ID AAKG2_MOUSE STANDARD; PRT; 566 AA. AC Q91WG5; Q6V7V5; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 21-MAR-2006, entry version 22. DE 5'-AMP-activated protein kinase, gamma-2 subunit (AMPK gamma-2 chain) DE (AMPK gamma2). GN Name=Prkag2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). RC STRAIN=C57BL/6J; RA Zhou G., Jiang D., Zhang Y.; RT "Cloning of mouse protein kinase, AMP-activated, gamma 2 non-catalytic RT subunit."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC STRAIN=FVB/N; TISSUE=Kidney; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: AMPK is responsible for the regulation of fatty acid CC synthesis by phosphorylation of acetyl-CoA carboxylase. Also CC regulates cholesterol synthesis via phosphorylation and CC inactivation of hydroxymethylglutaryl-CoA reductase and hormone- CC sensitive lipase. This is a regulatory subunit (By similarity). CC -!- SUBUNIT: Heterotrimer of an alpha catalytic subunit, a beta and a CC gamma non-catalytic regulatory subunits (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q91WG5-1; Sequence=Displayed; CC Name=B; CC IsoId=Q91WG5-2; Sequence=VSP_015586; CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma CC subunit family. CC -!- SIMILARITY: Contains 4 CBS domains. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY348864; AAQ55224.1; -; mRNA. DR EMBL; BC015283; AAH15283.1; -; mRNA. DR Ensembl; ENSMUSG00000028944; Mus musculus. DR MGI; MGI:1336153; Prkag2. DR GO; GO:0004679; F:AMP-activated protein kinase activity; TAS. DR GO; GO:0006695; P:cholesterol biosynthesis; RCA. DR GO; GO:0006633; P:fatty acid biosynthesis; RCA. DR GO; GO:0006950; P:response to stress; TAS. DR InterPro; IPR000644; CBS. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 4. KW Alternative splicing; CBS domain; Fatty acid biosynthesis; KW Lipid synthesis; Repeat. FT CHAIN 1 566 5'-AMP-activated protein kinase, gamma-2 FT subunit. FT /FTId=PRO_0000204382. FT DOMAIN 276 324 CBS 1. FT DOMAIN 357 405 CBS 2. FT DOMAIN 432 479 CBS 3. FT DOMAIN 504 551 CBS 4. FT VARSPLIC 1 240 Missing (in isoform B). FT /FTId=VSP_015586. FT CONFLICT 257 257 F -> V (in Ref. 1). FT CONFLICT 516 516 T -> N (in Ref. 1). SQ SEQUENCE 566 AA; 62997 MW; 754DE4D696102C7D CRC64; MGSAAMDTKK KKEVSSPGGS SGKKNPSLKR RSLRVHIPDL SSFAMPLLDG DVENSEKHSS RKVDSPFSSG SPSRGLFSRG PQPRPSSPVS APVRPKTSPG SPKTVFPFSY QESPPRSPRR MSFSGIFRSS SKESSPNSNP STSPGGIRFF SRSRKTSSVS SSPSTPTQVT KQHPFPLESY KQEPERPESR IYASSSPPDT GQRFCLAFQS PARPPLASPT YHAPLRTAVL AAAPGPAEAG MLEKLEFQEE EDSESGFYMR FMRSHKCYDI VPTSSKLVVF DTTLQVKKAF FALVANGVRA APLWESKKQS FVGMLTITDF INILHRYYKS PMVQIYELEE HKIETWRELY LQETFKPLVN ISPDASLFDA VYSLIKNKIH RLPVIDPISG NALYILTHKR ILKFLQLFMS DMPKPAFMKQ NLDELGIGTY HNIAFIHPDT PIIKALNIFV ERRISALPVV DESGKVVDIY SKFDVINLAA EKTYNNLDIT VTQALQHRSQ YFEGVVKCSK LETLETIVDR IVRAEVHRLV VVNEADSIVG IISLSDILQA LILTPAGAKQ KETETE //