GenomeNet

Database: RefSeq
Entry: NP_037142
LinkDB: NP_037142
Original site: NP_037142 
LOCUS       NP_037142                330 aa            linear   ROD 19-JUN-2020
DEFINITION  5'-AMP-activated protein kinase subunit gamma-1 [Rattus
            norvegicus].
ACCESSION   NP_037142
VERSION     NP_037142.1
DBSOURCE    REFSEQ: accession NM_013010.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Dopie J, Rajakyla EK, Joensuu MS, Huet G, Ferrantelli E, Xie T,
            Jaalinoja H, Jokitalo E and Vartiainen MK.
  TITLE     Genome-wide RNAi screen for nuclear actin reveals a network of
            cofilin regulators
  JOURNAL   J. Cell. Sci. 128 (13), 2388-2400 (2015)
   PUBMED   26021350
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Xiao B, Sanders MJ, Underwood E, Heath R, Mayer FV, Carmena D, Jing
            C, Walker PA, Eccleston JF, Haire LF, Saiu P, Howell SA, Aasland R,
            Martin SR, Carling D and Gamblin SJ.
  TITLE     Structure of mammalian AMPK and its regulation by ADP
  JOURNAL   Nature 472 (7342), 230-233 (2011)
   PUBMED   21399626
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Zhu L, Chen L, Zhou XM, Zhang YY, Zhang YJ, Zhao J, Ji SR, Wu JW
            and Wu Y.
  TITLE     Structural insights into the architecture and allostery of
            full-length AMP-activated protein kinase
  JOURNAL   Structure 19 (4), 515-522 (2011)
   PUBMED   21481774
  REMARK    GeneRIF: Studies determine the three-dimensional reconstruction and
            subunit organization of the full-length rat AMPK
            (alpha1beta1gamma1) through single-particle electron
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Ghosh D, Lippert D, Krokhin O, Cortens JP and Wilkins JA.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Jiang W, Zhu Z and Thompson HJ.
  TITLE     Dietary energy restriction modulates the activity of AMP-activated
            protein kinase, Akt, and mammalian target of rapamycin in mammary
            carcinomas, mammary gland, and liver
  JOURNAL   Cancer Res. 68 (13), 5492-5499 (2008)
   PUBMED   18593953
  REMARK    GeneRIF: Dietary energy restriction modulates the activity of
            AMP-activated protein kinase in mammary carcinomas, mammary gland,
            and liver.
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Cheung PC, Salt IP, Davies SP, Hardie DG and Carling D.
  TITLE     Characterization of AMP-activated protein kinase gamma-subunit
            isoforms and their role in AMP binding
  JOURNAL   Biochem. J. 346 Pt 3, 659-669 (2000)
   PUBMED   10698692
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Turnley AM, Stapleton D, Mann RJ, Witters LA, Kemp BE and Bartlett
            PF.
  TITLE     Cellular distribution and developmental expression of AMP-activated
            protein kinase isoforms in mouse central nervous system
  JOURNAL   J. Neurochem. 72 (4), 1707-1716 (1999)
   PUBMED   10098881
REFERENCE   8  (residues 1 to 330)
  AUTHORS   Woods A, Cheung PC, Smith FC, Davison MD, Scott J, Beri RK and
            Carling D.
  TITLE     Characterization of AMP-activated protein kinase beta and gamma
            subunits. Assembly of the heterotrimeric complex in vitro
  JOURNAL   J. Biol. Chem. 271 (17), 10282-10290 (1996)
   PUBMED   8626596
REFERENCE   9  (residues 1 to 330)
  AUTHORS   Gao G, Fernandez CS, Stapleton D, Auster AS, Widmer J, Dyck JR,
            Kemp BE and Witters LA.
  TITLE     Non-catalytic beta- and gamma-subunit isoforms of the
            5'-AMP-activated protein kinase
  JOURNAL   J. Biol. Chem. 271 (15), 8675-8681 (1996)
   PUBMED   8621499
REFERENCE   10 (residues 1 to 330)
  AUTHORS   Stapleton D, Gao G, Michell BJ, Widmer J, Mitchelhill K, Teh T,
            House CM, Witters LA and Kemp BE.
  TITLE     Mammalian 5'-AMP-activated protein kinase non-catalytic subunits
            are homologs of proteins that interact with yeast Snf1 protein
            kinase
  JOURNAL   J. Biol. Chem. 269 (47), 29343-29346 (1994)
   PUBMED   7961907
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097940.1.
            
            Summary: non-catalytic component of the heterotrimeric
            AMP-activated protein kinase; may phosphorylate and inactivate
            enzymes involved in lipid metabolism; may play a role in response
            to metabolic stress [RGD, Feb 2006].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097940.1, X95578.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01906349 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..330
                     /product="5'-AMP-activated protein kinase subunit gamma-1"
                     /note="AMP-activated protein kinase, noncatalytic gamma-1
                     subunit; protein kinase, AMP-activated, gamma 1
                     non-catalytic subunit; AMPKg; AMPK gamma-1 chain; AMPK
                     gamma1; AMPK subunit gamma-1; Protein kinase AMP-activated
                     gamma"
                     /calculated_mol_wt=37255
     Region          45..174
                     /region_name="CBS_pair_5"
                     /note="The CBS domain, named after human CBS, is a small
                     domain originally identified in cystathionine
                     beta-synthase and is subsequently found in a wide range of
                     different proteins. CBS domains usually occur in tandem
                     repeats. They associate to form a so-called...; cd04618"
                     /db_xref="CDD:239990"
     Region          137..158
                     /region_name="AMPK pseudosubstrate"
                     /note="propagated from UniProtKB/Swiss-Prot (P80385.3)"
     Region          201..320
                     /region_name="CBS_pair_28"
                     /note="The CBS domain, named after human CBS, is a small
                     domain originally identified in cystathionine
                     beta-synthase and is subsequently found in a wide range of
                     different proteins. CBS domains usually occur in tandem
                     repeats. They associate to form a so-called...; cd04641"
                     /db_xref="CDD:240012"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ULK1.
                     /evidence=ECO:0000305|PubMed:21460634; propagated from
                     UniProtKB/Swiss-Prot (P80385.3)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ULK1.
                     /evidence=ECO:0000305|PubMed:21460634; propagated from
                     UniProtKB/Swiss-Prot (P80385.3)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ULK1.
                     /evidence=ECO:0000269|PubMed:21460634; propagated from
                     UniProtKB/Swiss-Prot (P80385.3)"
     CDS             1..330
                     /gene="Prkag1"
                     /gene_synonym="Prkaac; Prkga1"
                     /coded_by="NM_013010.2:17..1009"
                     /db_xref="GeneID:25520"
                     /db_xref="RGD:3388"
ORIGIN      
        1 mesvaaesap apenehsqet pesnssvytt fmkshrcydl iptssklvvf dtslqvkkaf
       61 falvtngvra aplwdskkqs fvgmltitdf inilhryyks alvqiyelee hkietwrevy
      121 lqdsfkplvc ispnaslfda vsslirnkih rlpvidpesg ntlyilthkr ilkflklfit
      181 efpkpefmsk sleelqigty aniamvrttt pvyvalgifv qhrvsalpvv dekgrvvdiy
      241 skfdvinlaa ektynnldvs vtkalqhrsh yfegvlkcyl hetleaiinr lveaevhrlv
      301 vvdehdvvkg ivslsdilqa lvltggekkp
//
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