ID A0A261CPN9_9PELO Unreviewed; 586 AA.
AC A0A261CPN9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=AMP-activated protein kinase glycogen-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=FL83_00213 {ECO:0000313|EMBL:OZG24487.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG24487.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZG24487.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZG24487.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) 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}.
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:OZG24487.1}.
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DR EMBL; NIPN01000001; OZG24487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261CPN9; -.
DR STRING; 1503980.A0A261CPN9; -.
DR Proteomes; UP000216463; Unassembled WGS sequence.
DR CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR CDD; cd19609; NTD_TDP-43; 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 InterPro; IPR041105; TDP43_N.
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; PF18694; TDP43_N; 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:UP000216463}.
FT DOMAIN 19..81
FT /note="TAR DNA-binding protein 43 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18694"
FT DOMAIN 509..585
FT /note="AMP-activated protein kinase glycogen-binding"
FT /evidence="ECO:0000259|Pfam:PF16561"
FT REGION 127..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..274
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 309..336
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 374..443
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 127..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZG24487.1"
SQ SEQUENCE 586 AA; 65976 MW; 34E7533869F3F19A CRC64;
MADVATKLPD ASWVRLEIEP VQVSHDGDET LNFATVQSVV PGAHGLYYRD DGERKALLFD
NNTGKVYPPP NGWDSVPIFI HLAHGSRHGT HFADYSKAND AFERNISAVQ KLFAAAGLGG
ARSNKVYTTG KTRARSTSKK NQPRSQFDAQ PENVNISEES EGRDSEKEKN DRQVEKLKNR
NDELKIRVKE YKSDLSAAQL KIKNLEKKLE TVKSTGYFDD NGDKFVRIDS ESDEKTQDHD
EEIKVHYSNL HNVIEELRNK LAAVESKKKE IEIKFSENQE YLKNAKDKVT YLENQLNSDA
HEEVKSTAVR ALEVKLGLAQ NSIRQIEADK QQLQEANWYA NERVGKLEQE NGYLKGITEQ
LKARADSSHV EKLLKESEKR VYEINEEKSK LEWRLGELSQ WWNDAKWKVG ELESSVALQR
NLLDTANSKI QSLNDELIQE VRTHSSTMSI PTDGFTISQG NRGTWNLANA SSQPCFTGAI
PSIPLVSALP FAGANPFIFG GANEGRNVTL TIAHTDHEVY LTGSFINWKC TLKCEKLSSG
KKGVTVNLTR GRHEFRFMIN GEWSTSTDYQ QVPNGLGGQN NVIFVE
//
