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H2A2_YEAST
ID   H2A2_YEAST              Reviewed;         132 AA.
AC   P04912; D6VPZ9;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 199.
DE   RecName: Full=Histone H2A.2;
GN   Name=HTA2; Synonyms=H2A2; OrderedLocusNames=YBL003C; ORFNames=YBL0103;
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=7041122; DOI=10.1073/pnas.79.5.1484;
RA   Choe J., Kolodrubetz D., Grunstein M.;
RT   "The two yeast histone H2A genes encode similar protein subtypes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:1484-1487(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091860; DOI=10.1002/yea.320100006;
RA   Wolfe K.H., Lohan A.J.E.;
RT   "Sequence around the centromere of Saccharomyces cerevisiae chromosome II:
RT   similarity of CEN2 to CEN4.";
RL   Yeast 10:S41-S46(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   ACETYLATION AT LYS-5 AND LYS-8.
RX   PubMed=10082517; DOI=10.1128/mcb.19.4.2515;
RA   Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.;
RT   "Esa1p is an essential histone acetyltransferase required for cell cycle
RT   progression.";
RL   Mol. Cell. Biol. 19:2515-2526(1999).
RN   [7]
RP   FUNCTION, MUTAGENESIS OF SER-129, AND PHOSPHORYLATION AT SER-129.
RX   PubMed=11140636; DOI=10.1038/35050000;
RA   Downs J.A., Lowndes N.F., Jackson S.P.;
RT   "A role for Saccharomyces cerevisiae histone H2A in DNA repair.";
RL   Nature 408:1001-1004(2000).
RN   [8]
RP   ACETYLATION AT LYS-8.
RX   PubMed=11545749; DOI=10.1016/s1097-2765(01)00301-x;
RA   Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.;
RT   "Highly specific antibodies determine histone acetylation site usage in
RT   yeast heterochromatin and euchromatin.";
RL   Mol. Cell 8:473-479(2001).
RN   [9]
RP   ACETYLATION AT SER-2.
RX   PubMed=12915400; DOI=10.1074/jbc.c300355200;
RA   Song O.-K., Wang X., Waterborg J.H., Sternglanz R.;
RT   "An Nalpha-acetyltransferase responsible for acetylation of the N-terminal
RT   residues of histones H4 and H2A.";
RL   J. Biol. Chem. 278:38109-38112(2003).
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, AND PHOSPHORYLATION.
RX   PubMed=15458641; DOI=10.1016/j.cub.2004.09.047;
RA   Shroff R., Arbel-Eden A., Pilch D.R., Ira G., Bonner W.M., Petrini J.H.J.,
RA   Haber J.E., Lichten M.;
RT   "Distribution and dynamics of chromatin modification induced by a defined
RT   DNA double-strand break.";
RL   Curr. Biol. 14:1703-1711(2004).
RN   [12]
RP   FUNCTION, AND PHOSPHORYLATION.
RX   PubMed=15610741; DOI=10.1016/j.molcel.2004.11.027;
RA   Uenal E., Arbel-Eden A., Sattler U., Shroff R., Lichten M., Haber J.E.,
RA   Koshland D.;
RT   "DNA damage response pathway uses histone modification to assemble a
RT   double-strand break-specific cohesin domain.";
RL   Mol. Cell 16:991-1002(2004).
RN   [13]
RP   INTERACTION WITH ARP4.
RX   PubMed=15610740; DOI=10.1016/j.molcel.2004.12.003;
RA   Downs J.A., Allard S., Jobin-Robitaille O., Javaheri A., Auger A.,
RA   Bouchard N., Kron S.J., Jackson S.P., Cote J.;
RT   "Binding of chromatin-modifying activities to phosphorylated histone H2A at
RT   DNA damage sites.";
RL   Mol. Cell 16:979-990(2004).
RN   [14]
RP   SUMOYLATION AT LYS-127.
RX   PubMed=16598039; DOI=10.1101/gad.1404206;
RA   Nathan D., Ingvarsdottir K., Sterner D.E., Bylebyl G.R., Dokmanovic M.,
RA   Dorsey J.A., Whelan K.A., Krsmanovic M., Lane W.S., Meluh P.B.,
RA   Johnson E.S., Berger S.L.;
RT   "Histone sumoylation is a negative regulator in Saccharomyces cerevisiae
RT   and shows dynamic interplay with positive-acting histone modifications.";
RL   Genes Dev. 20:966-976(2006).
RN   [15]
RP   FUNCTION, AND DEPHOSPHORYLATION.
RX   PubMed=16299494; DOI=10.1038/nature04384;
RA   Keogh M.-C., Kim J.-A., Downey M., Fillingham J., Chowdhury D.,
RA   Harrison J.C., Onishi M., Datta N., Galicia S., Emili A., Lieberman J.,
RA   Shen X., Buratowski S., Haber J.E., Durocher D., Greenblatt J.F.,
RA   Krogan N.J.;
RT   "A phosphatase complex that dephosphorylates gamma-H2AX regulates DNA
RT   damage checkpoint recovery.";
RL   Nature 439:497-501(2006).
