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Database: UniProt
Entry: P80385
LinkDB: P80385
Original site: P80385 
ID   AAKG1_RAT               Reviewed;         330 AA.
AC   P80385; Q4QQW6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   17-JUN-2020, entry version 157.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RX   PubMed=8626596; DOI=10.1074/jbc.271.17.10282;
RA   Woods A., Cheung P.C.F., Smith F.C., Davison M.D., Scott J., Beri R.K.,
RA   Carling D.;
RT   "Characterization of AMP-activated protein kinase beta and gamma subunits.
RT   Assembly of the heterotrimeric complex in vitro.";
RL   J. Biol. Chem. 271:10282-10290(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-330.
RC   STRAIN=Sprague-Dawley; TISSUE=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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 48-330, AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=7961907;
RA   Stapleton D., Gao G., Michell B.J., Widmer J., Mitchelhill K.I., Teh T.,
RA   House C.M., Witters L.A., Kemp B.E.;
RT   "Mammalian 5'-AMP-activated protein kinase non-catalytic subunits are
RT   homologs of proteins that interact with yeast Snf1 protein kinase.";
RL   J. Biol. Chem. 269:29343-29346(1994).
RN   [5]
RP   PHOSPHORYLATION BY ULK1 AND ULK2, AND PHOSPHORYLATION AT SER-260; THR-262
RP   AND SER-269.
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   [6] {ECO:0000244|PDB:2V8Q, ECO:0000244|PDB:2V92, ECO:0000244|PDB:2V9J}
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PRKAA1 AND PRKAB2,
RP   FUNCTION, DOMAIN CBS, AMP-BINDING, AND ATP-BINDING.
RX   PubMed=17851531; DOI=10.1038/nature06161;
RA   Xiao B., Heath R., Saiu P., Leiper F.C., Leone P., Jing C., Walker P.A.,
RA   Haire L., Eccleston J.F., Davis C.T., Martin S.R., Carling D.,
RA   Gamblin S.J.;
RT   "Structural basis for AMP binding to mammalian AMP-activated protein
RT   kinase.";
RL   Nature 449:496-500(2007).
RN   [7] {ECO:0000244|PDB:2Y8L, ECO:0000244|PDB:2Y8Q, ECO:0000244|PDB:2YA3, ECO:0000244|PDB:4CFH}
RP   X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) IN COMPLEX WITH PRKAA1 AND PRKAB2,
RP   FUNCTION, DOMAIN CBS, AND ADP-BINDING.
RX   PubMed=21399626; DOI=10.1038/nature09932;
RA   Xiao B., Sanders M.J., Underwood E., Heath R., Mayer F.V., Carmena D.,
RA   Jing C., Walker P.A., Eccleston J.F., Haire L.F., Saiu P., Howell S.A.,
RA   Aasland R., Martin S.R., Carling D., Gamblin S.J.;
RT   "Structure of mammalian AMPK and its regulation by ADP.";
RL   Nature 472:230-233(2011).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEXES WITH AMP AND ATP.
RX   PubMed=22659875; DOI=10.1038/nsmb.2319;
RA   Chen L., Wang J., Zhang Y.Y., Yan S.F., Neumann D., Schlattner U.,
RA   Wang Z.X., Wu J.W.;
RT   "AMP-activated protein kinase undergoes nucleotide-dependent conformational
RT   changes.";
RL   Nat. Struct. Mol. Biol. 19:716-718(2012).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.34 ANGSTROMS) IN COMPLEXES WITH ADP AND AMP.
RX   PubMed=25066137; DOI=10.1016/j.str.2014.06.009;
RA   Calabrese M.F., Rajamohan F., Harris M.S., Caspers N.L., Magyar R.,
RA   Withka J.M., Wang H., Borzilleri K.A., Sahasrabudhe P.V., Hoth L.R.,
RA   Geoghegan K.F., Han S., Brown J., Subashi T.A., Reyes A.R., Frisbie R.K.,
RA   Ward J., Miller R.A., Landro J.A., Londregan A.T., Carpino P.A., Cabral S.,
RA   Smith A.C., Conn E.L., Cameron K.O., Qiu X., Kurumbail R.G.;
RT   "Structural basis for AMPK activation: natural and synthetic ligands
RT   regulate kinase activity from opposite poles by different molecular
RT   mechanisms.";
RL   Structure 22:1161-1172(2014).
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:17851531,
CC       ECO:0000269|PubMed:21399626}.
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:17851531, ECO:0000269|PubMed:21399626}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart and brain, also found in
CC       kidney, white adipose tissue, lung and spleen.
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:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626,
CC       ECO:0000269|PubMed:22659875, ECO:0000269|PubMed:25066137}.
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. There is some ambiguity for a
CC       phosphosite: Ser-260/Thr-262. {ECO:0000269|PubMed:21460634}.
