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Database: UniProt
Entry: P32481
LinkDB: P32481
Original site: P32481 
ID   IF2G_YEAST              Reviewed;         527 AA.
AC   P32481; D3DLS4;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   07-APR-2021, entry version 192.
DE   RecName: Full=Eukaryotic translation initiation factor 2 subunit gamma;
DE            Short=eIF-2-gamma;
DE            EC=3.6.5.3 {ECO:0000269|PubMed:3888990};
GN   Name=GCD11; Synonyms=SUI4, TIF213; OrderedLocusNames=YER025W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8417348; DOI=10.1128/mcb.13.1.506;
RA   Hannig E.M., Cigan A.M., Freeman B.A., Kinzy T.G.;
RT   "GCD11, a negative regulator of GCN4 expression, encodes the gamma subunit
RT   of eIF-2 in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 13:506-520(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=3888989;
RA   Ahmad M.F., Nasrin N., Banerjee A.C., Gupta N.K.;
RT   "Purification and properties of eukaryotic initiation factor 2 and its
RT   ancillary protein factor (Co-eIF-2A) from yeast Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 260:6955-6959(1985).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=3888990;
RA   Ahmad M.F., Nasrin N., Bagchi M.K., Chakravarty I., Gupta N.K.;
RT   "A comparative study of the characteristics of eIF-2 and eIF-2-ancillary
RT   factor activities from yeast Saccharomyces cerevisiae and rabbit
RT   reticulocytes.";
RL   J. Biol. Chem. 260:6960-6965(1985).
RN   [6]
RP   FUNCTION.
RX   PubMed=9308967; DOI=10.1101/gad.11.18.2396;
RA   Huang H.K., Yoon H., Hannig E.M., Donahue T.F.;
RT   "GTP hydrolysis controls stringent selection of the AUG start codon during
RT   translation initiation in Saccharomyces cerevisiae.";
RL   Genes Dev. 11:2396-2413(1997).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF TYR-142 AND LYS-250.
RX   PubMed=8947054; DOI=10.1002/j.1460-2075.1996.tb01021.x;
RA   Erickson F.L., Hannig E.M.;
RT   "Ligand interactions with eukaryotic translation initiation factor 2: role
RT   of the gamma-subunit.";
RL   EMBO J. 15:6311-6320(1996).
RN   [8]
RP   SUBUNIT.
RX   PubMed=11018020; DOI=10.1101/gad.831800;
RA   Asano K., Clayton J., Shalev A., Hinnebusch A.G.;
RT   "A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3,
RT   eIF5, and initiator tRNA(Met) is an important translation initiation
RT   intermediate in vivo.";
RL   Genes Dev. 14:2534-2546(2000).
RN   [9]
RP   FUNCTION.
RX   PubMed=11042214; DOI=10.1074/jbc.m007398200;
RA   Nika J., Rippel S., Hannig E.M.;
RT   "Biochemical analysis of the eIF2beta gamma complex reveals a structural
RT   function for eIF2alpha in catalyzed nucleotide exchange.";
RL   J. Biol. Chem. 276:1051-1056(2001).
RN   [10]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [11]
RP   FUNCTION.
RX   PubMed=14698289; DOI=10.1016/j.jmb.2003.11.025;
RA   Kapp L.D., Lorsch J.R.;
RT   "GTP-dependent recognition of the methionine moiety on initiator tRNA by
RT   translation factor eIF2.";
RL   J. Mol. Biol. 335:923-936(2004).
RN   [12]
RP   FUNCTION.
RX   PubMed=16246727; DOI=10.1016/j.molcel.2005.09.008;
RA   Algire M.A., Maag D., Lorsch J.R.;
RT   "Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-
RT   site selection during eukaryotic translation initiation.";
RL   Mol. Cell 20:251-262(2005).
RN   [13]
RP   SUBUNIT.
RX   PubMed=16522633; DOI=10.1074/jbc.m511700200;
RA   Alone P.V., Dever T.E.;
RT   "Direct binding of translation initiation factor eIF2gamma-G domain to its
RT   GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B epsilon.";
RL   J. Biol. Chem. 281:12636-12644(2006).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60 AND SER-258, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [16]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS).
