AAKG1_HUMAN
ID AAKG1_HUMAN Reviewed; 331 AA.
AC P54619; B4DDT7; Q8N7V9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=5'-AMP-activated protein kinase subunit gamma-1;
DE Short=AMPK gamma1;
DE Short=AMPK subunit gamma-1;
DE Short=AMPKg;
GN Name=PRKAG1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fetal liver;
RX PubMed=8621499; DOI=10.1074/jbc.271.15.8675;
RA Gao G., Fernandez C.S., Stapleton D., Auster A.S., Widmer J., Dyck J.R.B.,
RA Kemp B.E., Witters L.A.;
RT "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated
RT protein kinase.";
RL J. Biol. Chem. 271:8675-8681(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Glial tumor, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [6]
RP DOMAIN CBS, AMP-BINDING, AND ATP-BINDING.
RX PubMed=14722619; DOI=10.1172/jci200419874;
RA Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A.,
RA Norman D.G., Hardie D.G.;
RT "CBS domains form energy-sensing modules whose binding of adenosine ligands
RT is disrupted by disease mutations.";
RL J. Clin. Invest. 113:274-284(2004).
RN [7]
RP INTERACTION WITH FNIP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17028174; DOI=10.1073/pnas.0603781103;
RA Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L., Iwamatsu A.,
RA Esposito D., Gillette W.K., Hopkins R.F. III, Hartley J.L., Furihata M.,
RA Oishi S., Zhen W., Burke T.R. Jr., Linehan W.M., Schmidt L.S., Zbar B.;
RT "Folliculin encoded by the BHD gene interacts with a binding protein,
RT FNIP1, and AMPK, and is involved in AMPK and mTOR signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006).
RN [8]
RP DOMAIN AMPK PSEUDOSUBSTRATE.
RX PubMed=17255938; DOI=10.1038/sj.emboj.7601542;
RA Scott J.W., Ross F.A., Liu J.K., Hardie D.G.;
RT "Regulation of AMP-activated protein kinase by a pseudosubstrate sequence
RT on the gamma subunit.";
RL EMBO J. 26:806-815(2007).
RN [9]
RP INTERACTION WITH FNIP2.
RX PubMed=18403135; DOI=10.1016/j.gene.2008.02.022;
RA Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M., Valera V.A.,
RA Linehan W.M., Schmidt L.S.;
RT "Identification and characterization of a novel folliculin-interacting
RT protein FNIP2.";
RL Gene 415:60-67(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION BY ULK1 AND ULK2.
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).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH PRKAA1 AND PRKAB1, DOMAIN CBS, ADP-BINDING, MUTAGENESIS OF
RP ASP-90; ASP-245 AND ASP-317, AND FUNCTION.
RX PubMed=21680840; DOI=10.1126/science.1200094;
RA Oakhill J.S., Steel R., Chen Z.P., Scott J.W., Ling N., Tam S., Kemp B.E.;
RT "AMPK is a direct adenylate charge-regulated protein kinase.";
RL Science 332:1433-1435(2011).
RN [14]
RP REVIEW ON FUNCTION.
RX PubMed=17307971; DOI=10.1161/01.res.0000256090.42690.05;
RA Towler M.C., Hardie D.G.;
RT "AMP-activated protein kinase in metabolic control and insulin signaling.";
RL Circ. Res. 100:328-341(2007).
RN [15]
RP REVIEW ON FUNCTION.
RX PubMed=17712357; DOI=10.1038/nrm2249;
RA Hardie D.G.;
RT "AMP-activated/SNF1 protein kinases: conserved guardians of cellular
RT energy.";
RL Nat. Rev. Mol. Cell Biol. 8:774-785(2007).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17] {ECO:0007744|PDB:2UV4, ECO:0007744|PDB:2UV5, ECO:0007744|PDB:2UV6, ECO:0007744|PDB:2UV7}
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 182-325 IN COMPLEX WITH AMP.
RX PubMed=17452784; DOI=10.1107/s0907444907009110;
RA Day P., Sharff A., Parra L., Cleasby A., Williams M., Hoerer S., Nar H.,
RA Redemann N., Tickle I., Yon J.;
RT "Structure of a CBS-domain pair from the regulatory gamma1 subunit of human
RT AMPK in complex with AMP and ZMP.";
RL Acta Crystallogr. D 63:587-596(2007).