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
CC       subunit family. {ECO:0000305}.
DR   EMBL; X95578; CAA64831.1; -; mRNA.
DR   EMBL; BC097940; AAH97940.1; -; mRNA.
DR   EMBL; U42413; AAC52580.1; -; mRNA.
DR   PIR; T10759; T10759.
DR   RefSeq; NP_037142.1; NM_013010.2.
DR   PDB; 2V8Q; X-ray; 2.10 A; E=1-330.
DR   PDB; 2V92; X-ray; 2.40 A; E=1-330.
DR   PDB; 2V9J; X-ray; 2.53 A; E=1-330.
DR   PDB; 2Y8L; X-ray; 2.50 A; E=1-330.
DR   PDB; 2Y8Q; X-ray; 2.80 A; E=1-330.
DR   PDB; 2YA3; X-ray; 2.51 A; E=1-330.
DR   PDB; 4CFH; X-ray; 3.24 A; E=1-330.
DR   PDB; 4EAG; X-ray; 2.70 A; C=1-330.
DR   PDB; 4EAI; X-ray; 2.28 A; C=1-330.
DR   PDB; 4EAJ; X-ray; 2.61 A; C=1-330.
DR   PDB; 4EAK; X-ray; 2.50 A; C=1-330.
DR   PDB; 4EAL; X-ray; 2.51 A; C=1-330.
DR   PDB; 4QFG; X-ray; 3.46 A; C=1-330.
DR   PDB; 4QFR; X-ray; 3.34 A; C=1-330.
DR   PDB; 4QFS; X-ray; 3.55 A; C=1-330.
DR   PDB; 5KQ5; X-ray; 3.41 A; C=1-330.
DR   PDB; 5T5T; X-ray; 3.46 A; C=1-330.
DR   PDB; 5UFU; X-ray; 3.45 A; C=1-330.
DR   PDB; 6E4T; X-ray; 3.40 A; C=1-330.
DR   PDB; 6E4U; X-ray; 3.27 A; C=1-330.
DR   PDB; 6E4W; X-ray; 3.35 A; C=1-330.
DR   PDBsum; 2V8Q; -.
DR   PDBsum; 2V92; -.
DR   PDBsum; 2V9J; -.
DR   PDBsum; 2Y8L; -.
DR   PDBsum; 2Y8Q; -.
DR   PDBsum; 2YA3; -.
DR   PDBsum; 4CFH; -.
DR   PDBsum; 4EAG; -.
DR   PDBsum; 4EAI; -.
DR   PDBsum; 4EAJ; -.
DR   PDBsum; 4EAK; -.
DR   PDBsum; 4EAL; -.
DR   PDBsum; 4QFG; -.
DR   PDBsum; 4QFR; -.
DR   PDBsum; 4QFS; -.
DR   PDBsum; 5KQ5; -.
DR   PDBsum; 5T5T; -.
DR   PDBsum; 5UFU; -.
DR   PDBsum; 6E4T; -.
DR   PDBsum; 6E4U; -.
DR   PDBsum; 6E4W; -.
DR   SMR; P80385; -.
DR   BioGRID; 247552; 2.
DR   DIP; DIP-37278N; -.
DR   IntAct; P80385; 4.
DR   STRING; 10116.ENSRNOP00000020093; -.
DR   BindingDB; P80385; -.
DR   ChEMBL; CHEMBL3885503; -.
DR   iPTMnet; P80385; -.
DR   PhosphoSitePlus; P80385; -.
DR   jPOST; P80385; -.
DR   PaxDb; P80385; -.
DR   PRIDE; P80385; -.
DR   Ensembl; ENSRNOT00000083354; ENSRNOP00000070458; ENSRNOG00000061499.
DR   GeneID; 25520; -.
DR   KEGG; rno:25520; -.
DR   UCSC; RGD:3388; rat.
DR   CTD; 5571; -.
DR   RGD; 3388; Prkag1.
DR   eggNOG; KOG1764; Eukaryota.
DR   eggNOG; COG0517; LUCA.
DR   GeneTree; ENSGT00940000156707; -.
DR   InParanoid; P80385; -.
DR   KO; K07200; -.
DR   OrthoDB; 631088at2759; -.
DR   PhylomeDB; P80385; -.
DR   TreeFam; TF313247; -.
DR   BRENDA; 2.7.11.31; 5301.
DR   Reactome; R-RNO-1632852; Macroautophagy.
DR   Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   EvolutionaryTrace; P80385; -.
DR   PRO; PR:P80385; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000061499; Expressed in heart and 9 other tissues.
DR   ExpressionAtlas; P80385; baseline and differential.