RX   PubMed=25417110; DOI=10.1016/j.cell.2014.10.001;
RA   Hussain T., Llacer J.L., Fernandez I.S., Munoz A., Martin-Marcos P.,
RA   Savva C.G., Lorsch J.R., Hinnebusch A.G., Ramakrishnan V.;
RT   "Structural changes enable start codon recognition by the eukaryotic
RT   translation initiation complex.";
RL   Cell 159:597-607(2014).
RN   [17]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.05 ANGSTROMS) IN COMPLEX WITH GTP.
RX   PubMed=30475211; DOI=10.7554/elife.39273;
RA   Llacer J.L., Hussain T., Saini A.K., Nanda J.S., Kaur S., Gordiyenko Y.,
RA   Kumar R., Hinnebusch A.G., Lorsch J.R., Ramakrishnan V.;
RT   "Translational initiation factor eIF5 replaces eIF1 on the 40S ribosomal
RT   subunit to promote start-codon recognition.";
RL   Elife 7:0-0(2018).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 410-527.
RX   PubMed=26211610; DOI=10.1016/j.str.2015.06.014;
RA   Panvert M., Dubiez E., Arnold L., Perez J., Mechulam Y., Seufert W.,
RA   Schmitt E.;
RT   "Cdc123, a cell cycle regulator needed for eIF2 assembly, is an ATP-grasp
RT   protein with unique features.";
RL   Structure 23:1596-1608(2015).
RN   [19]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS).
RX   PubMed=26212456; DOI=10.1016/j.molcel.2015.06.033;
RA   Llacer J.L., Hussain T., Marler L., Aitken C.E., Thakur A., Lorsch J.R.,
RA   Hinnebusch A.G., Ramakrishnan V.;
RT   "Conformational differences between open and closed states of the
RT   eukaryotic translation initiation complex.";
RL   Mol. Cell 59:399-412(2015).
RN   [20]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.93 ANGSTROMS).
RX   PubMed=31086188; DOI=10.1038/s41467-019-10167-3;
RA   Adomavicius T., Guaita M., Zhou Y., Jennings M.D., Latif Z., Roseman A.M.,
RA   Pavitt G.D.;
RT   "The structural basis of translational control by eIF2 phosphorylation.";
RL   Nat. Commun. 10:2136-2136(2019).
RN   [21]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS).
RX   PubMed=31201334; DOI=10.1038/s41467-019-10606-1;
RA   Gordiyenko Y., Llacer J.L., Ramakrishnan V.;
RT   "Structural basis for the inhibition of translation through eIF2alpha
RT   phosphorylation.";
RL   Nat. Commun. 10:2640-2640(2019).
CC   -!- FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF-2),
CC       involved in the early steps of protein synthesis. In the presence of
CC       GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and
CC       then recruits the 40S ribosomal complex and initiation factors eIF-1,
CC       eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a
CC       step that determines the rate of protein translation. The 43S PIC binds
CC       to mRNA and scans downstream to the initiation codon, where it forms a
CC       48S initiation complex by codon-anticodon base pairing. This leads to
CC       the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-
CC       5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release
CC       of Pi, which makes GTP hydrolysis irreversible, causes the release of
CC       the eIF-2-GDP binary complex from the 40S subunit, an event that is
CC       essential for the subsequent joining of the 60S ribosomal subunit to
CC       form an elongation-competent 80S ribosome. In order for eIF-2 to
CC       recycle and catalyze another round of initiation, the GDP bound to eIF-
CC       2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP
CC       exchange factor (GEF) eIF-2B. {ECO:0000269|PubMed:11042214,
CC       ECO:0000269|PubMed:14698289, ECO:0000269|PubMed:16246727,
CC       ECO:0000269|PubMed:3888989, ECO:0000269|PubMed:3888990,
CC       ECO:0000269|PubMed:8947054, ECO:0000269|PubMed:9308967}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC         Evidence={ECO:0000269|PubMed:3888990};
CC   -!- SUBUNIT: Eukaryotic translation initiation factor 2 (eIF-2) is a
CC       heterotrimeric G-protein composed of an alpha, a beta and a gamma
CC       subunit. The factors eIF-1, eIF-1A, eIF-2, eIF-3, TIF5/eIF-5 and
CC       methionyl-tRNAi form a multifactor complex (MFC) that may bind to the
CC       40S ribosome. {ECO:0000269|PubMed:11018020,
CC       ECO:0000269|PubMed:16522633}.
