ID A0A3Q1EGQ4_9TELE Unreviewed; 271 AA.
AC A0A3Q1EGQ4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=5'-AMP-activated protein kinase subunit beta-2-like {ECO:0000313|Ensembl:ENSAPOP00000003621.1};
GN Name=PRKAB2 {ECO:0000313|Ensembl:ENSAPOP00000003621.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000003621.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000003621.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000256|ARBA:ARBA00010926}.
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DR AlphaFoldDB; A0A3Q1EGQ4; -.
DR STRING; 80966.ENSAPOP00000003621; -.
DR Ensembl; ENSAPOT00000011449.1; ENSAPOP00000003621.1; ENSAPOG00000005152.1.
DR GeneTree; ENSGT00940000159284; -.
DR InParanoid; A0A3Q1EGQ4; -.
DR Proteomes; UP000257200; Unplaced.
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:SF92; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2; 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:UP000257200}.
FT DOMAIN 181..271
FT /note="Association with the SNF1 complex (ASC)"
FT /evidence="ECO:0000259|SMART:SM01010"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 271 AA; 30106 MW; D7206B212BEE7A77 CRC64;
MGNTSDRVSG DRHGGKAHRS DSSGSHKDQE QSSKMVDSTD DPNIFNTHGP DSKASGEKEF
TPDLDDLVKT GPQARPTVIR WAGGGKEVYI AGSFNNWSTK IPLNKSHNDF VAILDLPEGE
HQYKFFVDGQ WVNDPSEPVV TSQLGTINNL IQVKKSDFEV FDALQVDSLE CSDTSGQTKC
QYSPPGPYGQ EQYVFRPEEH FKAPPILPPH LLQVILNKDT NISCDPALLP EPNHVMLNHL
YALSIKDGVM VLSATHRYKK KYVTSLLYKP I
//
