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Database: UniProt
Entry: A0A2G8LMW2_STIJA
LinkDB: A0A2G8LMW2_STIJA
Original site: A0A2G8LMW2_STIJA 
ID   A0A2G8LMW2_STIJA        Unreviewed;       374 AA.
AC   A0A2G8LMW2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Association with the SNF1 complex (ASC) domain-containing protein {ECO:0000259|SMART:SM01010};
GN   ORFNames=BSL78_01533 {ECO:0000313|EMBL:PIK61520.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK61520.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK61520.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK61520.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK61520.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIK61520.1}.
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DR   EMBL; MRZV01000030; PIK61520.1; -; Genomic_DNA.
DR   STRING; 307972.A0A2G8LMW2; -.
DR   Proteomes; UP000230750; Unassembled WGS sequence.
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: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:UP000230750}.
FT   DOMAIN          250..340
FT                   /note="Association with the SNF1 complex (ASC)"
FT                   /evidence="ECO:0000259|SMART:SM01010"
FT   REGION          73..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  42102 MW;  6992C0AE7781BF3E CRC64;
     MPLWKQKYIV FCAILSKRQI CRQPIKKYXN NLNTTVHIKH QDVSFDLQIF TVVVKQAVPH
     QQSLTGVHTV LTMGNAPGKR ESKDGSPLSP TKDGFDQKVF LQQASLDDTI DLQPRLERLM
     KAESGVEEDL RRGGRPRSST VNEASNSTAS SLPVVFKWDG TGKEIYVCGN FNNWQRIPMN
     KSHGNFTAIV DLPEGEYEYK FHVDGNWQHS TKQQTRNNKM GVTNNVVNVQ KSDFEVFEAL
     AIDSSTTKNR GSPPGEYGQT VPTKDTMDRS GGPPFLPPHL LQVILNKDIG PQYEPALLPE
     PNHVMLNHLY ALSIKDGVMV LSATHRYRKK YVTCLLYKPX LKAMKITELL FPISCYHGDG
     VGDIXQQMSI LRSD
//
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