ID A0A3Q1EHI0_9TELE Unreviewed; 344 AA.
AC A0A3Q1EHI0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Protein kinase, AMP-activated, gamma 2 non-catalytic subunit a {ECO:0000313|Ensembl:ENSAPOP00000003941.1};
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:ENSAPOP00000003941.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000003941.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 gamma
CC subunit family. {ECO:0000256|ARBA:ARBA00006750}.
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 AlphaFoldDB; A0A3Q1EHI0; -.
DR STRING; 80966.ENSAPOP00000003941; -.
DR Ensembl; ENSAPOT00000010895.1; ENSAPOP00000003941.1; ENSAPOG00000006000.1.
DR GeneTree; ENSGT00950000183019; -.
DR InParanoid; A0A3Q1EHI0; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR CDD; cd04618; CBS_euAMPK_gamma-like_repeat1; 1.
DR CDD; cd04641; CBS_euAMPK_gamma-like_repeat2; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR PANTHER; PTHR13780:SF122; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-2; 1.
DR PANTHER; PTHR13780; AMP-ACTIVATED PROTEIN KINASE, GAMMA REGULATORY SUBUNIT; 1.
DR Pfam; PF00571; CBS; 4.
DR SMART; SM00116; CBS; 4.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR PROSITE; PS51371; CBS; 4.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT DOMAIN 27..87
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 109..168
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 186..248
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 260..317
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 344 AA; 39431 MW; 522B99F79123D6F8 CRC64;
MCLTTCWVLG DIYMRFMKCH KCYDIIPTSS KLVVFDTTLQ VKKAFFALVA NGVRAAPLWE
SKKQSFVGML TITDFINILT RYYKSPMVQI YELEEHKIET WRELYLQETF KPLVHISPDA
SIFDAVYSLI KNKIHRLPVI DPVSGNALYI LTHKRILKFL NVYDNLNVCE MPMPAFMKQT
LEELGVGTYN NIAYIHPDTP LITALSVFTH RRVSALPVVD HHGKVVDIYS KFDVINLAAE
KTYNNLDVTV TQALRHRSQY FEGVMKCNRL ETLETIVDRI VKAEVHRLVV VDEESRIIGI
VSLSDILQAL VLTPAGTHTH THTHTHTHTI RHKETSHLSV CLQV
//
