ADA2_YEAST
ID ADA2_YEAST Reviewed; 434 AA.
AC Q02336; D6VT73;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Transcriptional adapter 2;
GN Name=ADA2; OrderedLocusNames=YDR448W; ORFNames=D9461.33;
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=1638630; DOI=10.1016/0092-8674(92)90100-q;
RA Berger S.L., Pina B., Silverman N., Marcus G.A., Agapite J., Regier J.L.,
RA Triezenberg S.J., Guarente L.;
RT "Genetic isolation of ADA2: a potential transcriptional adaptor required
RT for function of certain acidic activation domains.";
RL Cell 70:251-265(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 INTERACTION WITH GCN5.
RX PubMed=7957049; DOI=10.1002/j.1460-2075.1994.tb06806.x;
RA Marcus G.A., Silverman N., Berger S.L., Horiuchi J., Guarente L.;
RT "Functional similarity and physical association between GCN5 and ADA2:
RT putative transcriptional adaptors.";
RL EMBO J. 13:4807-4815(1994).
RN [5]
RP IDENTIFICATION IN THE ADA/GCN5 COMPLEX.
RC STRAIN=ATCC MYA-3516 / BWG1-7A;
RX PubMed=9154821; DOI=10.1128/mcb.17.6.3220;
RA Horiuchi J., Silverman N., Pina B., Marcus G.A., Guarente L.;
RT "ADA1, a novel component of the ADA/GCN5 complex, has broader effects than
RT GCN5, ADA2, or ADA3.";
RL Mol. Cell. Biol. 17:3220-3228(1997).
RN [6]
RP IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9674426; DOI=10.1016/s0092-8674(00)81220-9;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C.,
RA Yates J.R. III, Workman J.L.;
RT "A subset of TAF(II)s are integral components of the SAGA complex required
RT for nucleosome acetylation and transcriptional stimulation.";
RL Cell 94:45-53(1998).
RN [7]
RP IDENTIFICATION IN A SAGA COMPLEX WITH SPT7; HFI1; SPT8; GCN5; SPT20; SPT2;
RP ADA3 AND TRA1.
RX PubMed=9885573; DOI=10.1016/s1097-2765(00)80300-7;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L.;
RT "The ATM-related cofactor Tra1 is a component of the purified SAGA
RT complex.";
RL Mol. Cell 2:863-867(1998).
RN [8]
RP FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX, AND FUNCTION IN
RP HISTONE ACETYLATION AT THE ADA COMPLEX.
RX PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL J. Biol. Chem. 274:5895-5900(1999).
RN [9]
RP IDENTIFICATION IN THE ADA COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10490601; DOI=10.1128/mcb.19.10.6621;
RA Eberharter A., Sterner D.E., Schieltz D., Hassan A., Yates J.R. III,
RA Berger S.L., Workman J.L.;
RT "The ADA complex is a distinct histone acetyltransferase complex in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 19:6621-6631(1999).
RN [10]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT "The novel SLIK histone acetyltransferase complex functions in the yeast
RT retrograde response pathway.";
RL Mol. Cell. Biol. 22:8774-8786(2002).
RN [11]
RP IDENTIFICATION IN THE SALSA COMPLEX.
RX PubMed=12186975; DOI=10.1073/pnas.182021199;
RA Sterner D.E., Belotserkovskaya R., Berger S.L.;
RT "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates
RT with activated transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002).
RN [12]
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 [13]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=15647753; DOI=10.1038/nature03242;
RA Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT dependent acetylation.";
RL Nature 433:434-438(2005).
RN [14]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
RN [15]
RP STRUCTURE BY NMR OF 348-434.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SWIRM domain of baker's yeast transcriptional
RT adapter 2.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is
CC involved in RNA polymerase II-dependent transcriptional regulation of
CC approximately 10% of yeast genes. At the promoters, SAGA is required
CC for recruitment of the basal transcription machinery. It influences RNA
CC polymerase II transcriptional activity through different activities
CC such as TBP interaction (SPT3, SPT8 and SPT20) and promoter
CC selectivity, interaction with transcription activators (GCN5, ADA2,
CC ADA3 and TRA1), and chromatin modification through histone acetylation
CC (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone
CC H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA
CC interacts with DNA via upstream activating sequences (UASs). SALSA, an
CC altered form of SAGA, may be involved in positive transcriptional
CC regulation. SLIK is proposed to have partly overlapping functions with
CC SAGA. It preferentially acetylates methylated histone H3, at least
CC after activation at the GAL1-10 locus. ADA preferentially acetylates
CC nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B.
CC {ECO:0000269|PubMed:10026213}.
CC -!- SUBUNIT: Component of the 1.8 MDa SAGA complex, which consists of at
CC least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12,
CC TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and
CC SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2
CC copies. SAGA is built of 5 distinct domains with specialized functions.
CC Domain I (containing TRA1) probably represents the activator
CC interaction surface. Domain II (containing TAF5 and TAF6, and probably
CC TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and
CC ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing
CC HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily
CC an architectural role. Domain III also harbors the HAT activity. Domain
CC V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-
CC interacting module, which may be associated transiently with SAGA.
