ID A0A1V9XUD6_9ACAR Unreviewed; 272 AA.
AC A0A1V9XUD6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=5'-AMP-activated protein kinase subunit beta-1-like {ECO:0000313|EMBL:OQR76978.1};
GN ORFNames=BIW11_07421 {ECO:0000313|EMBL:OQR76978.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR76978.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR76978.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR76978.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(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:OQR76978.1}.
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DR EMBL; MNPL01004081; OQR76978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XUD6; -.
DR STRING; 418985.A0A1V9XUD6; -.
DR InParanoid; A0A1V9XUD6; -.
DR OrthoDB; 120305at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:OQR76978.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Transferase {ECO:0000313|EMBL:OQR76978.1}.
FT DOMAIN 176..272
FT /note="Association with the SNF1 complex (ASC)"
FT /evidence="ECO:0000259|SMART:SM01010"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 272 AA; 30564 MW; 470E4798FD404537 CRC64;
MGNTSSGKRE RAFSSEVPCS PGKEDRALEF NTRRFHGQNS LEENEEFLNS LRQSEDYMRP
RASTVSDDKN GVLPTVFKWE KGGKDVSICG TFTQWKPIPM VKSHGDFVII LDVPEGEHEY
RFKVDGHWHL DDTEPTVEAE EGQSKNNVIK VKQSDFEVFE ALAVDSLATQ SANAISRSPP
GDYTQEIPTK FVQEPSPNGG EQQGPPILPP HLLQVILNKD IPLSCEPTLL PEPNHVMLNH
LYALSIKDGV MVLSGTQRYR KKYVTTLLYK PI
//
