ATD2B_HUMAN
ID ATD2B_HUMAN Reviewed; 1458 AA.
AC Q9ULI0; B9ZVQ5; Q6ZNA6; Q8N9E7;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=ATPase family AAA domain-containing protein 2B;
GN Name=ATAD2B; Synonyms=KIAA1240;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1076 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 721-1458 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-79; SER-86; SER-1338
RP AND SER-1347, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-79; SER-81; SER-86;
RP SER-140; THR-221; SER-318 AND SER-1347, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=24561620; DOI=10.1038/ncb2918;
RA Alabert C., Bukowski-Wills J.C., Lee S.B., Kustatscher G., Nakamura K.,
RA de Lima Alves F., Menard P., Mejlvang J., Rappsilber J., Groth A.;
RT "Nascent chromatin capture proteomics determines chromatin dynamics during
RT DNA replication and identifies unknown fork components.";
RL Nat. Cell Biol. 16:281-293(2014).
RN [10]
RP STRUCTURE BY NMR OF 958-1080.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the bromodomain of human protein KIAA1240.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 952-1086, AND SUBUNIT.
RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA Gingras A.C., Arrowsmith C.H., Knapp S.;
RT "Histone recognition and large-scale structural analysis of the human
RT bromodomain family.";
RL Cell 149:214-231(2012).
CC -!- SUBUNIT: Binds acetylated lysine residues in histone H1.4, H2A, H2B, H3
CC and H4 (in vitro). {ECO:0000269|PubMed:22464331}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24561620}.
CC Note=Partially localizes to replication sites.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULI0-2; Sequence=VSP_023276;
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD18469.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC009242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC066692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK094821; BAC04429.1; -; mRNA.
DR EMBL; AK131301; BAD18469.1; ALT_INIT; mRNA.
DR EMBL; AB033066; BAA86554.1; -; mRNA.
DR CCDS; CCDS46227.1; -. [Q9ULI0-1]
DR RefSeq; NP_001229267.2; NM_001242338.2.
DR RefSeq; NP_060022.2; NM_017552.3.
DR PDB; 2DKW; NMR; -; A=958-1080.
DR PDB; 3LXJ; X-ray; 2.33 A; A/B/C/D=952-1086.
DR PDB; 6VEO; X-ray; 2.40 A; A=953-1085.
DR PDBsum; 2DKW; -.
DR PDBsum; 3LXJ; -.
DR PDBsum; 6VEO; -.
DR AlphaFoldDB; Q9ULI0; -.
DR SMR; Q9ULI0; -.
DR BioGRID; 119961; 3.
DR IntAct; Q9ULI0; 2.
DR MINT; Q9ULI0; -.
DR STRING; 9606.ENSP00000238789; -.
DR BindingDB; Q9ULI0; -.
DR ChEMBL; CHEMBL2176775; -.
DR GuidetoPHARMACOLOGY; 2720; -.
DR iPTMnet; Q9ULI0; -.
DR PhosphoSitePlus; Q9ULI0; -.
DR BioMuta; ATAD2B; -.
DR DMDM; 296439432; -.
DR EPD; Q9ULI0; -.
DR jPOST; Q9ULI0; -.
DR MassIVE; Q9ULI0; -.
DR MaxQB; Q9ULI0; -.
DR PaxDb; Q9ULI0; -.
DR PeptideAtlas; Q9ULI0; -.
DR PRIDE; Q9ULI0; -.
DR ProteomicsDB; 85032; -. [Q9ULI0-1]
DR ProteomicsDB; 85033; -. [Q9ULI0-2]
DR ABCD; Q9ULI0; 1 sequenced antibody.
DR Antibodypedia; 27378; 26 antibodies from 12 providers.
DR DNASU; 54454; -.
DR Ensembl; ENST00000238789.10; ENSP00000238789.5; ENSG00000119778.15.
DR GeneID; 54454; -.
DR KEGG; hsa:54454; -.
DR UCSC; uc002rek.5; human. [Q9ULI0-1]
DR CTD; 54454; -.
DR DisGeNET; 54454; -.
DR GeneCards; ATAD2B; -.
DR HGNC; HGNC:29230; ATAD2B.
DR HPA; ENSG00000119778; Low tissue specificity.
DR MIM; 615347; gene.
DR neXtProt; NX_Q9ULI0; -.
DR PharmGKB; PA162377039; -.
DR VEuPathDB; HostDB:ENSG00000119778; -.
DR eggNOG; KOG0730; Eukaryota.
DR eggNOG; KOG0732; Eukaryota.
