IF2G_YEAST
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 03-AUG-2022, entry version 197.
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.13.1.506-520.1993;
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; DOI=10.1016/s0021-9258(18)88873-1;
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; DOI=10.1016/s0021-9258(18)88874-3;
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 AlphaFoldDB; P32481; -.
DR SMR; P32481; -.
DR BioGRID; 36759; 458.
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 BioCyc; YEAST:G3O-30207-MON; -.
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:0005840; C:ribosome; IDA:ComplexPortal.
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; IDA:ComplexPortal.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.40.50.300; -; 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 REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 37..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:30475211"
FT BINDING 249..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:30475211"
FT BINDING 284..286
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:30475211"
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:0007829|PDB:4ZGN"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:4ZGN"
FT STRAND 469..478
FT /evidence="ECO:0007829|PDB:4ZGN"
FT STRAND 480..493
FT /evidence="ECO:0007829|PDB:4ZGN"
FT STRAND 498..504
FT /evidence="ECO:0007829|PDB:4ZGN"
FT STRAND 506..523
FT /evidence="ECO:0007829|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