RN [18] {ECO:0007744|PDB:4CFE, ECO:0007744|PDB:4CFF}
RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) IN COMPLEX WITH AMP.
RX PubMed=24352254; DOI=10.1038/ncomms4017;
RA Xiao B., Sanders M.J., Carmena D., Bright N.J., Haire L.F., Underwood E.,
RA Patel B.R., Heath R.B., Walker P.A., Hallen S., Giordanetto F.,
RA Martin S.R., Carling D., Gamblin S.J.;
RT "Structural basis of AMPK regulation by small molecule activators.";
RL Nat. Commun. 4:3017-3017(2013).
RN [19] {ECO:0007744|PDB:4RER, ECO:0007744|PDB:4REW}
RP X-RAY CRYSTALLOGRAPHY (4.05 ANGSTROMS) OF 24-327 IN COMPLEX WITH AMP.
RX PubMed=25412657; DOI=10.1038/cr.2014.150;
RA Li X., Wang L., Zhou X.E., Ke J., de Waal P.W., Gu X., Tan M.H., Wang D.,
RA Wu D., Xu H.E., Melcher K.;
RT "Structural basis of AMPK regulation by adenine nucleotides and glycogen.";
RL Cell Res. 25:50-66(2015).
RN [20] {ECO:0007744|PDB:4ZHX, ECO:0007744|PDB:5EZV}
RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 2-331 IN COMPLEX WITH AMP.
RX PubMed=26952388; DOI=10.1038/ncomms10912;
RA Langendorf C.G., Ngoei K.R., Scott J.W., Ling N.X., Issa S.M., Gorman M.A.,
RA Parker M.W., Sakamoto K., Oakhill J.S., Kemp B.E.;
RT "Structural basis of allosteric and synergistic activation of AMPK by
RT furan-2-phosphonic derivative C2 binding.";
RL Nat. Commun. 7:10912-10912(2016).
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:0000269|PubMed:21680840}.
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:0000269|PubMed:17028174, ECO:0000269|PubMed:18403135,
CC ECO:0000269|PubMed:21680840}.
CC -!- INTERACTION:
CC P54619; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-1181439, EBI-946029;
CC P54619; P55212: CASP6; NbExp=3; IntAct=EBI-1181439, EBI-718729;
CC P54619; P35520: CBS; NbExp=3; IntAct=EBI-1181439, EBI-740135;
CC P54619; Q14145: KEAP1; NbExp=6; IntAct=EBI-1181439, EBI-751001;
CC P54619; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-1181439, EBI-11959885;
CC P54619; P60412: KRTAP10-11; NbExp=5; IntAct=EBI-1181439, EBI-10217483;
CC P54619; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-1181439, EBI-10172150;
CC P54619; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-1181439, EBI-739863;
CC P54619; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-1181439, EBI-10172511;
CC P54619; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-1181439, EBI-1044640;
CC P54619; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-1181439, EBI-11958364;
CC P54619; P50221: MEOX1; NbExp=3; IntAct=EBI-1181439, EBI-2864512;
CC P54619; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1181439, EBI-16439278;
CC P54619; P26367: PAX6; NbExp=3; IntAct=EBI-1181439, EBI-747278;
CC P54619; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-1181439, EBI-742388;
CC P54619; Q13131: PRKAA1; NbExp=14; IntAct=EBI-1181439, EBI-1181405;
CC P54619; P54646: PRKAA2; NbExp=13; IntAct=EBI-1181439, EBI-1383852;
CC P54619; Q9Y478: PRKAB1; NbExp=12; IntAct=EBI-1181439, EBI-719769;
CC P54619; O43741: PRKAB2; NbExp=17; IntAct=EBI-1181439, EBI-1053424;
CC P54619; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-1181439, EBI-5280197;
CC P54619; Q969V4: TEKT1; NbExp=6; IntAct=EBI-1181439, EBI-10180409;
CC P54619; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-1181439, EBI-2505861;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P54619-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54619-2; Sequence=VSP_046711;
CC Name=3;
CC IsoId=P54619-3; Sequence=VSP_046712;
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.
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:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254,
CC ECO:0000269|PubMed:25412657}.
CC -!- PTM: Phosphorylated by ULK1 and ULK2; leading to negatively regulate
CC AMPK activity and suggesting the existence of a regulatory feedback
CC loop between ULK1, ULK2 and AMPK. {ECO:0000269|PubMed:21460634}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
CC subunit family. {ECO:0000305}.
