ID A0A087RHZ5_APTFO Unreviewed; 273 AA.
AC A0A087RHZ5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=5'-AMP-activated protein kinase subunit beta-1 {ECO:0000256|ARBA:ARBA00040010};
GN ORFNames=AS27_08333 {ECO:0000313|EMBL:KFM13099.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM13099.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM13099.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM13099.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK),
CC an 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. Beta non-catalytic subunit
CC acts as a scaffold on which the AMPK complex assembles, via its C-
CC terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits
CC (PRKAG1, PRKAG2 or PRKAG3). {ECO:0000256|ARBA:ARBA00025180}.
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:0000256|ARBA:ARBA00025878}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000256|ARBA:ARBA00010926}.
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DR EMBL; KL226375; KFM13099.1; -; Genomic_DNA.
DR RefSeq; XP_019329732.1; XM_019474187.1.
DR AlphaFoldDB; A0A087RHZ5; -.
DR STRING; 9233.A0A087RHZ5; -.
DR GeneID; 103905767; -.
DR CTD; 5564; -.
DR OrthoDB; 120305at2759; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR Gene3D; 6.20.250.60; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR006828; ASC_dom.
DR InterPro; IPR037256; ASC_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR10343; 5'-AMP-ACTIVATED PROTEIN KINASE , BETA SUBUNIT; 1.
DR PANTHER; PTHR10343:SF96; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR Pfam; PF04739; AMPKBI; 1.
DR SMART; SM01010; AMPKBI; 1.
DR SUPFAM; SSF160219; AMPKBI-like; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KFM13099.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW Transferase {ECO:0000313|EMBL:KFM13099.1}.
FT DOMAIN 183..273
FT /note="Association with the SNF1 complex (ASC)"
FT /evidence="ECO:0000259|SMART:SM01010"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 273 AA; 30647 MW; F6D44972A760ACF1 CRC64;
MGNTSSERAG LERHGHKASR GDNSGGAIST KEGDRPKILM DSPEDADLFH SEEMKAPLEK
EEFLAWQQDL EVNDKTPTQA RPTVFRWTGG GKEVYLSGSF NNWSKIPLTR SHNNFVAILD
LPEGEHQYKF FVDGQWTHDP SEPVVTSQLG TVNNIIQVKK TDFEVFDALM VDSQKCSDMS
ELSSSPPGPY HQEPYVCKAE ERFKSPPILP PHLLQVILNK DTGISCDPAL LPEPNHVMLN
HLYALSIKDG VMVLSATHRY KKKYVTTLLY KPI
//