CC Component of the SALSA complex, which consists of at least TRA1, SPT7
CC (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1,
CC GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of
CC at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1,
CC UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Component of the
CC ADA/GCN5 complex that consists of HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and
CC GCN5 and is probably a subcomplex of SAGA. Component of the 0.8 MDa ADA
CC complex, which at least consists of ADA2, ADA3, AHC1 and GCN5. ADA2
CC interacts with GCN5. {ECO:0000269|PubMed:10490601,
CC ECO:0000269|PubMed:12186975, ECO:0000269|PubMed:12446794,
CC ECO:0000269|PubMed:15647753, ECO:0000269|PubMed:7957049,
CC ECO:0000269|PubMed:9154821, ECO:0000269|PubMed:9674426,
CC ECO:0000269|PubMed:9885573}.
CC -!- INTERACTION:
CC Q02336; Q03330: GCN5; NbExp=41; IntAct=EBI-2186, EBI-7458;
CC Q02336; Q12060: HFI1; NbExp=25; IntAct=EBI-2186, EBI-8287;
CC Q02336; P32494: NGG1; NbExp=28; IntAct=EBI-2186, EBI-2192;
CC Q02336; Q00772: SLT2; NbExp=2; IntAct=EBI-2186, EBI-17372;
CC Q02336; P38811: TRA1; NbExp=26; IntAct=EBI-2186, EBI-24638;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 1720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M95396; AAA34393.1; -; Genomic_DNA.
DR EMBL; U33007; AAB64871.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12283.1; -; Genomic_DNA.
DR PIR; A43252; A43252.
DR RefSeq; NP_010736.3; NM_001180756.3.
DR PDB; 2ELJ; NMR; -; A=354-434.
DR PDB; 6CW2; X-ray; 2.67 A; C=1-120.
DR PDB; 6CW3; X-ray; 1.98 A; E/G=2-120.
DR PDBsum; 2ELJ; -.
DR PDBsum; 6CW2; -.
DR PDBsum; 6CW3; -.
DR AlphaFoldDB; Q02336; -.
DR SMR; Q02336; -.
DR BioGRID; 32503; 307.
DR ComplexPortal; CPX-608; ADA complex.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-183N; -.
DR IntAct; Q02336; 164.
DR MINT; Q02336; -.
DR STRING; 4932.YDR448W; -.
DR iPTMnet; Q02336; -.
DR MaxQB; Q02336; -.
DR PaxDb; Q02336; -.
DR PRIDE; Q02336; -.
DR ABCD; Q02336; 1 sequenced antibody.
DR DNASU; 852059; -.
DR EnsemblFungi; YDR448W_mRNA; YDR448W; YDR448W.
DR GeneID; 852059; -.
DR KEGG; sce:YDR448W; -.
DR SGD; S000002856; ADA2.
DR VEuPathDB; FungiDB:YDR448W; -.
DR eggNOG; KOG0457; Eukaryota.
DR GeneTree; ENSGT00940000157318; -.
DR HOGENOM; CLU_018273_3_0_1; -.
DR InParanoid; Q02336; -.
DR OMA; EFETEYF; -.
DR BioCyc; YEAST:G3O-29979-MON; -.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR EvolutionaryTrace; Q02336; -.
DR PRO; PR:Q02336; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q02336; protein.
DR GO; GO:0140671; C:ADA complex; IDA:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0070461; C:SAGA-type complex; IBA:GO_Central.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0016578; P:histone deubiquitination; IC:ComplexPortal.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IMP:SGD.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02335; ZZ_ADA2; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR041983; ADA2-like_ZZ.
DR InterPro; IPR016827; Ada2/TADA2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..434
FT /note="Transcriptional adapter 2"
FT /id="PRO_0000197082"
FT DOMAIN 60..112
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 349..434
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT ZN_FING 2..58
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 325..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:6CW3"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:6CW3"
FT HELIX 32..36
FT /evidence="ECO:0007829|PDB:6CW3"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:6CW3"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6CW3"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:6CW3"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:6CW3"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:6CW3"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:6CW3"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:6CW3"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:2ELJ"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:2ELJ"
FT HELIX 371..379
FT /evidence="ECO:0007829|PDB:2ELJ"
FT HELIX 384..401
FT /evidence="ECO:0007829|PDB:2ELJ"
FT HELIX 407..413
FT /evidence="ECO:0007829|PDB:2ELJ"
FT HELIX 418..430
FT /evidence="ECO:0007829|PDB:2ELJ"
SQ SEQUENCE 434 AA; 50569 MW; 9637E1EDBBED0AC3 CRC64;
MSNKFHCDVC SADCTNRVRV SCAICPEYDL CVPCFSQGSY TGKHRPYHDY RIIETNSYPI
LCPDWGADEE LQLIKGAQTL GLGNWQDIAD HIGSRGKEEV KEHYLKYYLE SKYYPIPDIT
QNIHVPQDEF LEQRRHRIES FRERPLEPPR KPMASVPSCH EVQGFMPGRL EFETEFENEA
EGPVKDMVFE PDDQPLDIEL KFAILDIYNS RLTTRAEKKR LLFENHLMDY RKLQAIDKKR
SKEAKELYNR IKPFARVMTA QDFEEFSKDI LEELHCRARI QQLQEWRSNG LTTLEAGLKY
ERDKQARISS FEKFGASTAA SLSEGNSRYR SNSAHRSNAE YSQNYSENGG RKKNMTISDI
QHAPDYALLS NDEQQLCIQL KILPKPYLVL KEVMFRELLK TGGNLSKSAC RELLNIDPIK
ANRIYDFFQS QNWM