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DR EMBL; U42412; AAC50495.1; -; mRNA.
DR EMBL; BT007345; AAP36009.1; -; mRNA.
DR EMBL; AK097606; BAC05117.1; -; mRNA.
DR EMBL; AK293332; BAG56848.1; -; mRNA.
DR EMBL; AC011603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000358; AAH00358.1; -; mRNA.
DR CCDS; CCDS55824.1; -. [P54619-2]
DR CCDS; CCDS55825.1; -. [P54619-3]
DR CCDS; CCDS8777.1; -. [P54619-1]
DR RefSeq; NP_001193638.1; NM_001206709.1. [P54619-3]
DR RefSeq; NP_001193639.1; NM_001206710.1. [P54619-2]
DR RefSeq; NP_002724.1; NM_002733.4. [P54619-1]
DR RefSeq; XP_006719562.1; XM_006719499.2.
DR RefSeq; XP_011536864.1; XM_011538562.2. [P54619-2]
DR PDB; 2UV4; X-ray; 1.33 A; A=182-325.
DR PDB; 2UV5; X-ray; 1.69 A; A=182-325.
DR PDB; 2UV6; X-ray; 2.00 A; A=182-325.
DR PDB; 2UV7; X-ray; 2.00 A; A=182-325.
DR PDB; 4CFE; X-ray; 3.02 A; E/F=1-331.
DR PDB; 4CFF; X-ray; 3.92 A; E/F=1-331.
DR PDB; 4RER; X-ray; 4.05 A; G=24-327.
DR PDB; 4REW; X-ray; 4.58 A; G=24-327.
DR PDB; 4ZHX; X-ray; 2.99 A; E/F=2-331.
DR PDB; 5EZV; X-ray; 2.99 A; E/F=2-331.
DR PDB; 5ISO; X-ray; 2.63 A; E/F=1-331.
DR PDB; 6B1U; X-ray; 2.77 A; E/F=2-331.
DR PDB; 6B2E; X-ray; 3.80 A; C=2-331.
DR PDB; 6C9F; X-ray; 2.92 A; C=1-331.
DR PDB; 6C9G; X-ray; 2.70 A; C=1-331.
DR PDB; 6C9H; X-ray; 2.65 A; C=1-331.
DR PDB; 6C9J; X-ray; 3.05 A; C=1-325.
DR PDB; 7JHG; EM; 3.47 A; G=24-327.
DR PDB; 7JHH; EM; 3.92 A; G=24-327.
DR PDB; 7JIJ; X-ray; 5.50 A; G=24-327.
DR PDB; 7M74; EM; 3.93 A; G=24-327.
DR PDBsum; 2UV4; -.
DR PDBsum; 2UV5; -.
DR PDBsum; 2UV6; -.
DR PDBsum; 2UV7; -.
DR PDBsum; 4CFE; -.
DR PDBsum; 4CFF; -.
DR PDBsum; 4RER; -.
DR PDBsum; 4REW; -.
DR PDBsum; 4ZHX; -.
DR PDBsum; 5EZV; -.
DR PDBsum; 5ISO; -.
DR PDBsum; 6B1U; -.
DR PDBsum; 6B2E; -.
DR PDBsum; 6C9F; -.
DR PDBsum; 6C9G; -.
DR PDBsum; 6C9H; -.
DR PDBsum; 6C9J; -.
DR PDBsum; 7JHG; -.
DR PDBsum; 7JHH; -.
DR PDBsum; 7JIJ; -.
DR PDBsum; 7M74; -.
DR AlphaFoldDB; P54619; -.
DR SMR; P54619; -.
DR BioGRID; 111558; 132.
DR ComplexPortal; CPX-5633; AMPK complex, alpha1-beta1-gamma1 variant.
DR ComplexPortal; CPX-5787; AMPK complex, alpha2-beta1-gamma1 variant.
DR ComplexPortal; CPX-5790; AMPK complex, alpha2-beta2-gamma1 variant.
DR ComplexPortal; CPX-5791; AMPK complex, alpha1-beta2-gamma1 variant.
DR CORUM; P54619; -.
DR DIP; DIP-39974N; -.
DR IntAct; P54619; 74.
DR MINT; P54619; -.
DR STRING; 9606.ENSP00000323867; -.
DR BindingDB; P54619; -.
