ID AMPKA_DICDI Reviewed; 727 AA.
AC Q54YF2; Q9XYP6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=5'-AMP-activated serine/threonine-protein kinase catalytic subunit alpha;
DE Short=AMPKA;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase, AMP-activated, alpha subunit;
DE AltName: Full=SNF1/AMP-activated kinase catalytic subunit;
DE AltName: Full=Sucrose non-fermenting protein snfA;
GN Name=snfA; Synonyms=ampka, prkaa; ORFNames=DDB_G0277905;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX3;
RA Sung S., Bisson S., Koehler S., Podgorski G.J.;
RT "The Dictyostelium SNF1/AMP-activated kinase.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17332500; DOI=10.1091/mbc.e06-09-0881;
RA Bokko P.B., Francione L., Bandala-Sanchez E., Ahmed A.U., Annesley S.J.,
RA Huang X., Khurana T., Kimmel A.R., Fisher P.R.;
RT "Diverse cytopathologies in mitochondrial disease are caused by AMP-
RT activated protein kinase signaling.";
RL Mol. Biol. Cell 18:1874-1886(2007).
CC -!- FUNCTION: Activated enzyme phosphorylates target proteins and initiates
CC downstream signaling pathways that shift metabolism from anabolic to
CC catabolic pathways. Acts as a highly sensitive cellular energy sensor.
CC {ECO:0000269|PubMed:17332500}.
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 -!- 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;
CC -!- SUBUNIT: Heterotrimer of an alpha catalytic subunit, a beta and a gamma
CC non-catalytic subunits. {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. Levels may
CC increase during the first 5 hours of starvation-induced
CC differentiation. {ECO:0000269|PubMed:17332500}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30963.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF118151; AAD30963.2; ALT_FRAME; Genomic_DNA.
DR EMBL; AAFI02000023; EAL68125.1; -; Genomic_DNA.
DR RefSeq; XP_642250.1; XM_637158.1.
DR AlphaFoldDB; Q54YF2; -.
DR SMR; Q54YF2; -.
DR STRING; 44689.Q54YF2; -.
DR PaxDb; 44689-DDB0215396; -.
DR EnsemblProtists; EAL68125; EAL68125; DDB_G0277905.
DR GeneID; 8621459; -.
DR KEGG; ddi:DDB_G0277905; -.
DR dictyBase; DDB_G0277905; snfA.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_3_1; -.
DR InParanoid; Q54YF2; -.
DR OMA; DFCSHSV; -.
DR PhylomeDB; Q54YF2; -.
DR Reactome; R-DDI-1632852; Macroautophagy.
DR Reactome; R-DDI-163680; AMPK inhibits chREBP transcriptional activation activity.
DR Reactome; R-DDI-200425; Carnitine metabolism.
DR Reactome; R-DDI-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-DDI-5628897; TP53 Regulates Metabolic Genes.
DR PRO; PR:Q54YF2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0030139; C:endocytic vesicle; IDA:dictyBase.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR GO; GO:0006754; P:ATP biosynthetic process; IMP:dictyBase.
DR GO; GO:0006914; P:autophagy; IMP:dictyBase.
DR GO; GO:1904630; P:cellular response to diterpene; IMP:dictyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:dictyBase.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; IMP:dictyBase.
DR GO; GO:0046956; P:positive phototaxis; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR GO; GO:0060176; P:regulation of aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:1901261; P:regulation of sorocarp spore cell differentiation; IMP:dictyBase.
DR GO; GO:0031285; P:regulation of sorocarp stalk cell differentiation; IMP:dictyBase.
DR CDD; cd12122; AMPKA_C; 1.
DR CDD; cd14079; STKc_AMPK_alpha; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
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 PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..727
FT /note="5'-AMP-activated serine/threonine-protein kinase
FT catalytic subunit alpha"
FT /id="PRO_0000358880"
FT DOMAIN 31..284
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 679..727
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 382..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 37..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="S -> P (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="F -> L (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="E -> K (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="R -> K (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..93
FT /note="IIK -> FIN (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="F -> P (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="T -> P (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..118
FT /note="FE -> LD (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="K -> R (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="K -> N (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="L -> P (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="D -> G (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 328..329
FT /note="EE -> GG (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 355..359
FT /note="ENEIN -> DDEVY (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 376..378
FT /note="QKS -> PQR (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="S -> T (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="Missing (in Ref. 1; AAD30963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 81639 MW; 481E0242FD2AB181 CRC64;
MSSYQQNPIG SFGGLYGSGG IEKSSQIIGN YRLDKTLGIG SFGKVKLAEH IRTGVKVAIK
ILNRTKIKNL KMDEKIRREI QNMKLFRHPH IIKLYEVIET TTDIFMVMEY VTGGELFEYI
VKNGKLLEDE SRRLFQQMIS GVDYCHHHMV VHRDLKPENL LLDPINKCIK IADFGLSNMM
QDGDFLKTSC GSPNYAAPEV ISGKLYAGPE VDVWSCGVIL YAFLCAKLPF DDESIPMLFK
KIREGVFSIP DFVSPSCADL IKKMLVVDPV KRITIHEIRN HPWFQVKLPK YLSSPHTFLS
KSIQTINNSI LNEMVQVYAP IDRERIIEEL QKSGEVNDLI VSYHLLVDSK RGSYENEINS
PNLVSPITTP IMSSAQKSPI MFTTTTGFNP SNSNSISNNN NNNNNNNNNT TNNNNNTTNN
NNSIINNNNI NNNNINNNNN NNNNNINNNN IINNNNNNNN NNNNNNNNNN NNNNNNNNNS
SISGGTEVFS ISPNLNNSYN SNSSGNSNGS NSNNNSNNNT NNDNNNNNNN NNNNNNNNNN
NNNNNNNNNN CIDSVNNSLN NENDVNNSNI NNNNNNNSDD GSNNNSYEGG GDVLLLSDLN
GNNQLGGNDN GNVVNLNNNF QLLNSLDLNS DIQTQPHRKW YLGAISQLPP HEIMGEIYRA
LKKVGFEWKL TGPYQLRCRM VNGKPIKLVL QLFRVAENRY LLDIKKIEGE IFIFFDICSL
MLEELNL
//