CC   -!- INTERACTION:
CC       P32481; Q05791: CDC123; NbExp=9; IntAct=EBI-8924, EBI-34676;
CC       P32481; P20459: SUI2; NbExp=11; IntAct=EBI-8924, EBI-8915;
CC       P32481; P09064: SUI3; NbExp=5; IntAct=EBI-8924, EBI-8920;
CC       P32481; P38431: TIF5; NbExp=3; IntAct=EBI-8924, EBI-9038;
CC       P32481; Q9P7N5: cdc123; Xeno; NbExp=4; IntAct=EBI-8924, EBI-16165908;
CC   -!- MISCELLANEOUS: Present with 20800 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; L04268; AAA34633.1; -; Genomic_DNA.
DR   EMBL; U18778; AAB64558.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07678.1; -; Genomic_DNA.
DR   PIR; A48117; A48117.
DR   RefSeq; NP_010942.1; NM_001178916.1.
DR   PDB; 3J81; EM; 4.00 A; k=1-527.
DR   PDB; 3JAP; EM; 4.90 A; k=1-527.
DR   PDB; 3JAQ; EM; 6.00 A; k=1-527.
DR   PDB; 4ZGN; X-ray; 2.90 A; B=410-527.
DR   PDB; 4ZGQ; X-ray; 3.00 A; B=410-527.
DR   PDB; 6FYX; EM; 3.05 A; k=1-527.
DR   PDB; 6FYY; EM; 3.05 A; k=1-527.
DR   PDB; 6GSM; EM; 5.15 A; k=90-519.
DR   PDB; 6GSN; EM; 5.75 A; k=90-519.
DR   PDB; 6I3M; EM; 3.93 A; O/P=1-527.
DR   PDB; 6I7T; EM; 4.61 A; O/P=1-527.
DR   PDB; 6QG0; EM; 4.20 A; M/N=1-527.
DR   PDB; 6QG1; EM; 4.20 A; M/N=1-527.
DR   PDB; 6QG2; EM; 4.60 A; M/N=1-527.
DR   PDB; 6QG3; EM; 9.40 A; M/N=1-527.
DR   PDB; 6QG5; EM; 10.10 A; M/N=1-527.
DR   PDB; 6QG6; EM; 4.65 A; M/N=1-527.
DR   PDBsum; 3J81; -.
DR   PDBsum; 3JAP; -.
DR   PDBsum; 3JAQ; -.
DR   PDBsum; 4ZGN; -.
DR   PDBsum; 4ZGQ; -.
DR   PDBsum; 6FYX; -.
DR   PDBsum; 6FYY; -.
DR   PDBsum; 6GSM; -.
DR   PDBsum; 6GSN; -.
DR   PDBsum; 6I3M; -.
DR   PDBsum; 6I7T; -.
DR   PDBsum; 6QG0; -.
DR   PDBsum; 6QG1; -.
DR   PDBsum; 6QG2; -.
DR   PDBsum; 6QG3; -.
DR   PDBsum; 6QG5; -.
DR   PDBsum; 6QG6; -.
DR   SMR; P32481; -.
DR   BioGRID; 36759; 438.
DR   ComplexPortal; CPX-427; Eukaryotic translation initiation factor 2 complex.
DR   DIP; DIP-2561N; -.
DR   IntAct; P32481; 79.
DR   MINT; P32481; -.
DR   STRING; 4932.YER025W; -.
DR   iPTMnet; P32481; -.
DR   MaxQB; P32481; -.
DR   PaxDb; P32481; -.
DR   PRIDE; P32481; -.
DR   EnsemblFungi; YER025W_mRNA; YER025W; YER025W.
DR   GeneID; 856746; -.
DR   KEGG; sce:YER025W; -.
DR   SGD; S000000827; GCD11.
DR   VEuPathDB; FungiDB:YER025W; -.
DR   eggNOG; KOG0466; Eukaryota.
DR   GeneTree; ENSGT00940000172475; -.
DR   HOGENOM; CLU_027154_0_1_1; -.
DR   InParanoid; P32481; -.
DR   OMA; NIGMVGH; -.
DR   Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SCE-381042; PERK regulates gene expression.
DR   Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-SCE-72731; Recycling of eIF2:GDP.
DR   PRO; PR:P32481; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P32481; protein.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:SGD.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IDA:SGD.
DR   GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IMP:SGD.
DR   GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IMP:SGD.
DR   GO; GO:0031369; F:translation initiation factor binding; IDA:SGD.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IDA:SGD.