RN   [16]
RP   INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA   Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA   Pemberton L.F.;
RT   "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT   function.";
RL   Mol. Cell. Biol. 28:1313-1325(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP   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   [18]
RP   SUCCINYLATION AT LYS-14 AND LYS-22, AND MALONYLATION AT LYS-120.
RX   PubMed=22389435; DOI=10.1074/mcp.m111.015875;
RA   Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
RT   "Lysine succinylation and lysine malonylation in histones.";
RL   Mol. Cell. Proteomics 11:100-107(2012).
RN   [19]
RP   METHYLATION AT GLN-106.
RX   PubMed=24352239; DOI=10.1038/nature12819;
RA   Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J.,
RA   Nielsen M.L., Kouzarides T.;
RT   "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated
RT   modification.";
RL   Nature 505:564-568(2014).
CC   -!- FUNCTION: Core component of nucleosome which plays a central role in
CC       DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA
CC       into chromatin, limiting DNA accessibility to the cellular machineries
CC       which require DNA as a template. Histones thereby play a central role
CC       in transcription regulation, DNA repair, DNA replication and
CC       chromosomal stability. DNA accessibility is regulated via a complex set
CC       of post-translational modifications of histones, also called histone
CC       code, and nucleosome remodeling. {ECO:0000269|PubMed:11140636,
CC       ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15610741,
CC       ECO:0000269|PubMed:16299494}.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC       each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC       two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC       DNA. Interacts with NAP1. {ECO:0000269|PubMed:15610740,
CC       ECO:0000269|PubMed:18086883}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC       from the PI3/PI4-kinase family.
CC   -!- PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA
CC       double-strand breaks (DSBs) generated by exogenous genotoxic agents and
CC       by stalled replication forks. Phosphorylation is dependent on the DNA
CC       damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side
CC       of a detected DSB site and may mark the surrounding chromatin for
CC       recruitment of proteins required for DNA damage signaling and repair.
CC       Gamma-H2A interacts with ARP4, a shared component of the NuA4 histone
CC       acetyltransferase complex and the INO80 and SWR1 chromatin remodeling
CC       complexes, and serves to recruit first NuA4, mediating histone H4
CC       acetylation, and subsequently the INO80/SWR1 complexes, facilitating
CC       DNA resection, to DSB sites. Gamma-H2A is required for sequestering
CC       cohesin around the break site, which is important for efficient post-
CC       replicative double-strand break repair by homologous recombination,
CC       holding the damaged chromatid close to its undamaged sister template.
CC       Gamma-H2A is removed from the DNA prior to the strand invasion-primer
CC       extension step of the repair process and subsequently dephosphorylated
CC       by PPH3, a component of the histone H2A phosphatase complex (HTP-C).
CC       Dephosphorylation is necessary for efficient recovery from the DNA
CC       damage checkpoint. {ECO:0000269|PubMed:11140636,
CC       ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15610741}.
CC   -!- PTM: N-acetylated by NAT4.
CC   -!- PTM: Acetylated by ESA1, a component of the NuA4 histone
CC       acetyltransferase (HAT) complex, to form H2AK4ac and H2AK7ac.
CC   -!- PTM: Glutamine methylation at Gln-106 (H2AQ105me) by NOP1 is
CC       specifically dedicated to polymerase I. It is present at 35S ribosomal
CC       DNA locus and impairs binding of the FACT complex (PubMed:24352239).
CC       {ECO:0000269|PubMed:24352239}.
CC   -!- PTM: Sumoylated to from H2AK126su. May lead to transcriptional
CC       repression. {ECO:0000269|PubMed:16598039}.
CC   -!- MISCELLANEOUS: In contrast to vertebrates and insects, its C-terminus
CC       is not monoubiquitinated. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 32100 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC   -!- CAUTION: To ensure consistency between histone entries, we follow the
CC       'Brno' nomenclature for histone modifications, with positions referring
CC       to those used in the literature for the 'closest' model organism. Due
CC       to slight variations in histone sequences between organisms and to the
CC       presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC       actual positions of modified amino acids in the sequence generally
CC       differ. In this entry the following conventions are used: H2AK4ac =
CC       acetylated Lys-5; H2AK7ac = acetylated Lys-8; H2AK126su = sumoylated
CC       Lys-127; H2AS128ph = phosphorylated Ser-129. {ECO:0000305}.
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DR   EMBL; V01305; CAA24612.1; -; Genomic_DNA.
DR   EMBL; Z26494; CAA81267.1; -; Genomic_DNA.
DR   EMBL; Z35764; CAA84818.1; -; Genomic_DNA.
DR   EMBL; AY693115; AAT93134.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07119.1; -; Genomic_DNA.
DR   PIR; S05814; HSBYA2.
