DPH2_YEAST
ID DPH2_YEAST Reviewed; 534 AA.
AC P32461; D6VX09;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000305};
DE AltName: Full=Diphthamide biosynthesis protein 2;
DE AltName: Full=Diphtheria toxin resistance protein 2;
DE AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 2;
GN Name=DPH2; OrderedLocusNames=YKL191W;
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], FUNCTION, AND PATHWAY.
RC STRAIN=S288c / GRF88;
RX PubMed=8406038; DOI=10.1016/0378-1119(93)90528-b;
RA Mattheakis L.C., Sor F., Collier R.J.;
RT "Diphthamide synthesis in Saccharomyces cerevisiae: structure of the DPH2
RT gene.";
RL Gene 132:149-154(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=8394042; DOI=10.1002/yea.320090612;
RA Cheret G., Mattheakis L.C., Sor F.;
RT "DNA sequence analysis of the YCN2 region of chromosome XI in Saccharomyces
RT cerevisiae.";
RL Yeast 9:661-667(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 258-534.
RX PubMed=8132612; DOI=10.1016/s0021-9258(17)37038-2;
RA Mendoza I., Rubio F., Rodriguez-Navarro A., Pardo J.M.;
RT "The protein phosphatase calcineurin is essential for NaCl tolerance of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 269:8792-8796(1994).
RN [7]
RP INTERACTION WITH KTI11.
RX PubMed=12940988; DOI=10.1046/j.1365-2958.2003.03632.x;
RA Fichtner L., Jablonowski D., Schierhorn A., Kitamoto H.K., Stark M.J.R.,
RA Schaffrath R.;
RT "Elongator's toxin-target (TOT) function is nuclear localization sequence
RT dependent and suppressed by post-translational modification.";
RL Mol. Microbiol. 49:1297-1307(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
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 [10]
RP INTERACTION WITH DPH1.
RX PubMed=15485916; DOI=10.1128/mcb.24.21.9487-9497.2004;
RA Liu S., Milne G.T., Kuremsky J.G., Fink G.R., Leppla S.H.;
RT "Identification of the proteins required for biosynthesis of diphthamide,
RT the target of bacterial ADP-ribosylating toxins on translation elongation
RT factor 2.";
RL Mol. Cell. Biol. 24:9487-9497(2004).
RN [11]
RP IDENTIFICATION IN THE 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE SYNTHASE
RP COMPLEX, INTERACTION WITH KTI11, AND DISRUPTION PHENOTYPE.
RX PubMed=18627462; DOI=10.1111/j.1365-2958.2008.06350.x;
RA Baer C., Zabel R., Liu S., Stark M.J., Schaffrath R.;
RT "A versatile partner of eukaryotic protein complexes that is involved in
RT multiple biological processes: Kti11/Dph3.";
RL Mol. Microbiol. 69:1221-1233(2008).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP INTERACTION WITH DPH1.
RX PubMed=23645155; DOI=10.3390/toxins5050958;
RA Abdel-Fattah W., Scheidt V., Uthman S., Stark M.J., Schaffrath R.;
RT "Insights into diphthamide, key diphtheria toxin effector.";
RL Toxins 5:958-968(2013).
RN [16]
RP FUNCTION, COFACTOR, AND IDENTIFICATION IN THE
RP 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE SYNTHASE COMPLEX.
RX PubMed=24422557; DOI=10.1021/ja4118957;
RA Dong M., Su X., Dzikovski B., Dando E.E., Zhu X., Du J., Freed J.H.,
RA Lin H.;
RT "Dph3 is an electron donor for Dph1-Dph2 in the first step of eukaryotic
RT diphthamide biosynthesis.";
RL J. Am. Chem. Soc. 136:1754-1757(2014).