DR   GO; GO:0045903; P:positive regulation of translational fidelity; IMP:SGD.
DR   GO; GO:0006413; P:translational initiation; IMP:SGD.
DR   CDD; cd01888; eIF2_gamma; 1.
DR   CDD; cd03688; eIF2_gamma_II; 1.
DR   CDD; cd15490; eIF2_gamma_III; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR015256; eIF2g_C.
DR   InterPro; IPR044127; eIF2g_dom_2.
DR   InterPro; IPR044128; eIF2g_GTP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   Pfam; PF09173; eIF2_C; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; GTP-binding; Hydrolase; Initiation factor;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..527
FT                   /note="Eukaryotic translation initiation factor 2 subunit
FT                   gamma"
FT                   /id="PRO_0000137448"
FT   DOMAIN          98..307
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   NP_BIND         110..115
FT                   /note="GTP"
FT                   /evidence="ECO:0000269|PubMed:30475211"
FT   NP_BIND         249..252
FT                   /note="GTP"
FT                   /evidence="ECO:0000269|PubMed:30475211"
FT   NP_BIND         284..286
FT                   /note="GTP"
FT                   /evidence="ECO:0000269|PubMed:30475211"
FT   REGION          107..114
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          135..139
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          193..196
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          249..252
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          284..286
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   COMPBIAS        155..179
FT                   /note="Cys-rich"
FT   MOD_RES         60
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:18407956"
FT   MUTAGEN         135
FT                   /note="N->K: In SUI4; defective in ternary complex
FT                   formation, correlating with a higher rate of dissociation
FT                   from charged initiator-tRNA in the absence of GTP
FT                   hydrolysis."
FT                   /evidence="ECO:0000269|PubMed:9308967"
FT   MUTAGEN         142
FT                   /note="Y->H: Reduces the affinity of eIF-2 for Met-
FT                   tRNAi(Met) without affecting the k(off) value for guanine
FT                   nucleotides."
FT                   /evidence="ECO:0000269|PubMed:8947054"
FT   MUTAGEN         250
FT                   /note="K->R: Increases the off-rate for GDP, without
FT                   altering the apparent dissociation constant for Met-
FT                   tRNAi(Met). Mimicks the function of the guanine nucleotide
FT                   exchange factor eIF-2B."
FT                   /evidence="ECO:0000269|PubMed:8947054"
FT   STRAND          425..436
FT                   /evidence="ECO:0007744|PDB:4ZGN"
FT   STRAND          460..466
FT                   /evidence="ECO:0007744|PDB:4ZGN"
FT   STRAND          469..478
FT                   /evidence="ECO:0007744|PDB:4ZGN"
FT   STRAND          480..493
FT                   /evidence="ECO:0007744|PDB:4ZGN"
FT   STRAND          498..504
FT                   /evidence="ECO:0007744|PDB:4ZGN"
FT   STRAND          506..523
FT                   /evidence="ECO:0007744|PDB:4ZGN"
SQ   SEQUENCE   527 AA;  57866 MW;  D498AE62BC3E81CD CRC64;
     MSDLQDQEPS IIINGNLEPV GEPDIVEETE VVAQETQETQ DADKPKKKVA FTGLEEDGET
     EEEKRKREFE EGGGLPEQPL NPDFSKLNPL SAEIINRQAT INIGTIGHVA HGKSTVVRAI
     SGVQTVRFKD ELERNITIKL GYANAKIYKC QEPTCPEPDC YRSFKSDKEI SPKCQRPGCP
     GRYKLVRHVS FVDCPGHDIL MSTMLSGAAV MDAALLLIAG NESCPQPQTS EHLAAIEIMK
     LKHVIILQNK VDLMREESAL EHQKSILKFI RGTIADGAPI VPISAQLKYN IDAVNEFIVK
     TIPVPPRDFM ISPRLIVIRS FDVNKPGAEI EDLKGGVAGG SILNGVFKLG DEIEIRPGIV
     TKDDKGKIQC KPIFSNIVSL FAEQNDLKFA VPGGLIGVGT KVDPTLCRAD RLVGQVVGAK
     GHLPNIYTDI EINYFLLRRL LGVKTDGQKQ AKVRKLEPNE VLMVNIGSTA TGARVVAVKA
     DMARLQLTSP ACTEINEKIA LSRRIEKHWR LIGWATIKKG TTLEPIA
//
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