DR ChEMBL; CHEMBL2393; -.
DR DrugBank; DB00945; Acetylsalicylic acid.
DR DrugBank; DB00131; Adenosine phosphate.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB00273; Topiramate.
DR GlyGen; P54619; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P54619; -.
DR PhosphoSitePlus; P54619; -.
DR BioMuta; PRKAG1; -.
DR DMDM; 1703037; -.
DR EPD; P54619; -.
DR jPOST; P54619; -.
DR MassIVE; P54619; -.
DR MaxQB; P54619; -.
DR PaxDb; P54619; -.
DR PeptideAtlas; P54619; -.
DR PRIDE; P54619; -.
DR ProteomicsDB; 3890; -.
DR ProteomicsDB; 56688; -. [P54619-1]
DR Antibodypedia; 25778; 466 antibodies from 34 providers.
DR DNASU; 5571; -.
DR Ensembl; ENST00000316299.9; ENSP00000323867.5; ENSG00000181929.13. [P54619-3]
DR Ensembl; ENST00000548065.7; ENSP00000447433.1; ENSG00000181929.13. [P54619-1]
DR Ensembl; ENST00000552212.5; ENSP00000448972.1; ENSG00000181929.13. [P54619-2]
DR GeneID; 5571; -.
DR KEGG; hsa:5571; -.
DR MANE-Select; ENST00000548065.7; ENSP00000447433.1; NM_002733.5; NP_002724.1.
DR UCSC; uc001rsy.4; human. [P54619-1]
DR CTD; 5571; -.
DR DisGeNET; 5571; -.
DR GeneCards; PRKAG1; -.
DR HGNC; HGNC:9385; PRKAG1.
DR HPA; ENSG00000181929; Low tissue specificity.
DR MIM; 602742; gene.
DR neXtProt; NX_P54619; -.
DR OpenTargets; ENSG00000181929; -.
DR PharmGKB; PA33751; -.
DR VEuPathDB; HostDB:ENSG00000181929; -.
DR eggNOG; KOG1764; Eukaryota.
DR GeneTree; ENSGT00950000183019; -.
DR HOGENOM; CLU_021740_3_0_1; -.
DR OMA; ACVKMLE; -.
DR OrthoDB; 631088at2759; -.
DR PhylomeDB; P54619; -.
DR TreeFam; TF313247; -.
DR BRENDA; 2.7.11.31; 2681.
DR PathwayCommons; P54619; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-9613354; Lipophagy.
DR Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs.
DR SignaLink; P54619; -.
DR SIGNOR; P54619; -.
DR BioGRID-ORCS; 5571; 46 hits in 1086 CRISPR screens.
DR ChiTaRS; PRKAG1; human.
DR EvolutionaryTrace; P54619; -.
DR GeneWiki; PRKAG1; -.
DR GenomeRNAi; 5571; -.
DR Pharos; P54619; Tchem.
DR PRO; PR:P54619; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P54619; protein.
DR Bgee; ENSG00000181929; Expressed in gastrocnemius and 202 other tissues.
DR ExpressionAtlas; P54619; baseline and differential.
DR Genevisible; P54619; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0043531; F:ADP binding; ISS:UniProtKB.
DR GO; GO:0016208; F:AMP binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; TAS:ProtInc.
DR GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; TAS:BHF-UCL.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
DR GO; GO:0019887; F:protein kinase regulator activity; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR GO; GO:0031669; P:cellular response to nutrient levels; IDA:ComplexPortal.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0051170; P:import into nucleus; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; TAS:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; IBA:GO_Central.
DR GO; GO:0006110; P:regulation of glycolytic process; TAS:BHF-UCL.
DR GO; GO:0071900; P:regulation of protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR Gene3D; 3.10.580.10; -; 2.
DR IDEAL; IID00660; -.
DR InterPro; IPR039166; AMPKG-1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR PANTHER; PTHR13780:SF38; PTHR13780:SF38; 1.
DR Pfam; PF00571; CBS; 3.
DR SMART; SM00116; CBS; 4.
DR SUPFAM; SSF54631; SSF54631; 2.
