ID A0A3P6U698_LITSI Unreviewed; 340 AA.
AC A0A3P6U698;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Association with the SNF1 complex (ASC) domain-containing protein {ECO:0000259|SMART:SM01010};
GN ORFNames=NLS_LOCUS1731 {ECO:0000313|EMBL:VDK72241.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK72241.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK72241.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) 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 -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000256|ARBA:ARBA00010926}.
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DR EMBL; UYRX01000066; VDK72241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P6U698; -.
DR STRING; 42156.A0A3P6U698; -.
DR Proteomes; UP000277928; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:SF84; ALICORN, ISOFORM A; 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 Reference proteome {ECO:0000313|Proteomes:UP000277928}.
FT DOMAIN 250..340
FT /note="Association with the SNF1 complex (ASC)"
FT /evidence="ECO:0000259|SMART:SM01010"
FT REGION 47..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 340 AA; 37478 MW; 3D69FA4CB0F44719 CRC64;
MQQNEVVKNI MKRGTKKRGI SLFLTNDSSD NKQGDCRGEA AEEDKVAGCG MGNNQGGLHK
RERALDGQHR SRQWATSSAP GGSGASSNMM SGSGTTEDGC PVQVKIAKSD GSVSTPSIQF
SEANEYPVVF KWQGGSQAGG VYISGSWDGW KRMTPLCKST QDFSTIINLS PGRHEYKFFI
DGKWVVDENA AKTDNKFGSQ NNVISIDEAD FEVFDALDRD LASSNAGEAM RKVNVTGAPP
SSHDTPNERE IEKLKNFTQE IPDRREFEKA QNPPVLPPHL LQVILNKDTP MQCDPNVLPE
PNHVMLNHLY ALSIKDGVMV LSATHRYRKK YVTTLLYKPI
//
