein kinase
RT   cascade.";
RL   J. Biol. 2:28.1-28.16(2003).
RN   [14]
RP   FUNCTION IN PHOSPHORYLATION OF HNF4A.
RX   PubMed=12740371; DOI=10.1074/jbc.m304112200;
RA   Hong Y.H., Varanasi U.S., Yang W., Leff T.;
RT   "AMP-activated protein kinase regulates HNF4alpha transcriptional activity
RT   by inhibiting dimer formation and decreasing protein stability.";
RL   J. Biol. Chem. 278:27495-27501(2003).
RN   [15]
RP   PHOSPHORYLATION AT THR-269 AND SER-496, MUTAGENESIS OF THR-183; THR-269 AND
RP   SER-496, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12764152; DOI=10.1074/jbc.m303946200;
RA   Woods A., Vertommen D., Neumann D., Turk R., Bayliss J., Schlattner U.,
RA   Wallimann T., Carling D., Rider M.H.;
RT   "Identification of phosphorylation sites in AMP-activated protein kinase
RT   (AMPK) for upstream AMPK kinases and study of their roles by site-directed
RT   mutagenesis.";
RL   J. Biol. Chem. 278:28434-28442(2003).
RN   [16]
RP   FUNCTION IN PHOSPHORYLATION OF EEF2K.
RX   PubMed=14709557; DOI=10.1074/jbc.m309773200;
RA   Browne G.J., Finn S.G., Proud C.G.;
RT   "Stimulation of the AMP-activated protein kinase leads to activation of
RT   eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel
RT   site, serine 398.";
RL   J. Biol. Chem. 279:12220-12231(2004).
RN   [17]
RP   PHOSPHORYLATION AT THR-183, AND ACTIVITY REGULATION.
RX   PubMed=16054095; DOI=10.1016/j.cmet.2005.05.009;
RA   Hawley S.A., Pan D.A., Mustard K.J., Ross L., Bain J., Edelman A.M.,
RA   Frenguelli B.G., Hardie D.G.;
RT   "Calmodulin-dependent protein kinase kinase-beta is an alternative upstream
RT   kinase for AMP-activated protein kinase.";
RL   Cell Metab. 2:9-19(2005).
RN   [18]
RP   PHOSPHORYLATION AT THR-183, AND ACTIVITY REGULATION.
RX   PubMed=16054096; DOI=10.1016/j.cmet.2005.06.005;
RA   Woods A., Dickerson K., Heath R., Hong S.-P., Momcilovic M.,
RA   Johnstone S.R., Carlson M., Carling D.;
RT   "Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-
RT   activated protein kinase in mammalian cells.";
RL   Cell Metab. 2:21-33(2005).
RN   [19]
RP   FUNCTION IN PHOSPHORYLATION OF SLC12A1.
RX   PubMed=17341212; DOI=10.1042/bj20061850;
RA   Fraser S.A., Gimenez I., Cook N., Jennings I., Katerelos M., Katsis F.,
RA   Levidiotis V., Kemp B.E., Power D.A.;
RT   "Regulation of the renal-specific Na+-K+-2Cl- co-transporter NKCC2 by AMP-
RT   activated protein kinase (AMPK).";
RL   Biochem. J. 405:85-93(2007).
RN   [20]
RP   PHOSPHORYLATION BY ULK1 AND ULK, AND PHOSPHORYLATION AT SER-360; THR-368;
RP   SER-397; SER-486 AND THR-488.
RX   PubMed=21460634; DOI=10.4161/auto.7.7.15451;
RA   Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
RA   Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
RT   "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory
RT   feedback loop.";
RL   Autophagy 7:696-706(2011).
RN   [21]
RP   FUNCTION IN PHOSPHORYLATION OF MAPT.
RX   PubMed=21204788; DOI=10.1042/bj20101485;
RA   Thornton C., Bright N.J., Sastre M., Muckett P.J., Carling D.;
RT   "AMP-activated protein kinase (AMPK) is a tau kinase, activated in response
RT   to amyloid beta-peptide exposure.";
RL   Biochem. J. 434:503-512(2011).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486; THR-490 AND SER-496, AND
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   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 405-557 IN COMPLEX WITH PRKAB2 AND
RP   PRKAG1.
