LOCUS NP_037142 330 aa linear ROD 27-APR-2025
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; RefSeq Select.
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 Bai,W., Guo,T., Wang,H., Li,B., Sun,Q., Wu,W., Zhang,J., Zhou,J.,
Luo,J., Zhu,M., Lu,J., Li,P., Dong,B., Han,S., Pang,X., Zhang,G.,
Bai,Y. and Wang,S.
TITLE S-nitrosylation of AMPKgamma impairs coronary collateral
circulation and disrupts VSMC reprogramming
JOURNAL EMBO Rep 25 (1), 128-143 (2024)
PUBMED 38177907
REMARK GeneRIF: S-nitrosylation of AMPKgamma impairs coronary collateral
circulation and disrupts VSMC reprogramming.
REFERENCE 2 (residues 1 to 330)
AUTHORS Jeon,Y.H., He,M., Austin,J., Shin,H., Pfleger,J. and Abdellatif,M.
TITLE Adiponectin enhances the bioenergetics of cardiac myocytes via an
AMPK- and succinate dehydrogenase-dependent mechanism
JOURNAL Cell Signal 78, 109866 (2021)
PUBMED 33271223
REMARK GeneRIF: Adiponectin enhances the bioenergetics of cardiac myocytes
via an AMPK- and succinate dehydrogenase-dependent mechanism.
REFERENCE 3 (residues 1 to 330)
AUTHORS Dopie,J., Rajakyla,E.K., Joensuu,M.S., Huet,G., Ferrantelli,E.,
Xie,T., Jaalinoja,H., Jokitalo,E. and Vartiainen,M.K.
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 4 (residues 1 to 330)
AUTHORS Xiao,B., Sanders,M.J., Underwood,E., Heath,R., Mayer,F.V.,
Carmena,D., Jing,C., Walker,P.A., Eccleston,J.F., Haire,L.F.,
Saiu,P., Howell,S.A., Aasland,R., Martin,S.R., Carling,D. and
Gamblin,S.J.
TITLE Structure of mammalian AMPK and its regulation by ADP
JOURNAL Nature 472 (7342), 230-233 (2011)
PUBMED 21399626
REFERENCE 5 (residues 1 to 330)
AUTHORS Zhu,L., Chen,L., Zhou,X.M., Zhang,Y.Y., Zhang,Y.J., Zhao,J.,
Ji,S.R., Wu,J.W. 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 6 (residues 1 to 330)
AUTHORS Cheung,P.C., Salt,I.P., Davies,S.P., Hardie,D.G. 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 (Pt 3), 659-669 (2000)
PUBMED 10698692
REFERENCE 7 (residues 1 to 330)
AUTHORS Turnley,A.M., Stapleton,D., Mann,R.J., Witters,L.A., Kemp,B.E. and
Bartlett,P.F.
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,P.C., Smith,F.C., Davison,M.D., Scott,J.,
Beri,R.K. 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,C.S., Stapleton,D., Auster,A.S., Widmer,J.,
Dyck,J.R., Kemp,B.E. and Witters,L.A.
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,B.J., Widmer,J., Mitchelhill,K.,
Teh,T., House,C.M., Witters,L.A. and Kemp,B.E.
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.
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 :: mixed sample support SAMD00132261,
SAMD00132262 [ECO:0006172]
##Evidence-Data-END##
##RefSeq-Attributes-START##
RefSeq Select criteria :: based on conservation, expression,
longest protein
##RefSeq-Attributes-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 1..25
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (P80385.3)"
Region 37..173
/region_name="CBS_euAMPK_gamma-like_repeat1"
/note="Two tandem repeats of the cystathionine
beta-synthase (CBS pair) domains found in AMP-activated
protein kinase gamma-like proteins, repeat 1; cd04618"
/db_xref="CDD:341388"
Site order(44,46..48,70..72,151,165,167,169..170,173)
/site_type="other"
/note="ligand binding site II [chemical binding]"
/db_xref="CDD:341388"
Region 44..117
/region_name="CBS repeat"
/note="CBS repeat [structural motif]"
/db_xref="CDD:341388"
Site order(70,84,88..89,92,129,151..153,169)
/site_type="other"
/note="ligand binding site I [chemical binding]"
/db_xref="CDD:341388"
Region 129..173
/region_name="CBS repeat"
/note="CBS repeat [structural motif]"
/db_xref="CDD:341388"
Region 137..158
/region_name="AMPK pseudosubstrate"
/note="propagated from UniProtKB/Swiss-Prot (P80385.3)"
Region 199..322
/region_name="CBS_euAMPK_gamma-like_repeat2"
/note="CBS pair domain found in 5'-AMP (adenosine
monophosphate)-activated protein kinase; cd04641"
/db_xref="CDD:341399"
Site order(200,202..204,226..228,298,311,313,315..316,319)
/site_type="other"
/note="ligand binding site II [chemical binding]"
/db_xref="CDD:341399"
Region 200..265
/region_name="CBS repeat"
/note="CBS repeat [structural motif]"
/db_xref="CDD:341399"
Site order(226,239,243..244,247,276,298..300,315)
/site_type="other"
/note="ligand binding site I [chemical binding]"
/db_xref="CDD:341399"
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)"
Region 276..319
/region_name="CBS repeat"
/note="CBS repeat [structural motif]"
/db_xref="CDD:341399"
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
//
