GenomeNet

Database: UniProt
Entry: A0A3Q4GM74_NEOBR
LinkDB: A0A3Q4GM74_NEOBR
Original site: A0A3Q4GM74_NEOBR 
ID   A0A3Q4GM74_NEOBR        Unreviewed;       326 AA.
AC   A0A3Q4GM74;
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=5'-AMP-activated protein kinase subunit gamma-2-like {ECO:0000313|Ensembl:ENSNBRP00000010076.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000010076.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000010076.1}
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}.
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DR   AlphaFoldDB; A0A3Q4GM74; -.
DR   Ensembl; ENSNBRT00000010356.1; ENSNBRP00000010076.1; ENSNBRG00000007411.1.
DR   GeneTree; ENSGT00950000183019; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000007411; Expressed in zone of skin and 4 other cell types or tissues.
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:SF41; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1 ISOFORM X1; 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; 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:UP000261580}.
FT   DOMAIN          43..103
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          122..180
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          197..260
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          264..323
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   326 AA;  36821 MW;  1AE9D1230BC64FA9 CRC64;
     MKVEMPNPVQ TVCCDQLVYF LLEADATVYM KFMKSHCCYD AIPTSCKLVI FDTTLQVKKA
     FYALVANGLR AAPLWDSKLQ RFVGMLTITD FINILHCYYK SPMVQMYELE SHKIETWRGD
     SLQSIPLLIS SPSSLFEAIY SLLRYKIHRL PVIDPESGNV LHILTHKRIL KFLHIFGKKP
     PKPAFTKRPI QELGIGTFRN IATVQQTASL YDALSIFVER RVSALPVVDE QGTLYSAVAN
     LAAQKTYNNL DMTMQEAVEK RICCVEGVIK CYPYETLDII IDRIVKAEVH RLVLVDRADV
     VKGIISLSDL LQAMVLTPAG IDALLS
//
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