RX   PubMed=17851531; DOI=10.1038/nature06161;
RA   Xiao B., Heath R., Saiu P., Leiper F.C., Leone P., Jing C., Walker P.A.,
RA   Haire L., Eccleston J.F., Davis C.T., Martin S.R., Carling D.,
RA   Gamblin S.J.;
RT   "Structural basis for AMP binding to mammalian AMP-activated protein
RT   kinase.";
RL   Nature 449:496-500(2007).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 13-559 IN COMPLEX WITH PRKAB2 AND
RP   PRKAG1, AND MUTAGENESIS OF 386-ARG--GLU-391.
RX   PubMed=21399626; DOI=10.1038/nature09932;
RA   Xiao B., Sanders M.J., Underwood E., Heath R., Mayer F.V., Carmena D.,
RA   Jing C., Walker P.A., Eccleston J.F., Haire L.F., Saiu P., Howell S.A.,
RA   Aasland R., Martin S.R., Carling D., Gamblin S.J.;
RT   "Structure of mammalian AMPK and its regulation by ADP.";
RL   Nature 472:230-233(2011).
CC   -!- FUNCTION: Catalytic subunit of AMP-activated protein kinase (AMPK), an
CC       energy sensor protein kinase that plays a key role in regulating
CC       cellular energy metabolism. In response to reduction of intracellular
CC       ATP levels, AMPK activates energy-producing pathways and inhibits
CC       energy-consuming processes: inhibits protein, carbohydrate and lipid
CC       biosynthesis, as well as cell growth and proliferation. AMPK acts via
CC       direct phosphorylation of metabolic enzymes, and by longer-term effects
CC       via phosphorylation of transcription regulators. Also acts as a
CC       regulator of cellular polarity by remodeling the actin cytoskeleton;
CC       probably by indirectly activating myosin. Regulates lipid synthesis by
CC       phosphorylating and inactivating lipid metabolic enzymes such as ACACA,
CC       ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol
CC       synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB)
CC       and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates
CC       insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and
CC       PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the
CC       translocation of the glucose transporter SLC2A4/GLUT4 to the plasma
CC       membrane, possibly by mediating phosphorylation of TBC1D4/AS160.
CC       Regulates transcription and chromatin structure by phosphorylating
CC       transcription regulators involved in energy metabolism such as
CC       CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300,
CC       HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator
CC       of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading
CC       to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress,
CC       phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote
CC       transcription. Acts as a key regulator of cell growth and proliferation
CC       by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient
CC       limitation, negatively regulates the mTORC1 complex by phosphorylating
CC       RPTOR component of the mTORC1 complex and by phosphorylating and
CC       activating TSC2. In response to nutrient limitation, promotes autophagy
CC       by phosphorylating and activating ATG1/ULK1. In that process also
CC       activates WDR45. In response to nutrient limitation, phosphorylates
CC       transcription factor FOXO3 promoting FOXO3 mitochondrial import (By
CC       similarity). AMPK also acts as a regulator of circadian rhythm by
CC       mediating phosphorylation of CRY1, leading to destabilize it. May
CC       regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading
CC       to stabilize it. Also has tau-protein kinase activity: in response to
CC       amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to
CC       phosphorylation of MAPT/TAU; however the relevance of such data remains
CC       unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and
CC       SLC12A1. {ECO:0000250|UniProtKB:Q5EG47, ECO:0000269|PubMed:10025949,
CC       ECO:0000269|PubMed:11069105, ECO:0000269|PubMed:11598104,
CC       ECO:0000269|PubMed:11724780, ECO:0000269|PubMed:12065600,
CC       ECO:0000269|PubMed:12740371, ECO:0000269|PubMed:14511394,
CC       ECO:0000269|PubMed:14709557, ECO:0000269|PubMed:17341212,
CC       ECO:0000269|PubMed:21204788, ECO:0000269|PubMed:2369897,
CC       ECO:0000269|PubMed:9029219}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000269|PubMed:2369897, ECO:0000269|PubMed:9029219};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000269|PubMed:2369897,
CC         ECO:0000269|PubMed:9029219};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[acetyl-CoA carboxylase]-L-serine + ATP = [acetyl-CoA
CC         carboxylase]-O-phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:20333,
CC         Rhea:RHEA-COMP:13722, Rhea:RHEA-COMP:13723, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.27;
CC         Evidence={ECO:0000269|PubMed:9029219};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[3-hydroxy-3-methylglutaryl-coenzyme A reductase]-L-serine +
CC         ATP = [3-hydroxy-3-methylglutaryl-coenzyme A reductase]-O-phospho-L-
CC         serine + ADP + H(+); Xref=Rhea:RHEA:23172, Rhea:RHEA-COMP:13692,
CC         Rhea:RHEA-COMP:13693, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.31; Evidence={ECO:0000269|PubMed:2369897};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[tau protein]-L-serine + ATP = [tau protein]-O-phospho-L-
CC         serine + ADP + H(+); Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701,
CC         Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.26; Evidence={ECO:0000305|PubMed:21204788};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[tau protein]-L-threonine + ATP = [tau protein]-O-phospho-L-
CC         threonine + ADP + H(+); Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC         Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.26; Evidence={ECO:0000305|PubMed:21204788};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-183. Binding
CC       of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or PRKAG3)
CC       results in allosteric activation, inducing phosphorylation on Thr-183.
