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Database: UniProt
Entry: A0A3Q2DX31_CYPVA
LinkDB: A0A3Q2DX31_CYPVA
Original site: A0A3Q2DX31_CYPVA 
ID   A0A3Q2DX31_CYPVA        Unreviewed;       385 AA.
AC   A0A3Q2DX31;
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-1-like {ECO:0000313|Ensembl:ENSCVAP00000024461.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000024461.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000024461.1}
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}.
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DR   AlphaFoldDB; A0A3Q2DX31; -.
DR   Ensembl; ENSCVAT00000004134.1; ENSCVAP00000024461.1; ENSCVAG00000008537.1.
DR   GeneTree; ENSGT00950000183019; -.
DR   Proteomes; UP000265020; 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; 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:UP000265020}.
FT   DOMAIN          62..123
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          144..205
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          220..278
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          287..350
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   385 AA;  43643 MW;  D5BBCE8E515977BD CRC64;
     MEAFAEVPLF EMDEYEEEEV LSMRSKGASS YATYPMAPPA GTDPDAYIYM NFMKSHSCYD
     AMPRSSKLVI FDTTLQVKKA FFALVANGVR AAPLWDSKLQ CFVGMLTITD FINILHRYYK
     SPLVQIYELE EHKIETWREI YLQYSVNRLI SIKPESSLFD AIYSLLKNKI HRLPVIDPTS
     GNVLHILTHK RILKFLHIFG SMIPKPRFLQ KQINEVPIGT FRQIATVQES ASVYEALAIF
     VERRVSALPV VNEQGKVVAL YSRFDVINLA AQKNYNNLNM TMKEAIASRS CWVEGVLKCY
     PHETLETIID RIAKAEVHRL VLVDREDVVR GIVSLSDILQ SLVLSPAVSS STTINNVHLS
     YEKPVSQIFT SGQAFKCKGK QDGNG
//
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