RN [17]
RP FUNCTION, INTERACTION WITH KTI11, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=27694803; DOI=10.1038/nchembio.2190;
RA Lin Z., Dong M., Zhang Y., Lee E.A., Lin H.;
RT "Cbr1 is a Dph3 reductase required for the tRNA wobble uridine
RT modification.";
RL Nat. Chem. Biol. 12:995-997(2016).
RN [18]
RP FUNCTION, COFACTOR, IDENTIFICATION IN THE
RP 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE SYNTHASE COMPLEX, INTERACTION WITH
RP DPH1, AND MUTAGENESIS OF CYS-33; CYS-106; CYS-107; CYS-128; CYS-167;
RP CYS-304; CYS-358 AND CYS-362.
RX PubMed=31463593; DOI=10.1007/s00775-019-01702-0;
RA Dong M., Dando E.E., Kotliar I., Su X., Dzikovski B., Freed J.H., Lin H.;
RT "The asymmetric function of Dph1-Dph2 heterodimer in diphthamide
RT biosynthesis.";
RL J. Biol. Inorg. Chem. 24:777-782(2019).
RN [19]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-239 AND
RP 329-LYS--LYS-534.
RX PubMed=32576952; DOI=10.1038/s41431-020-0668-y;
RA Hawer H., Mendelsohn B.A., Mayer K., Kung A., Malhotra A., Tuupanen S.,
RA Schleit J., Brinkmann U., Schaffrath R.;
RT "Diphthamide-deficiency syndrome: a novel human developmental disorder and
RT ribosomopathy.";
RL Eur. J. Hum. Genet. 28:1497-1508(2020).
RN [20]
RP FUNCTION.
RX PubMed=34154323; DOI=10.1021/jacs.1c03956;
RA Zhang Y., Su D., Dzikovski B., Majer S.H., Coleman R., Chandrasekaran S.,
RA Fenwick M.K., Crane B.R., Lancaster K.M., Freed J.H., Lin H.;
RT "Dph3 Enables Aerobic Diphthamide Biosynthesis by Donating One Iron Atom to
RT Transform a [3Fe-4S] to a [4Fe-4S] Cluster in Dph1-Dph2.";
RL J. Am. Chem. Soc. 143:9314-9319(2021).
CC -!- FUNCTION: Required for the first step of diphthamide biosynthesis, a
CC post-translational modification of histidine which occurs in elongation
CC factor 2 (PubMed:8406038, PubMed:24422557, PubMed:27694803,
CC PubMed:31463593, PubMed:32576952, PubMed:34154323). DPH1 and DPH2
CC transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-
CC methionine (SAM) to a histidine residue, the reaction is assisted by a
CC reduction system comprising KTI11/DPH3 and a NADH-dependent reductase,
CC predominantly CBR1 (PubMed:8406038, PubMed:24422557, PubMed:27694803,
CC PubMed:31463593, PubMed:34154323). Facilitates the reduction of the
CC catalytic iron-sulfur cluster found in the DPH1 subunit
CC (PubMed:31463593). {ECO:0000269|PubMed:24422557,
CC ECO:0000269|PubMed:27694803, ECO:0000269|PubMed:31463593,
CC ECO:0000269|PubMed:32576952, ECO:0000269|PubMed:34154323,
CC ECO:0000269|PubMed:8406038}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:31463593, ECO:0000305|PubMed:24422557};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the
CC reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
CC {ECO:0000269|PubMed:31463593};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000305|PubMed:8406038}.
CC -!- SUBUNIT: Component of the 2-(3-amino-3-carboxypropyl)histidine synthase
CC complex composed of DPH1, DPH2, KTI11/DPH3 and a NADH-dependent
CC reductase, predominantly CBR1 (PubMed:31463593, PubMed:24422557,
CC PubMed:18627462). Interacts with DPH1; the interaction is direct
CC (PubMed:15485916, PubMed:23645155, PubMed:31463593). Interacts with
CC KTI11/DPH3 (PubMed:12940988, PubMed:27694803, PubMed:18627462).