CC       AMP-binding to gamma subunit also sustains activity by preventing
CC       dephosphorylation of Thr-183. ADP also stimulates Thr-183
CC       phosphorylation, without stimulating already phosphorylated AMPK. ATP
CC       promotes dephosphorylation of Thr-183, rendering the enzyme inactive.
CC       Under physiological conditions AMPK mainly exists in its inactive form
CC       in complex with ATP, which is much more abundant than AMP. Selectively
CC       inhibited by compound C (6-[4-(2-Piperidin-1-yl-ethoxy)-phenyl)]-3-
CC       pyridin-4-yl-pyyrazolo[1,5-a] pyrimidine. Activated by resveratrol, a
CC       natural polyphenol present in red wine, and S17834, a synthetic
CC       polyphenol. {ECO:0000269|PubMed:14511394, ECO:0000269|PubMed:14614828,
CC       ECO:0000269|PubMed:16054095, ECO:0000269|PubMed:16054096,
CC       ECO:0000269|PubMed:8910387}.
CC   -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1
CC       or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic
CC       subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2.
CC       {ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626,
CC       ECO:0000269|PubMed:7961907}.
CC   -!- INTERACTION:
CC       P54645; Q76JQ2: Flcn; NbExp=2; IntAct=EBI-7596967, EBI-7596839;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=In response to stress, recruited by p53/TP53 to specific
CC       promoters. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Low expression in kidney, liver, lung, heart and
CC       brain.
CC   -!- DOMAIN: The AIS (autoinhibitory sequence) region shows some sequence
CC       similarity with the ubiquitin-associated domains and represses kinase
CC       activity. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. {ECO:0000250}.
CC   -!- PTM: Phosphorylated at Thr-183 by STK11/LKB1 in complex with STE20-
CC       related adapter-alpha (STRADA) pseudo kinase and CAB39. Also
CC       phosphorylated at Thr-183 by CAMKK2; triggered by a rise in
CC       intracellular calcium ions, without detectable changes in the AMP/ATP
CC       ratio. CAMKK1 can also phosphorylate Thr-183, but at a much lower
CC       level. Dephosphorylated by protein phosphatase 2A and 2C (PP2A and
CC       PP2C). Phosphorylated by ULK1 and ULK2; leading to negatively regulate
CC       AMPK activity and suggesting the existence of a regulatory feedback
CC       loop between ULK1, ULK2 and AMPK. There is some ambiguity for some
CC       phosphosites: Ser-360/Thr-368 and Ser-486/Thr-488. Dephosphorylated by
CC       PPM1A and PPM1B (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000305}.
DR   EMBL; CH474048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U40819; AAC52355.1; -; mRNA.
DR   RefSeq; NP_062015.2; NM_019142.2.
DR   PDB; 2V8Q; X-ray; 2.10 A; A=407-559.
DR   PDB; 2V92; X-ray; 2.40 A; A=407-559.
DR   PDB; 2V9J; X-ray; 2.53 A; A=407-559.
DR   PDB; 2Y8L; X-ray; 2.50 A; A=407-555.
DR   PDB; 2Y8Q; X-ray; 2.80 A; A=407-555.
DR   PDB; 2YA3; X-ray; 2.51 A; A=407-555.
DR   PDB; 4CFH; X-ray; 3.24 A; A=13-481, C=535-559.
DR   PDB; 4EAI; X-ray; 2.28 A; A=405-479, A=540-559.
DR   PDB; 4EAJ; X-ray; 2.61 A; A=405-479, A=540-559.
