ID AAKG2_MOUSE Reviewed; 566 AA. AC Q91WG5; E9QK80; Q6V7V5; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 24-JAN-2024, entry version 155. DE RecName: Full=5'-AMP-activated protein kinase subunit gamma-2; DE Short=AMPK gamma2; DE Short=AMPK subunit gamma-2; GN Name=Prkag2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; 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 GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC STRAIN=FVB/N; TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-71; SER-73; SER-90; RP SER-138; SER-143; SER-158; SER-161 AND SER-196, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-71; SER-143; SER-161; RP SER-162 AND THR-165, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, RC and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP PHOSPHORYLATION BY ULK1. RX PubMed=21460634; DOI=10.4161/auto.7.7.15451; RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.; RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory RT feedback loop."; RL Autophagy 7:696-706(2011). CC -!- FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase CC (AMPK), an energy sensor protein kinase that plays a key role in CC regulating cellular energy metabolism. In response to reduction of CC intracellular ATP levels, AMPK activates energy-producing pathways and CC inhibits energy-consuming processes: inhibits protein, carbohydrate and CC lipid biosynthesis, as well as cell growth and proliferation. AMPK acts CC via direct phosphorylation of metabolic enzymes, and by longer-term CC effects via phosphorylation of transcription regulators. Also acts as a CC regulator of cellular polarity by remodeling the actin cytoskeleton; CC probably by indirectly activating myosin. Gamma non-catalytic subunit CC mediates binding to AMP, ADP and ATP, leading to activate or inhibit CC AMPK: AMP-binding results in allosteric activation of alpha catalytic CC subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and CC preventing dephosphorylation of catalytic subunits. ADP also stimulates CC phosphorylation, without stimulating already phosphorylated catalytic CC subunit. ATP promotes dephosphorylation of catalytic subunit, rendering CC the AMPK enzyme inactive. {ECO:0000250|UniProtKB:Q9UGJ0}. 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 (By CC similarity). {ECO:0000250}. 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 -!- DOMAIN: The AMPK pseudosubstrate motif resembles the sequence around CC sites phosphorylated on target proteins of AMPK, except the presence of CC a non-phosphorylatable residue in place of Ser. In the absence of AMP CC this pseudosubstrate sequence may bind to the active site groove on the CC alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the CC upstream activating kinase STK11/LKB1 (By similarity). {ECO:0000250}. CC -!- DOMAIN: The 4 CBS domains mediate binding to nucleotides. Of the 4 CC potential nucleotide-binding sites, 3 are occupied, designated as sites CC 1, 3, and 4 based on the CBS modules that provide the acidic residue CC for coordination with the 2'- and 3'-hydroxyl groups of the ribose of CC AMP. Of these, site 4 appears to be a structural site that retains a CC tightly held AMP molecule (AMP 3). The 2 remaining sites, 1 and 3, can CC bind either AMP, ADP or ATP. Site 1 (AMP, ADP or ATP 1) is the high- CC affinity binding site and likely accommodates AMP or ADP. Site 3 (AMP, CC ADP or ATP 2) is the weakest nucleotide-binding site on the gamma CC subunit, yet it is exquisitely sensitive to changes in nucleotide CC levels and this allows AMPK to respond rapidly to changes in cellular CC energy status. Site 3 is likely to be responsible for protection of a CC conserved threonine in the activation loop of the alpha catalytic CC subunit through conformational changes induced by binding of AMP or CC ADP. {ECO:0000250|UniProtKB:P80385}. CC -!- PTM: Phosphorylated by ULK1; leading to negatively regulate AMPK CC activity and suggesting the existence of a regulatory feedback loop CC between ULK1 and AMPK. {ECO:0000269|PubMed:21460634}. CC -!- PTM: Glycosylated; O-GlcNAcylated by OGT, promoting the AMP-activated CC protein kinase (AMPK) activity. {ECO:0000250|UniProtKB:Q9UGJ0}. CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma CC subunit family. {ECO:0000305}. 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; AC116151; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC125270; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015283; AAH15283.1; -; mRNA. DR CCDS; CCDS19130.1; -. [Q91WG5-1] DR CCDS; CCDS51437.1; -. [Q91WG5-2] DR RefSeq; NP_001164027.1; NM_001170556.1. [Q91WG5-2] DR RefSeq; NP_663376.2; NM_145401.2. [Q91WG5-1] DR AlphaFoldDB; Q91WG5; -. DR SMR; Q91WG5; -. DR BioGRID; 223832; 8. DR ComplexPortal; CPX-5849; AMPK complex, alpha1-beta1-gamma2 variant. DR ComplexPortal; CPX-5858; AMPK complex, alpha2-beta1-gamma2 variant. DR ComplexPortal; CPX-5859; AMPK complex, alpha2-beta2-gamma2 variant. DR ComplexPortal; CPX-5860; AMPK complex, alpha1-beta2-gamma2 variant. DR IntAct; Q91WG5; 1. DR STRING; 10090.ENSMUSP00000030784; -. DR BindingDB; Q91WG5; -. DR ChEMBL; CHEMBL4524004; -. DR iPTMnet; Q91WG5; -. DR PhosphoSitePlus; Q91WG5; -. DR jPOST; Q91WG5; -. DR MaxQB; Q91WG5; -. DR PaxDb; 10090-ENSMUSP00000030784; -. DR ProteomicsDB; 286012; -. [Q91WG5-1] DR ProteomicsDB; 286013; -. [Q91WG5-2] DR Pumba; Q91WG5; -. DR Antibodypedia; 1327; 195 antibodies from 30 providers. DR DNASU; 108099; -. DR Ensembl; ENSMUST00000030784.14; ENSMUSP00000030784.8; ENSMUSG00000028944.15. [Q91WG5-1] DR Ensembl; ENSMUST00000114975.8; ENSMUSP00000110626.2; ENSMUSG00000028944.15. [Q91WG5-2] DR GeneID; 108099; -. DR KEGG; mmu:108099; -. DR UCSC; uc008wsk.2; mouse. [Q91WG5-1] DR AGR; MGI:1336153; -. DR CTD; 51422; -. DR MGI; MGI:1336153; Prkag2. DR VEuPathDB; HostDB:ENSMUSG00000028944; -. DR