CC {ECO:0000269|PubMed:12940988, ECO:0000269|PubMed:15485916,
CC ECO:0000269|PubMed:18627462, ECO:0000269|PubMed:23645155,
CC ECO:0000269|PubMed:24422557, ECO:0000269|PubMed:27694803,
CC ECO:0000269|PubMed:31463593}.
CC -!- INTERACTION:
CC P32461; P40487: DPH1; NbExp=3; IntAct=EBI-6090, EBI-25162;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Abolishes diphthamide modification of elongation
CC factor 2 (PubMed:32576952). Abolishes the interaction between DPH1 and
CC DPH3 (PubMed:18627462). Resistance to diphtheria toxin, sordarin, and
CC zymocin (PubMed:18627462, PubMed:27694803, PubMed:32576952). Sensitive
CC to hygromycin B (PubMed:32576952). {ECO:0000269|PubMed:18627462,
CC ECO:0000269|PubMed:27694803, ECO:0000269|PubMed:32576952}.
CC -!- MISCELLANEOUS: Present with 3486 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC {ECO:0000305}.
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DR EMBL; L01424; AAA64990.1; -; Genomic_DNA.
DR EMBL; X69765; CAA49420.1; -; Genomic_DNA.
DR EMBL; X74151; CAA52247.1; -; Genomic_DNA.
DR EMBL; Z28191; CAA82035.1; -; Genomic_DNA.
DR EMBL; Z26521; CAA81289.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08975.1; -; Genomic_DNA.
DR PIR; B59228; S34679.
DR RefSeq; NP_012730.1; NM_001179757.1.
DR AlphaFoldDB; P32461; -.
DR SMR; P32461; -.
DR BioGRID; 33930; 123.
DR DIP; DIP-5654N; -.
DR IntAct; P32461; 2.
DR MINT; P32461; -.
DR STRING; 4932.YKL191W; -.
DR iPTMnet; P32461; -.
DR MaxQB; P32461; -.
DR PaxDb; P32461; -.
DR PRIDE; P32461; -.
DR EnsemblFungi; YKL191W_mRNA; YKL191W; YKL191W.
DR GeneID; 853643; -.
DR KEGG; sce:YKL191W; -.
DR SGD; S000001674; DPH2.
DR VEuPathDB; FungiDB:YKL191W; -.
DR eggNOG; KOG2648; Eukaryota.
DR GeneTree; ENSGT00940000153694; -.
DR HOGENOM; CLU_015210_1_0_1; -.
DR InParanoid; P32461; -.
DR OMA; PFNNMYD; -.
DR BioCyc; MetaCyc:MON-15579; -.
DR BioCyc; YEAST:MON-15579; -.
DR BRENDA; 2.5.1.108; 984.
DR Reactome; R-SCE-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR PRO; PR:P32461; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32461; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IDA:UniProtKB.
DR Gene3D; 3.40.50.11840; -; 1.
DR Gene3D; 3.40.50.11860; -; 1.
DR InterPro; IPR010014; DHP2.
DR InterPro; IPR016435; DPH1/DPH2.
DR InterPro; IPR042263; DPH1/DPH2_1.
DR InterPro; IPR042265; DPH1/DPH2_3.
DR PANTHER; PTHR10762; PTHR10762; 1.
DR PANTHER; PTHR10762:SF2; PTHR10762:SF2; 1.
DR Pfam; PF01866; Diphthamide_syn; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR TIGRFAMs; TIGR00322; diphth2_R; 1.
DR TIGRFAMs; TIGR00272; DPH2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..534
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 2"
FT /id="PRO_0000083394"
FT BINDING 107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305|PubMed:31463593"
FT BINDING 128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305|PubMed:31463593"
FT BINDING 362
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305|PubMed:31463593"
FT MUTAGEN 33
FT /note="C->A: Normal sensitivity to diphtheria toxin."