DR   Genevisible; P80385; RN.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR   GO; GO:0016208; F:AMP binding; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR   GO; GO:0019887; F:protein kinase regulator activity; IDA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0051170; P:import into nucleus; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR   GO; GO:0050790; P:regulation of catalytic activity; IDA:RGD.
DR   GO; GO:0071900; P:regulation of protein serine/threonine kinase activity; IEA:InterPro.
DR   InterPro; IPR039166; AMPKG-1.
DR   InterPro; IPR000644; CBS_dom.
DR   PANTHER; PTHR13780:SF38; PTHR13780:SF38; 1.
DR   Pfam; PF00571; CBS; 3.
DR   SMART; SM00116; CBS; 4.
DR   PROSITE; PS51371; CBS; 4.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; CBS domain; Direct protein sequencing;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..330
FT                   /note="5'-AMP-activated protein kinase subunit gamma-1"
FT                   /id="PRO_0000204380"
FT   DOMAIN          42..102
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          124..186
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          197..259
FT                   /note="CBS 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          271..328
FT                   /note="CBS 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   NP_BIND         86..89
FT                   /note="AMP, ADP or ATP 1"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   NP_BIND         150..151
FT                   /note="AMP, ADP or ATP 1"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   NP_BIND         225..226
FT                   /note="AMP 3"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   NP_BIND         241..244
FT                   /note="AMP, ADP or ATP 2"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   NP_BIND         297..298
FT                   /note="AMP, ADP or ATP 2"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   NP_BIND         313..316
FT                   /note="AMP 3"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   MOTIF           137..158
FT                   /note="AMPK pseudosubstrate"
FT   BINDING         69
FT                   /note="AMP, ADP or ATP 2"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   BINDING         129
FT                   /note="AMP, ADP or ATP 1; via amide nitrogen and carbonyl
FT                   oxygen"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   BINDING         150
FT                   /note="AMP 3"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   BINDING         169
FT                   /note="AMP, ADP or ATP 2"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   BINDING         199
FT                   /note="AMP 3"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   BINDING         204
FT                   /note="AMP 3; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   BINDING         268
FT                   /note="AMP, ADP or ATP 2"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   BINDING         276
FT                   /note="AMP, ADP or ATP 2; via amide nitrogen and carbonyl
FT                   oxygen"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   BINDING         297
FT                   /note="AMP 3"
FT                   /evidence="ECO:0000269|PubMed:17851531"
FT   MOD_RES         260
FT                   /note="Phosphoserine; by ULK1"
FT                   /evidence="ECO:0000305|PubMed:21460634"
FT   MOD_RES         262
FT                   /note="Phosphothreonine; by ULK1"
FT                   /evidence="ECO:0000305|PubMed:21460634"
FT   MOD_RES         269
FT                   /note="Phosphoserine; by ULK1"
FT                   /evidence="ECO:0000269|PubMed:21460634"
FT   CONFLICT        114
FT                   /note="E -> Q (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201
FT                   /note="A -> P (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           24..26
FT                   /evidence="ECO:0000244|PDB:4EAL"
FT   HELIX           27..34
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           37..40
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          43..51
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           56..66
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          69..75
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   TURN            76..79
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          80..86
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           87..101
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   TURN            102..104
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           108..110
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           113..120
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          121..124
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           137..147
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          152..155
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   TURN            157..159
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          162..166
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           168..178
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          181..183
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           186..189
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           192..195
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          206..209
FT                   /evidence="ECO:0000244|PDB:6E4U"
FT   HELIX           212..222
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          225..230
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          234..241
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           242..244
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           246..250
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          258..260
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           261..264
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           265..267
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          269..271
FT                   /evidence="ECO:0000244|PDB:2YA3"
FT   STRAND          277..279
FT                   /evidence="ECO:0000244|PDB:2V9J"
FT   STRAND          280..283
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   HELIX           284..294
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          297..302
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          306..313
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           314..322
FT                   /evidence="ECO:0000244|PDB:2V8Q"
SQ   SEQUENCE   330 AA;  37386 MW;  36031E526C1F1E97 CRC64;
     MESVAAESAP APENEHSQET PESNSSVYTT FMKSHRCYDL IPTSSKLVVF DTSLQVKKAF
     FALVTNGVRA APLWDSKKQS FVGMLTITDF INILHRYYKS ALVQIYELEE HKIETWREVY
     LQDSFKPLVC ISPNASLFDA VSSLIRNKIH RLPVIDPESG NTLYILTHKR ILKFLKLFIT
     EFPKPEFMSK SLEELQIGTY ANIAMVRTTT PVYVALGIFV QHRVSALPVV DEKGRVVDIY
     SKFDVINLAA EKTYNNLDVS VTKALQHRSH YFEGVLKCYL HETLEAIINR LVEAEVHRLV
     VVDEHDVVKG IVSLSDILQA LVLTGGEKKP
//
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