ID A0A0K0D5X2_ANGCA Unreviewed; 260 AA.
AC A0A0K0D5X2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=AMPK1_CBM domain-containing protein {ECO:0000313|WBParaSite:ACAC_0000546701-mRNA-1};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000546701-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0000546701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0K0D5X2; -.
DR STRING; 6313.A0A0K0D5X2; -.
DR WBParaSite; ACAC_0000546701-mRNA-1; ACAC_0000546701-mRNA-1; ACAC_0000546701.
DR Proteomes; UP000035642; 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:SF84; ALICORN, ISOFORM A; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000035642}.
FT DOMAIN 189..259
FT /note="AMP-activated protein kinase glycogen-binding"
FT /evidence="ECO:0000259|Pfam:PF16561"
FT COILED 5..39
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 63..125
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 260 AA; 29813 MW; 8E79BB2FBA25A250 CRC64;
LETKLQLANQ SFRNSEAERQ KYEQINRDTM KHVVQLENEN GRLRGITEEL SSKLRDSASV
QVLDEKDARL RDLADERSRL QWRIGELCQW WSDAKWKIGE LEAGLAHQRH LLDTANIKIQ
SLNEQAPQPS TTYVMPPSSY SVSQPPFPNQ WRFANTCLPS PVYALTPLCH SHLPTCETKR
VKIEIEHGNQ QDIFLMGSFL DWKWALRCDP IGEGKSGVTL DLPRGRHEFR FLVDGRWLTS
SLHTKVPNGL GGDNNLLCIE
//