DR PROSITE; PS51371; CBS; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; CBS domain;
KW Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..331
FT /note="5'-AMP-activated protein kinase subunit gamma-1"
FT /id="PRO_0000204377"
FT DOMAIN 43..103
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 125..187
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 198..260
FT /note="CBS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 272..329
FT /note="CBS 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 138..159
FT /note="AMPK pseudosubstrate"
FT BINDING 70
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 70
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24352254,
FT ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 85..90
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 85..90
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24352254,
FT ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFE"
FT BINDING 85..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 130
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 130
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24352254,
FT ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFE"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 151..152
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 151..152
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24352254,
FT ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFE"
FT BINDING 151..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 151
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17452784,
FT ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657,
FT ECO:0007744|PDB:4CFF"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 170
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 170
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24352254,
FT ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF"
FT BINDING 170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 200
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17452784,
FT ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657,
FT ECO:0007744|PDB:4CFF"
FT BINDING 205
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17452784,
FT ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657,
FT ECO:0007744|PDB:4CFF"
FT BINDING 226..227
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17452784,
FT ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657,
FT ECO:0007744|PDB:4CFF"
FT BINDING 242..245
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 242..245
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24352254,
FT ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF"
FT BINDING 242..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 269
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 269
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24352254,
FT ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 277
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 277
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24352254,
FT ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 298..299
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 298..299
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24352254,
FT ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF"
FT BINDING 298..299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT BINDING 298
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17452784,
FT ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657,
FT ECO:0007744|PDB:4CFF"
FT BINDING 314..317
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17452784,
FT ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657,
FT ECO:0007744|PDB:4CFF"
FT MOD_RES 261
FT /note="Phosphoserine; by ULK1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT MOD_RES 263
FT /note="Phosphothreonine; by ULK1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT MOD_RES 270
FT /note="Phosphoserine; by ULK1"
FT /evidence="ECO:0000250|UniProtKB:P80385"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046711"
FT VAR_SEQ 83
FT /note="V -> VVLRALSCPL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046712"
FT VARIANT 89
FT /note="T -> S (in dbSNP:rs1126930)"
FT /id="VAR_033453"
FT VARIANT 329
FT /note="K -> N (in dbSNP:rs34210356)"
FT /id="VAR_033454"
FT MUTAGEN 90
FT /note="D->A: Reduced AMP-activation of phosphorylation of
FT PRKAA1 or PRKAA2. Reduced ADP activation of phosphorylation
FT of PRKAA1 or PRKAA2."
FT /evidence="ECO:0000269|PubMed:21680840"
FT MUTAGEN 245
FT /note="D->A: Reduced AMP-activation of phosphorylation of
FT PRKAA1 or PRKAA2. Reduced ADP activation of phosphorylation
FT of PRKAA1 or PRKAA2."
FT /evidence="ECO:0000269|PubMed:21680840"
FT MUTAGEN 317
FT /note="D->A: Reduced AMP-activation of phosphorylation of
FT PRKAA1 or PRKAA2. Does not affect ADP activation of
FT phosphorylation of PRKAA1 or PRKAA2."
FT /evidence="ECO:0000269|PubMed:21680840"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:5ISO"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:5ISO"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:5ISO"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:5ISO"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:5ISO"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:5ISO"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:5ISO"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:5ISO"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6B1U"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:5ISO"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:5ISO"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:6C9F"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:6C9G"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:5ISO"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5ISO"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:5ISO"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:5ISO"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:5ISO"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5ISO"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:2UV4"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6B1U"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:2UV4"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6C9F"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:2UV4"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:2UV4"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:2UV4"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:2UV4"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:5EZV"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:2UV4"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:2UV4"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2UV4"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:2UV4"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:2UV4"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:2UV4"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:2UV4"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:5EZV"
SQ SEQUENCE 331 AA; 37579 MW; 0F22B9CA1DBD87AE CRC64;
METVISSDSS PAVENEHPQE TPESNNSVYT SFMKSHRCYD LIPTSSKLVV FDTSLQVKKA
FFALVTNGVR AAPLWDSKKQ SFVGMLTITD FINILHRYYK SALVQIYELE EHKIETWREV
YLQDSFKPLV CISPNASLFD AVSSLIRNKI HRLPVIDPES GNTLYILTHK RILKFLKLFI
TEFPKPEFMS KSLEELQIGT YANIAMVRTT TPVYVALGIF VQHRVSALPV VDEKGRVVDI
YSKFDVINLA AEKTYNNLDV SVTKALQHRS HYFEGVLKCY LHETLETIIN RLVEAEVHRL
VVVDENDVVK GIVSLSDILQ ALVLTGGEKK P