DR   PDB; 4EAK; X-ray; 2.50 A; A=405-479, A=540-559.
DR   PDB; 4EAL; X-ray; 2.51 A; A=405-479, A=540-559.
DR   PDB; 4F2L; X-ray; 1.50 A; A=295-347.
DR   PDB; 4QFG; X-ray; 3.46 A; A=11-480, A=536-559.
DR   PDB; 4QFR; X-ray; 3.34 A; A=11-480, A=536-559.
DR   PDB; 4QFS; X-ray; 3.55 A; A=11-479, A=536-559.
DR   PDB; 5KQ5; X-ray; 3.41 A; A=11-480, A=536-559.
DR   PDB; 5T5T; X-ray; 3.46 A; A=11-480, A=536-559.
DR   PDB; 5UFU; X-ray; 3.45 A; A=269-559.
DR   PDB; 6E4T; X-ray; 3.40 A; A=11-480, A=536-559.
DR   PDB; 6E4U; X-ray; 3.27 A; A=11-480, A=536-559.
DR   PDB; 6E4W; X-ray; 3.35 A; A=11-480, A=536-559.
DR   PDBsum; 2V8Q; -.
DR   PDBsum; 2V92; -.
DR   PDBsum; 2V9J; -.
DR   PDBsum; 2Y8L; -.
DR   PDBsum; 2Y8Q; -.
DR   PDBsum; 2YA3; -.
DR   PDBsum; 4CFH; -.
DR   PDBsum; 4EAI; -.
DR   PDBsum; 4EAJ; -.
DR   PDBsum; 4EAK; -.
DR   PDBsum; 4EAL; -.
DR   PDBsum; 4F2L; -.
DR   PDBsum; 4QFG; -.
DR   PDBsum; 4QFR; -.
DR   PDBsum; 4QFS; -.
DR   PDBsum; 5KQ5; -.
DR   PDBsum; 5T5T; -.
DR   PDBsum; 5UFU; -.
DR   PDBsum; 6E4T; -.
DR   PDBsum; 6E4U; -.
DR   PDBsum; 6E4W; -.
DR   SMR; P54645; -.
DR   BioGRID; 249325; 368.
DR   CORUM; P54645; -.
DR   DIP; DIP-57168N; -.
DR   IntAct; P54645; 316.
DR   MINT; P54645; -.
DR   STRING; 10116.ENSRNOP00000017626; -.
DR   BindingDB; P54645; -.
DR   ChEMBL; CHEMBL4533; -.
DR   iPTMnet; P54645; -.
DR   PhosphoSitePlus; P54645; -.
DR   jPOST; P54645; -.
DR   PaxDb; P54645; -.
DR   PRIDE; P54645; -.
DR   Ensembl; ENSRNOT00000017626; ENSRNOP00000017626; ENSRNOG00000012799.
DR   GeneID; 65248; -.
DR   KEGG; rno:65248; -.
DR   CTD; 5562; -.
DR   RGD; 3387; Prkaa1.
DR   eggNOG; KOG0586; Eukaryota.
DR   eggNOG; ENOG410XNQ0; LUCA.
DR   GeneTree; ENSGT00940000158865; -.
DR   HOGENOM; CLU_000288_59_3_1; -.
DR   InParanoid; P54645; -.
DR   KO; K07198; -.
DR   OMA; YRSCQKD; -.
DR   OrthoDB; 1127668at2759; -.
DR   PhylomeDB; P54645; -.
DR   TreeFam; TF314032; -.
DR   BRENDA; 2.7.11.1; 5301.
DR   BRENDA; 2.7.11.31; 5301.
DR   Reactome; R-RNO-1632852; Macroautophagy.
DR   Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   SABIO-RK; P54645; -.
DR   EvolutionaryTrace; P54645; -.
DR   PRO; PR:P54645; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Proteomes; UP000234681; Chromosome 2.
DR   Proteomes; UP000234681; Unassembled WGS sequence.
DR   Bgee; ENSRNOG00000012799; Expressed in colon and 8 other tissues.
DR   Genevisible; P54645; RN.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030424; C:axon; IMP:ARUK-UCL.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030425; C:dendrite; IMP:ARUK-UCL.
DR   GO; GO:0043025; C:neuronal cell body; IMP:ARUK-UCL.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0050405; F:[acetyl-CoA carboxylase] kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047322; F:[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0042557; F:eukaryotic elongation factor-2 kinase activator activity; NAS:UniProtKB.