FT /evidence="ECO:0000269|PubMed:31463593"
FT MUTAGEN 106
FT /note="C->A: Normal sensitivity to diphtheria toxin."
FT /evidence="ECO:0000269|PubMed:31463593"
FT MUTAGEN 107
FT /note="C->A: Resistance to diphtheria toxin."
FT /evidence="ECO:0000269|PubMed:31463593"
FT MUTAGEN 107
FT /note="C->S: Normal sensitivity to diphtheria toxin.
FT Abolishes [4Fe-4S] cluster binding and leads to abnormal
FT reduction of the DPH1 [4Fe-4S] cluster; when associated
FT with S-362."
FT /evidence="ECO:0000269|PubMed:31463593"
FT MUTAGEN 128
FT /note="C->A: Resistance to diphtheria toxin."
FT /evidence="ECO:0000269|PubMed:31463593"
FT MUTAGEN 128
FT /note="C->S: Normal sensitivity to diphtheria toxin."
FT /evidence="ECO:0000269|PubMed:31463593"
FT MUTAGEN 167
FT /note="C->A: Normal sensitivity to diphtheria toxin."
FT /evidence="ECO:0000269|PubMed:31463593"
FT MUTAGEN 239
FT /note="K->C: Abolishes diphthamide modification of
FT elongation factor 2. Resistance to diphtheria toxin and
FT sordarin. Sensitive to hygromycin B."
FT /evidence="ECO:0000269|PubMed:32576952"
FT MUTAGEN 304
FT /note="C->A: Normal sensitivity to diphtheria toxin."
FT /evidence="ECO:0000269|PubMed:31463593"
FT MUTAGEN 329..534
FT /note="Missing: Abolishes diphthamide modification of
FT elongation factor 2. Resistance to diphtheria toxin and
FT sordarin. Sensitive to hygromycin B."
FT /evidence="ECO:0000269|PubMed:32576952"
FT MUTAGEN 358
FT /note="C->A: Normal sensitivity to diphtheria toxin."
FT /evidence="ECO:0000269|PubMed:31463593"
FT MUTAGEN 362
FT /note="C->A: Resistance to diphtheria toxin."
FT /evidence="ECO:0000269|PubMed:31463593"
FT MUTAGEN 362
FT /note="C->S: Resistance to diphtheria toxin. Abolishes
FT [4Fe-4S] cluster binding and leads to abnormal reduction of
FT the DPH1 [4Fe-4S] cluster; when associated with S-107."
FT /evidence="ECO:0000269|PubMed:31463593"
SQ SEQUENCE 534 AA; 59775 MW; 9F2728DAE0A27431 CRC64;
MEVAPALSTT QSDVAFQKVE THEIDRSSYL GPCYNSDELM QLISAYYNVE PLVGYLEQHP
EYQNVTLQFP DDLIKDSSLI VRLLQSKFPH GKIKFWVLAD TAYSACCVDE VAAEHVHAEV
VVHFGDACLN AIQNLPVVYS FGTPFLDLAL VVENFQRAFP DLSSKICLMA NAPFSKHLSQ
LYNILKGDLH YTNIIYSQVN TSAVEEKFVT ILDTFHVPED VDQVGVFEKN SVLFGQHDKA
DNISPEDYHL FHLTTPQDPR LLYLSTVFQS VHIFDPALPG MVTGPFPSLM RRYKYMHVAR
TAGCIGILVN TLSLRNTRET INELVKLIKT REKKHYLFVV GKPNVAKLAN FEDIDIWCIL
GCSQSGIIVD QFNEFYKPII TPYELNLALS EEVTWTGKWV VDFRDAIDEI EQNLGGQDTI
SASTTSDEPE FDVVRGRYTS TSRPLRALTH LELEAADDDD SKQLTTRHTA SGAVIKGTVS
TSASALQNRS WKGLGSDFDS TEVDNTGADI EEGISGVARG YGFDREDAMK KENK
