(data stored in ACNUC26462 zone)

HOGENOM: MOUSE4_PE1556

ID   MOUSE4_PE1556                        STANDARD;      PRT;   552 AA.
AC   MOUSE4_PE1556; Q8BRK8; B1ASQ8; Q3UYM4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-2;
DE   Short=AMPK subunit alpha-2; EC=2.7.11 1; (MOUSE4.PE1556).
GN   Name=Prkaa2;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE4.PE1556.
CC       Mus musculus chromosome 4 NCBIM37  sequence 1..155630120 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:AAPK2_MOUSE
CC   -!- FUNCTION: Responsible for the regulation of fatty acid synthesis
CC       by phosphorylation of acetyl-CoA carboxylase. It also regulates
CC       cholesterol synthesis via phosphorylation and inactivation of
CC       hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase.
CC       Appears to act as a metabolic stress-sensing protein kinase
CC       switching off biosynthetic pathways when cellular ATP levels are
CC       depleted and when 5'-AMP rises in response to fuel limitation
CC       and/or hypoxia. This is a catalytic subunit.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Binding of AMP results in allosteric
CC       activation, inducing phosphorylation on Thr-172. Also activated by
CC       phosphorylation by CAMKK2 triggered by a rise in intracellular
CC       calcium ions, without detectable changes in the AMP/ATP ratio (By
CC       similarity).
CC   -!- SUBUNIT: Heterotrimer of a catalytic subunit, a beta and a gamma
CC       non-catalytic subunits (By similarity).
CC   -!- PTM: Phosphorylated at Thr-172 by STK11/LKB1 in complex with
CC       STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39 (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice develop obesity when animals are fed a
CC       high-fat diet, as a result of an enhanced lipid accumulation in
CC       pre-existing adipocytes but not in other tissues.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. SNF1 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- GENE_FAMILY: HOG000233016 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000028518;ENSMUST00000030243;ENSMUSP00000030243.
DR   EMBL; AK044030; - ;
DR   EMBL; AK134573; - ;
DR   EMBL; AL627307; - ;
DR   EMBL; AL929466; - ;
DR   EMBL; BC138565; - ;
DR   EMBL; BC138566; - ;
DR   UniProtKB/Swiss-Prot; Q8BRK8; B1ASQ8; Q3UYM4; -.
DR   EMBL; AL627307; CAM18832.1; -; Genomic_DNA.
DR   EMBL; AL929466; CAM18832.1; JOINED; Genomic_DNA.
DR   EMBL; AL929466; CAM24127.1; -; Genomic_DNA.
DR   EMBL; AL627307; CAM24127.1; JOINED; Genomic_DNA.
DR   EMBL; BC138565; AAI38566.1; -; mRNA.
DR   EMBL; BC138566; AAI38567.1; -; mRNA.
DR   EMBL; AK044030; BAC31746.1; -; mRNA.
DR   EMBL; AK134573; BAE22188.1; -; mRNA.
DR   IPI; IPI00123445; -.
DR   RefSeq; NP_835279.2; NM_178143.2.
DR   UniGene; Mm.48638; -.
DR   HSSP; P06782; 2EUE.
DR   ProteinModelPortal; Q8BRK8; -.
DR   STRING; Q8BRK8; -.
DR   PhosphoSite; Q8BRK8; -.
DR   PRIDE; Q8BRK8; -.
DR   Ensembl; ENSMUST00000030243; ENSMUSP00000030243; ENSMUSG00000028518.
DR   GeneID; 108079; -.
DR   CTD; 5563; -.
DR   MGI; MGI:1336173; Prkaa2.
DR   eggNOG; roNOG12508; -.
DR   GeneTree; ENSGT00600000084026; -.
DR   InParanoid; Q8BRK8; -.
DR   OrthoDB; EOG4XSKPM; -.
DR   PhylomeDB; Q8BRK8; -.
DR   NextBio; 360016; -.
DR   ArrayExpress; Q8BRK8; -.
DR   Bgee; Q8BRK8; -.
DR   Genevestigator; Q8BRK8; -.
DR   GermOnline; ENSMUSG00000028518; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   HOGENOMDNA; MOUSE4.PE1556; -.
KW   ENSMUSG000000285185old_1320000031; ENSMUSP000000302431old_1320000031;
KW   B1ASQ8_MOUSE; AK044030; AK134573; AL627307; AL929466; BC138565; BC138566;
KW   Acetylation; ATP-binding; Cholesterol biosynthesis; Complete proteome;
KW   Fatty acid biosynthesis; Kinase; Lipid synthesis; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Steroid biosynthesis;
KW   Sterol biosynthesis; Transferase.
SQ   SEQUENCE   552 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ KIRSLDVVGK
     IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE LFDYICKHGR VEEVEARRLF
     QQILSAVDYC HRHMVVHRDL KPENVLLDAQ MNAKIADFGL SNMMSDGEFL RTSCGSPNYA
     APEVISGRLY AGPEVDIWSC GVILYALLCG TLPFDDEHVP TLFKKIRGGV FYIPDYLNRS
     VATLLMHMLQ VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIDD EAVKEVCEKF
     ECTESEVMNS LYSGDPQDQL AVAYHLIIDN RRIMNQASEF YLASSPPSGS FMDDSAMHIP
     PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA KWHLGIRSQS KACDIMAEVY
     RAMKQLGFEW KVVNAYHLRV RRKNPVTGNY VKMSLQLYLV DSRSYLLDFK SIDDEVVEQR
     SGSSTPQRSC SAAGLHRARS SFDSSTAENH SLSGSLTGSL TGSTLSSASP RLGSHTMDFF
     EMCASLITAL AR
//

If you have problems or comments...

PBIL Back to PBIL home page