ID A0A3B5AMJ7_9TELE Unreviewed; 376 AA.
AC A0A3B5AMJ7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=5'-AMP-activated protein kinase subunit gamma-1-like {ECO:0000313|Ensembl:ENSSPAP00000022100.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000022100.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000022100.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B5AMJ7; -.
DR Ensembl; ENSSPAT00000022450.1; ENSSPAP00000022100.1; ENSSPAG00000016026.1.
DR GeneTree; ENSGT00950000183019; -.
DR Proteomes; UP000261400; 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:SF31; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-3; 1.
DR PANTHER; PTHR13780; AMP-ACTIVATED PROTEIN KINASE, GAMMA REGULATORY SUBUNIT; 1.
DR Pfam; PF00571; CBS; 3.
DR SMART; SM00116; CBS; 4.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR PROSITE; PS51371; CBS; 3.
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}.
FT DOMAIN 185..240
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 242..300
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 314..373
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 376 AA; 42478 MW; FD166FE2F66B557A CRC64;
MLFWFCGAAG LYVAVKHEPR VKTNSQNLLL GAQRVKQTRT RLFLLPFHVQ TKHQTLWSFS
RNPCCVSAGG CSYAAVAPPA DSDPDTFIYM NFMKSHCCYD AIPTSSKLVI FDTTLQVKKA
FFALVANGVR AAPLWDNKLK CFVGMLTITD FINILHRYYK SPLVQIYELE EHKIETWREI
YLQYSINRLI SITPDSSLFD AIYSLLKNKI HRLPVIDPAS GNVLHILTHK RILKMSLFPI
GTFKEIATVQ ESASVYDALT IFVERRVSAL PVVNEEGKVV ALYSRFDVIN LAAQKNYNNL
NMTMREAVSS RGGWMEGVLK CYPHETLETI IDRIAKAEVH RLVLVDRDNV VRGIVSLSDL
LQALVLTPAG IDALYS
//