GenomeNet

Database: UniProt
Entry: A5YT84_PETMA
LinkDB: A5YT84_PETMA
Original site: A5YT84_PETMA 
ID   A5YT84_PETMA            Unreviewed;       325 AA.
AC   A5YT84;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=AMP-activated protein kinase gamma B {ECO:0000313|EMBL:ABQ59298.1};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|EMBL:ABQ59298.1};
RN   [1] {ECO:0000313|EMBL:ABQ59298.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grignani R., Pinter K., Farza H., Khor C.C., Carballo S., Ling E.,
RA   Paterakis P., Grignani D., Peden J., Watkins H.;
RT   "Differential expression of AMPK gamma isoforms in vertebrate development
RT   and evolution: A mechanism for phenotype.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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   EMBL; EF584739; ABQ59298.1; -; mRNA.
DR   AlphaFoldDB; A5YT84; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; AMP-ACTIVATED PROTEIN KINASE, GAMMA REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR13780:SF35; LD22662P; 1.
DR   Pfam; PF00571; CBS; 3.
DR   SMART; SM00116; CBS; 4.
DR   SUPFAM; SSF54631; CBS-domain pair; 2.
DR   PROSITE; PS51371; CBS; 4.
PE   2: Evidence at transcript level;
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   Kinase {ECO:0000313|EMBL:ABQ59298.1};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW   Transferase {ECO:0000313|EMBL:ABQ59298.1}.
FT   DOMAIN          34..94
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          116..176
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          189..251
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          263..320
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   325 AA;  37308 MW;  A6A4F180F15DE5EC CRC64;
     MLETLHWYED QAEEGEESVY SRLMKAQCCY EVIPTSSKLV VFDISLQVKK AFFALVDSGV
     RAAPLWDSKL QTFVGMLTIT DFINILHRYY KSPMVQIYEL EEHKIETWRE VYLQDSFKPL
     VSITPEASLF DAVYSLIKNK IHRLPIIDPV SGNVLYILTH KRILRFLHLF ISELPKPRFM
     CRPLGELRVG TFNDIAFIYT DTPIITALNL FVERRVSALS VVDRSGRVVD VYSKFDVINL
     AAEKNYNNLD MTVTQALHHR SQYFEGVVKC RRHESLETIV GRLVHAEVHR VVVVDENDRV
     VGILSLSDYL QALILTPAGV DALNS
//
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