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Database: UniProt
Entry: A0A3P9Q713_POERE
LinkDB: A0A3P9Q713_POERE
Original site: A0A3P9Q713_POERE 
ID   A0A3P9Q713_POERE        Unreviewed;       265 AA.
AC   A0A3P9Q713;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=5'-AMP-activated protein kinase subunit beta-1 {ECO:0000256|ARBA:ARBA00040010};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000029962.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000029962.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000029962.1};
RG   Ensembl;
RL   Submitted (SEP-2023) 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   -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1
CC       or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic
CC       subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2.
CC       {ECO:0000256|ARBA:ARBA00025878}.
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC       family. {ECO:0000256|ARBA:ARBA00010926}.
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DR   RefSeq; XP_008415783.1; XM_008417561.2.
DR   RefSeq; XP_008415784.1; XM_008417562.2.
DR   AlphaFoldDB; A0A3P9Q713; -.
DR   STRING; 8081.ENSPREP00000029962; -.
DR   Ensembl; ENSPRET00000030303.1; ENSPREP00000029962.1; ENSPREG00000020279.1.
DR   GeneID; 103469702; -.
DR   KEGG; pret:103469702; -.
DR   CTD; 335232; -.
DR   GeneTree; ENSGT00940000155307; -.
DR   OMA; IMMDSND; -.
DR   OrthoDB; 120305at2759; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000020279; Expressed in head and 1 other cell type or tissue.
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:SF96; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1; 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   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242638}.
FT   DOMAIN          175..265
FT                   /note="Association with the SNF1 complex (ASC)"
FT                   /evidence="ECO:0000259|SMART:SM01010"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  29550 MW;  DCE360578805FE6E CRC64;
     MGNSSSDRSS NERSFRDGPS GGKEARPNIM MDSNDDAELF HREDPKATPD IQEFLAWQQD
     LDCDSKEPAQ ARPTVFRWAG SAKEVFVSGS FNNWATKIPL NKSQNNFVAI VDLPEGEHQY
     KFCVDGQWTL DPTGPVTTTK TGTVNNVIQV NQTDFEVFDA LKIDSQDSTD LSDLSSSPPG
     PYQQNGYLIK PDDKIKQPPI LPPHLLQVLL NKDTGVSCDP TLLPEPNHVM LNHLYALSIK
     DGVMVLSATH RYKKKYVTTL LYKPI
//
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