ID A8X4W7_CAEBR Unreviewed; 268 AA.
AC A8X4W7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Protein CBR-AAKB-1 {ECO:0000313|EMBL:CAP27677.1};
GN Name=aakb-1 {ECO:0000313|WormBase:CBG07378};
GN Synonyms=Cbr-aakb-1 {ECO:0000313|EMBL:CAP27677.1};
GN ORFNames=CBG07378 {ECO:0000313|WormBase:CBG07378}, CBG_07378
GN {ECO:0000313|EMBL:CAP27677.1};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP27677.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP27677.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP27677.1,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE601041; CAP27677.1; -; Genomic_DNA.
DR RefSeq; XP_002645713.1; XM_002645667.1.
DR AlphaFoldDB; A8X4W7; -.
DR STRING; 6238.A8X4W7; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR EnsemblMetazoa; CBG07378.1; CBG07378.1; WBGene00029442.
DR GeneID; 8587712; -.
DR KEGG; cbr:CBG_07378; -.
DR CTD; 8587712; -.
DR WormBase; CBG07378; CBP07603; WBGene00029442; Cbr-aakb-1.
DR eggNOG; KOG1616; Eukaryota.
DR HOGENOM; CLU_070949_2_2_1; -.
DR InParanoid; A8X4W7; -.
DR OMA; IPPHKPW; -.
DR OrthoDB; 120305at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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:UP000008549}.
FT DOMAIN 178..268
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"
FT REGION 156..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 268 AA; 30046 MW; 3BFF6A4F5767C26D CRC64;
MGNNQPGGMY KRDRPFDSEK GGSKSRTGAP SASPPNEDEC PVQMKIAKSD DKTKLFPVVF
KWNQANTSAR NVAICGSWDK WNQRIPLVKS SGDFSTIVDL EPGKHEYKFY VDHKWVVDDN
QQKTSNHLGG ENNVVMIDEA DYEVFDALDK DLASSNAGEA LRSNHPTKES HDTPNDRELE
KLHQFGQETP TRADFGKAAP PPVLPPHLLQ VILNKDTPVQ CDPNVLPEPD HVMLNHLYAL
SIKDGVMVLS ATHRYRKKFV TTLLYKPI
//
