ID A0A3B4VDJ1_SERDU Unreviewed; 269 AA.
AC A0A3B4VDJ1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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 Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000027980.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000027980.1}
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 -!- 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 AlphaFoldDB; A0A3B4VDJ1; -.
DR STRING; 41447.ENSSDUP00000027980; -.
DR Ensembl; ENSSDUT00000028471.1; ENSSDUP00000027980.1; ENSSDUG00000020217.1.
DR GeneTree; ENSGT00940000155307; -.
DR OMA; QPTVFRW; -.
DR OrthoDB; 120305at2759; -.
DR Proteomes; UP000261420; 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: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}.
FT DOMAIN 179..269
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 COMPBIAS 13..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 30324 MW; C957997446EF77D2 CRC64;
MGNTSSERAA MGQGEKAQRR DSRGIKEGER PKILMDSPED ADIFHGEDLK APLEKEEFLA
WQQDLEADDK APTLDRPTVF RWTGDGKEVY LSGSFNNWAN KIPLIRSQNT FVAIVDLPEG
EHQYKFYVDG QWTHDPAEPV VTSQLGTVNN VIQVKKTDFE VFDALMVDSQ KCSDMSDLSS
SPPGPYHQDA YIPKQEEKFK SPPILPPHLL QVILNKDTGI SCDPALLPEP NHVMLNHLYA
LSIKDGVMVL SATHRYKKKY VTTLLYKPI
//