ID A0A3B3UCH2_9TELE Unreviewed; 267 AA.
AC A0A3B3UCH2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=5'-AMP-activated protein kinase subunit beta-2-like {ECO:0000313|Ensembl:ENSPLAP00000010359.1};
GN Name=PRKAB2 {ECO:0000313|Ensembl:ENSPLAP00000010359.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000010359.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000010359.1}
RP IDENTIFICATION.
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 -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000256|ARBA:ARBA00010926}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014873889.1; XM_015018403.1.
DR RefSeq; XP_014873890.1; XM_015018404.1.
DR AlphaFoldDB; A0A3B3UCH2; -.
DR STRING; 48699.ENSPLAP00000010359; -.
DR Ensembl; ENSPLAT00000017415.1; ENSPLAP00000010359.1; ENSPLAG00000013268.1.
DR GeneID; 106937073; -.
DR KEGG; plai:106937073; -.
DR CTD; 5565; -.
DR GeneTree; ENSGT00940000159284; -.
DR OrthoDB; 120305at2759; -.
DR Proteomes; UP000261500; 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;
FT DOMAIN 177..267
FT /note="Association with the SNF1 complex (ASC)"
FT /evidence="ECO:0000259|SMART:SM01010"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 267 AA; 29580 MW; EA7FC160DB00C9BF CRC64;
MGNTSDRVSG DRHGKAHRTD SGGSHKDQES GSKMVDSTDD PNVFNTHGPE SKSSGDKEFT
PDLDDLVKTG PQARPTVIRW AGGGKEVYIA GSFNNWSNKI PLNKSHNDFV AILDLPEGEH
QYKFFVDGQW LHDPSEPVVT SQLGTINNLI TVKKSDFEVF DALQVDSLEC SDTSDLSSSP
PGPYGQEQYI FRPEEHFKAP PILPPHLLQV ILNKDTNVSC DPALLPEPNH VMLNHLYALS
IKDGVMVLSA THRYKKKYVT SLLYKPI
//