DR   GO; GO:0035174; F:histone serine kinase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR   GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015721; P:bile acid and bile salt transport; IEP:RGD.
DR   GO; GO:0038183; P:bile acid signaling pathway; IEP:RGD.
DR   GO; GO:0061762; P:CAMKK-AMPK signaling cascade; ISO:RGD.
DR   GO; GO:0071277; P:cellular response to calcium ion; IMP:ARUK-UCL.
DR   GO; GO:0035690; P:cellular response to drug; IEP:RGD.
DR   GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
DR   GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IMP:ARUK-UCL.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR   GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
DR   GO; GO:0071417; P:cellular response to organonitrogen compound; IEP:RGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:RGD.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009631; P:cold acclimation; IDA:RGD.
DR   GO; GO:0097009; P:energy homeostasis; IDA:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055089; P:fatty acid homeostasis; IDA:UniProtKB.
DR   GO; GO:0019395; P:fatty acid oxidation; ISO:RGD.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0008610; P:lipid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0061744; P:motor behavior; ISO:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:RGD.
DR   GO; GO:0050995; P:negative regulation of lipid catabolic process; ISS:UniProtKB.
DR   GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
DR   GO; GO:0017148; P:negative regulation of translation; NAS:UniProtKB.
DR   GO; GO:1904428; P:negative regulation of tubulin deacetylation; ISO:RGD.
DR   GO; GO:0070050; P:neuron cellular homeostasis; ISO:RGD.
DR   GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR   GO; GO:1903829; P:positive regulation of cellular protein localization; ISO:RGD.
DR   GO; GO:0046321; P:positive regulation of fatty acid oxidation; NAS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; NAS:UniProtKB.
DR   GO; GO:0046326; P:positive regulation of glucose import; NAS:UniProtKB.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IDA:UniProtKB.
DR   GO; GO:1903109; P:positive regulation of mitochondrial transcription; ISO:RGD.
DR   GO; GO:2000758; P:positive regulation of peptidyl-lysine acetylation; ISO:RGD.
DR   GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; ISO:RGD.
DR   GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; ISO:RGD.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR   GO; GO:0120188; P:regulation of bile acid secretion; IEP:RGD.
DR   GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IEP:RGD.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:RGD.
DR   GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR   GO; GO:0062028; P:regulation of stress granule assembly; ISO:RGD.
DR   GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:RGD.
DR   GO; GO:1904486; P:response to 17alpha-ethynylestradiol; IEP:RGD.
DR   GO; GO:0014823; P:response to activity; IDA:RGD.
DR   GO; GO:0031000; P:response to caffeine; IDA:RGD.
DR   GO; GO:1901563; P:response to camptothecin; ISO:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISO:RGD.
DR   GO; GO:0009411; P:response to UV; ISO:RGD.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd12199; AMPKA1_C; 1.
DR   InterPro; IPR032270; AMPK_C.
DR   InterPro; IPR039137; AMPKA1_C.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF16579; AdenylateSensor; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF103243; SSF103243; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Autophagy; Biological rhythms;
KW   Cholesterol biosynthesis; Cholesterol metabolism; Chromatin regulator;
KW   Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Kinase; Lipid biosynthesis; Lipid metabolism;
KW   Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation;
KW   Wnt signaling pathway.
