ID A0A2I0MBX0_COLLI Unreviewed; 180 AA.
AC A0A2I0MBX0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=AMP-activated protein kinase glycogen-binding domain-containing protein {ECO:0000259|Pfam:PF16561};
DE Flags: Fragment;
GN ORFNames=A306_00000031 {ECO:0000313|EMBL:PKK27175.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK27175.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK27175.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK27175.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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 -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000256|ARBA:ARBA00010926}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK27175.1}.
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DR EMBL; AKCR02000021; PKK27175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0MBX0; -.
DR STRING; 8932.A0A2I0MBX0; -.
DR InParanoid; A0A2I0MBX0; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR032640; AMPK1_CBM.
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:SF92; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053872}.
FT DOMAIN 79..161
FT /note="AMP-activated protein kinase glycogen-binding"
FT /evidence="ECO:0000259|Pfam:PF16561"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 180
FT /evidence="ECO:0000313|EMBL:PKK27175.1"
SQ SEQUENCE 180 AA; 19927 MW; 935AC0CF1CE3BAA9 CRC64;
MGNTTSERVS GERHGSKSHR ADGSGAAHPA KEHPHKIMVG STDDPSVFSS HDSKIPGDKE
FMSWQPDLEE SKPSQQARPT VIRWADGGKE VFISGSFNNW STKIPLIKSH NDFVAILDLP
EGEHQYKFFV DGQWVHDPSE PVVTSQMGTI NNLIHVKKSD FEVFDALKVD SLESSETSGR
//