eggNOG; KOG1764; Eukaryota. DR GeneTree; ENSGT00950000183019; -. DR HOGENOM; CLU_021740_6_0_1; -. DR InParanoid; Q91WG5; -. DR OMA; XVQIYEL; -. DR OrthoDB; 880743at2759; -. DR PhylomeDB; Q91WG5; -. DR TreeFam; TF313247; -. DR Reactome; R-MMU-1632852; Macroautophagy. DR Reactome; R-MMU-163680; AMPK inhibits chREBP transcriptional activation activity. DR Reactome; R-MMU-200425; Carnitine metabolism. DR Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK. DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation. DR BioGRID-ORCS; 108099; 4 hits in 81 CRISPR screens. DR ChiTaRS; Prkag2; mouse. DR PRO; PR:Q91WG5; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q91WG5; Protein. DR Bgee; ENSMUSG00000028944; Expressed in seminiferous tubule of testis and 259 other cell types or tissues. DR ExpressionAtlas; Q91WG5; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISO:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0043531; F:ADP binding; ISO:MGI. DR GO; GO:0016208; F:AMP binding; ISO:MGI. DR GO; GO:0004679; F:AMP-activated protein kinase activity; TAS:MGI. DR GO; GO:0005524; F:ATP binding; ISO:MGI. DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; ISO:MGI. DR GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; ISO:MGI. DR GO; GO:0008607; F:phosphorylase kinase regulator activity; ISO:MGI. DR GO; GO:0030295; F:protein kinase activator activity; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0019887; F:protein kinase regulator activity; ISS:UniProtKB. DR GO; GO:0031669; P:cellular response to nutrient levels; ISS:ComplexPortal. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0005977; P:glycogen metabolic process; ISO:MGI. DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI. DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI. DR GO; GO:0019217; P:regulation of fatty acid metabolic process; ISO:MGI. DR GO; GO:0006110; P:regulation of glycolytic process; ISO:MGI. 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:SF122; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-2; 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. DR Genevisible; Q91WG5; MM. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; CBS domain; Fatty acid biosynthesis; KW Fatty acid metabolism; Glycoprotein; Lipid biosynthesis; Lipid metabolism; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..566 FT /note="5'-AMP-activated protein kinase subunit gamma-2" FT /id="PRO_0000204382" FT DOMAIN 272..332 FT /note="CBS 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703" FT DOMAIN 354..412 FT /note="CBS 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703" FT DOMAIN 427..489 FT /note="CBS 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703" FT DOMAIN 501..559 FT /note="CBS 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703" FT REGION 1..198 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 367..388 FT /note="AMPK pseudosubstrate" FT COMPBIAS 1..17 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 102..175 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 299 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 299 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 299 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 299 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 314..319 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 314..319 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 314..319 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 359 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 359 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 359 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 380..381 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 380..381 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 380..381 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 380 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 381 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 399 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 399 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 399 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 429 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 434 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 455..456 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 471..474 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 471..474 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 471..474 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 498 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 498 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 498 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 527..528 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 527..528 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 527..528 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 527 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P80385" FT BINDING 543..546 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P80385" FT MOD_RES 65 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 71 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 73 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 90 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 158 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 162 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 165 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 196 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT VAR_SEQ 1..240 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_015586" FT CONFLICT 257 FT /note="V -> F (in Ref. 3; AAH15283)" FT /evidence="ECO:0000305" FT CONFLICT 516 FT /note="T -> N (in Ref. 1; AAQ55224)" FT /evidence="ECO:0000305" SQ SEQUENCE 566 AA; 62949 MW; D112BFD69D1C5ACB 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 EDSESGVYMR 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 //