FT   CHAIN           1..559
FT                   /note="5'-AMP-activated protein kinase catalytic subunit
FT                   alpha-1"
FT                   /id="PRO_0000085593"
FT   DOMAIN          27..279
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         33..41
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          302..381
FT                   /note="AIS"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        150
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         56
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         32
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13131"
FT   MOD_RES         183
FT                   /note="Phosphothreonine; by LKB1 and CaMKK2"
FT                   /evidence="ECO:0000269|PubMed:14511394,
FT                   ECO:0000269|PubMed:14614828, ECO:0000269|PubMed:16054095,
FT                   ECO:0000269|PubMed:16054096, ECO:0000269|PubMed:8910387"
FT   MOD_RES         269
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:12764152"
FT   MOD_RES         355
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13131"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13131"
FT   MOD_RES         360
FT                   /note="Phosphoserine; by ULK1"
FT                   /evidence="ECO:0000305|PubMed:21460634"
FT   MOD_RES         368
FT                   /note="Phosphothreonine; by ULK1"
FT                   /evidence="ECO:0000305|PubMed:21460634"
FT   MOD_RES         382
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13131"
FT   MOD_RES         397
FT                   /note="Phosphoserine; by ULK1"
FT                   /evidence="ECO:0000269|PubMed:21460634"
FT   MOD_RES         467
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13131"
FT   MOD_RES         486
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:22673903"
FT   MOD_RES         486
FT                   /note="Phosphoserine; by ULK1"
FT                   /evidence="ECO:0000244|PubMed:22673903,
FT                   ECO:0000305|PubMed:21460634"
FT   MOD_RES         488
FT                   /note="Phosphothreonine; by ULK1"
FT                   /evidence="ECO:0000305|PubMed:21460634"
FT   MOD_RES         490
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:22673903"
FT   MOD_RES         496
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:22673903,
FT                   ECO:0000269|PubMed:12764152"
FT   MOD_RES         508
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13131"
FT   MOD_RES         524
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13131"
FT   MOD_RES         527
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13131"
FT   MUTAGEN         183
FT                   /note="T->E: Hinders activation."
FT                   /evidence="ECO:0000269|PubMed:12764152"
FT   MUTAGEN         269
FT                   /note="T->A: Hinders activation."
FT                   /evidence="ECO:0000269|PubMed:12764152"
FT   MUTAGEN         269
FT                   /note="T->D: Retains activation ability."
FT                   /evidence="ECO:0000269|PubMed:12764152"
FT   MUTAGEN         386..391
FT                   /note="RHTLDE->AHALAA: Allosterically activated by AMP but
FT                   is not protected against dephosphorylation by AMP or ADP."
FT                   /evidence="ECO:0000269|PubMed:21399626"
FT   MUTAGEN         496
FT                   /note="S->A: Hinders activation."
FT                   /evidence="ECO:0000269|PubMed:12764152"
FT   MUTAGEN         496
FT                   /note="S->D: Retains activation ability."
FT                   /evidence="ECO:0000269|PubMed:12764152"
FT   CONFLICT        13..14
FT                   /note="Missing (in Ref. 2; AAC52355)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        473
FT                   /note="D -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          27..34
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   STRAND          37..39
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   STRAND          41..46
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   TURN            47..49
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   STRAND          52..59
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           60..63
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   TURN            64..67
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           69..80
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   STRAND          90..95
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   STRAND          97..105
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   TURN            112..117
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   STRAND          118..121
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           124..143
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   STRAND          146..149
FT                   /evidence="ECO:0000244|PDB:4QFG"
FT   STRAND          155..158
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   STRAND          164..166
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           169..171
FT                   /evidence="ECO:0000244|PDB:6E4U"
FT   STRAND          188..190
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           193..196
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           204..220
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           230..238
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           250..259
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   TURN            264..266
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           270..274
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           277..280
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   STRAND          287..289
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           301..311
FT                   /evidence="ECO:0000244|PDB:4F2L"
FT   HELIX           315..323
FT                   /evidence="ECO:0000244|PDB:4F2L"
FT   HELIX           330..347
FT                   /evidence="ECO:0000244|PDB:4F2L"
FT   HELIX           349..351
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           372..374
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           376..381
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   STRAND          407..413
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           417..430
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          434..439
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          442..448
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   TURN            450..452
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          455..464
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          466..468
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          470..477
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           542..555
FT                   /evidence="ECO:0000244|PDB:2V8Q"
SQ   SEQUENCE   559 AA;  63973 MW;  A869C340A85785ED CRC64;
     MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG HKVAVKILNR
     QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI FMVMEYVSGG ELFDYICKNG
     RLDEKESRRL FQQILSGVDY CHRHMVVHRD LKPENVLLDA HMNAKIADFG LSNMMSDGEF
     LRTSCGSPNY AAPEVISGRL YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG
     IFYTPQYLNP SVISLLKHML QVDPMKRATI KDIREHEWFK QDLPKYLFPE DPSYSSTMID
     DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD FYLATSPPDS
     FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ GVRKAKWHLG IRSQSRPNDI
     MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP VTSTFSKMSL QLYQVDSRTY LLDFRSIDDE
     ITEAKSGTAT PQRSGSISNY RSCQRSDSDA EAQGKPSEVS LTSSVTSLDS SPVDVAPRPG
     SHTIEFFEMC ANLIKILAQ
//
DBGET integrated database retrieval system