DR   RefSeq; NP_009552.1; NM_001178243.1.
DR   PDB; 4JJN; X-ray; 3.09 A; C/G=2-132.
DR   PDB; 4KUD; X-ray; 3.20 A; C/G=1-132.
DR   PDBsum; 4JJN; -.
DR   PDBsum; 4KUD; -.
DR   AlphaFoldDB; P04912; -.
DR   SMR; P04912; -.
DR   BioGRID; 32699; 320.
DR   ComplexPortal; CPX-1610; Nucleosome, variant HTA2-HTB2.
DR   ComplexPortal; CPX-1611; Nucleosome, variant HTA2-HTB1.
DR   DIP; DIP-6377N; -.
DR   IntAct; P04912; 162.
DR   MINT; P04912; -.
DR   STRING; 4932.YBL003C; -.
DR   iPTMnet; P04912; -.
DR   MaxQB; P04912; -.
DR   PaxDb; P04912; -.
DR   PRIDE; P04912; -.
DR   TopDownProteomics; P04912; -.
DR   EnsemblFungi; YBL003C_mRNA; YBL003C; YBL003C.
DR   GeneID; 852283; -.
DR   KEGG; sce:YBL003C; -.
DR   SGD; S000000099; HTA2.
DR   VEuPathDB; FungiDB:YBL003C; -.
DR   eggNOG; KOG1756; Eukaryota.
DR   GeneTree; ENSGT00940000153118; -.
DR   HOGENOM; CLU_062828_3_0_1; -.
DR   InParanoid; P04912; -.
DR   OMA; VMPYIHP; -.
DR   BioCyc; YEAST:G3O-28909-MON; -.
DR   Reactome; R-SCE-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR   Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR   Reactome; R-SCE-427359; SIRT1 negatively regulates rRNA expression.
DR   Reactome; R-SCE-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR   Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR   Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-SCE-68616; Assembly of the ORC complex at the origin of replication.
DR   Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR   PRO; PR:P04912; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P04912; protein.
DR   GO; GO:0000786; C:nucleosome; TAS:SGD.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; TAS:SGD.
DR   GO; GO:0006281; P:DNA repair; IMP:SGD.
DR   CDD; cd00074; H2A; 1.
DR   Gene3D; 1.10.20.10; -; 1.
DR   IDEAL; IID50137; -.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR032454; Histone_H2A_C.
DR   InterPro; IPR032458; Histone_H2A_CS.
DR   PANTHER; PTHR23430; PTHR23430; 1.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF16211; Histone_H2A_C; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00046; HISTONE_H2A; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chromosome; DNA damage; DNA repair; DNA-binding;
KW   Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12915400"
FT   CHAIN           2..132
FT                   /note="Histone H2A.2"
FT                   /id="PRO_0000055327"
FT   MOTIF           129..130
FT                   /note="[ST]-Q motif"
FT   SITE            120
FT                   /note="Not ubiquitinated"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:12915400"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:10082517"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:10082517,
FT                   ECO:0000269|PubMed:11545749"
FT   MOD_RES         14
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:22389435"
FT   MOD_RES         22
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:22389435"
FT   MOD_RES         106
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000269|PubMed:24352239"
FT   MOD_RES         120
FT                   /note="N6-malonyllysine"
FT                   /evidence="ECO:0000269|PubMed:22389435"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:11140636,
FT                   ECO:0007744|PubMed:18407956"
FT   CROSSLNK        127
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT   MUTAGEN         129
FT                   /note="S->A: Causes hypersensitivity to DNA-damage-inducing
FT                   agents."
FT                   /evidence="ECO:0000269|PubMed:11140636"
FT   MUTAGEN         129
FT                   /note="S->E,T: No effect."
FT                   /evidence="ECO:0000269|PubMed:11140636"
FT   HELIX           19..22
FT                   /evidence="ECO:0007829|PDB:4JJN"
FT   HELIX           29..37
FT                   /evidence="ECO:0007829|PDB:4JJN"
FT   TURN            38..40
FT                   /evidence="ECO:0007829|PDB:4JJN"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:4JJN"
FT   HELIX           49..74
FT                   /evidence="ECO:0007829|PDB:4JJN"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:4JJN"
FT   HELIX           82..89
FT                   /evidence="ECO:0007829|PDB:4JJN"
FT   HELIX           93..98
FT                   /evidence="ECO:0007829|PDB:4JJN"
FT   TURN            99..101
FT                   /evidence="ECO:0007829|PDB:4JJN"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:4JJN"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:4JJN"
SQ   SEQUENCE   132 AA;  13989 MW;  E808C94A0363CD53 CRC64;
     MSGGKGGKAG SAAKASQSRS AKAGLTFPVG RVHRLLRRGN YAQRIGSGAP VYLTAVLEYL
     AAEILELAGN AARDNKKTRI IPRHLQLAIR NDDELNKLLG NVTIAQGGVL PNIHQNLLPK
     KSAKTAKASQ EL
 
 
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