DR HOGENOM; CLU_001448_3_2_1; -.
DR InParanoid; Q9ULI0; -.
DR OrthoDB; 443983at2759; -.
DR PhylomeDB; Q9ULI0; -.
DR TreeFam; TF314783; -.
DR PathwayCommons; Q9ULI0; -.
DR SignaLink; Q9ULI0; -.
DR BioGRID-ORCS; 54454; 6 hits in 1080 CRISPR screens.
DR ChiTaRS; ATAD2B; human.
DR EvolutionaryTrace; Q9ULI0; -.
DR GenomeRNAi; 54454; -.
DR Pharos; Q9ULI0; Tchem.
DR PRO; PR:Q9ULI0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9ULI0; protein.
DR Bgee; ENSG00000119778; Expressed in buccal mucosa cell and 182 other tissues.
DR ExpressionAtlas; Q9ULI0; baseline and differential.
DR Genevisible; Q9ULI0; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR045199; ATAD2-like.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23069; PTHR23069; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Bromodomain; Coiled coil;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1458
FT /note="ATPase family AAA domain-containing protein 2B"
FT /id="PRO_0000050789"
FT DOMAIN 975..1045
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 943..974
FT /evidence="ECO:0000255"
FT COMPBIAS 34..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..278
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 441..448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 988..992
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574462"
FT /id="VSP_023276"
FT VARIANT 118
FT /note="S -> P (in dbSNP:rs10210982)"
FT /id="VAR_055467"
FT CONFLICT 207
FT /note="Q -> R (in Ref. 2; BAC04429)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="T -> A (in Ref. 2; BAC04429)"
FT /evidence="ECO:0000305"
FT HELIX 952..975
FT /evidence="ECO:0007829|PDB:3LXJ"
FT HELIX 978..980
FT /evidence="ECO:0007829|PDB:3LXJ"
FT TURN 989..991
FT /evidence="ECO:0007829|PDB:3LXJ"
FT HELIX 995..998
FT /evidence="ECO:0007829|PDB:3LXJ"
FT HELIX 1005..1013
FT /evidence="ECO:0007829|PDB:3LXJ"
FT HELIX 1020..1037
FT /evidence="ECO:0007829|PDB:3LXJ"
FT STRAND 1040..1042
FT /evidence="ECO:0007829|PDB:3LXJ"
FT HELIX 1043..1066
FT /evidence="ECO:0007829|PDB:3LXJ"
FT HELIX 1069..1083
FT /evidence="ECO:0007829|PDB:3LXJ"
SQ SEQUENCE 1458 AA; 164914 MW; CE7480D7EEBE6F9C CRC64;
MVNTRKSSLR LLGSKSPGPG PGPGAGAEPG ATGGSSHFIS SRTRSSKTRA ASCPAAKAGG
SGGAGVTLDE ARKVEVDGSL SDSHVSPPAK RTLKQPDSVC KDKSKSRSTG QREEWNLSTG
QARLTSQPGA TLPNGHSGLS LRSHPLRGEK KGDGDLSCIN GDMEVRKSCR SRKNRFESVN
QSLLFDQLVN STAEAVLQEM DNINIRQNRR SGEVERLRMW TDTEFENMDM YSRVKRRRKS
LRRNSYGIQN HHEVSTEGEE EESQEEDGDI EVEEAEGEEN DRPYNLRQRK TVDRYQAPPI
VPAHQKKREN TLFDIHRSPA RRSHIRRKKH AIHSSDTTSS DEERFERRKS KSMARARNRC
LPMNFRAEDL ASGILRERVK VGASLADVDP MNIDKSVRFD SIGGLSHHIH ALKEMVVFPL
LYPEIFEKFK IQPPRGCLFY GPPGTGKTLV ARALANECSQ GDKKVAFFMR KGADCLSKWV
GESERQLRLL FDQAYLMRPS IIFFDEIDGL APVRSSRQDQ IHSSIVSTLL ALMDGLDNRG
EIVVIGATNR LDSIDPALRR PGRFDREFLF NLPDQKARKH ILQIHTRDWN PKLSDAFLGE
LAEKCVGYCG ADIKALCTEA ALIALRRRYP QIYASSHKLQ LDVSSIVLSA QDFYHAMQNI
VPASQRAVMS SGHALSPIIR PLLERSFNNI LAVLQKVFPH AEISQSDKKE DIETLILEDS
EDENALSIFE TNCHSGSPKK QSSSAAIHKP YLHFTMSPYH QPTSYRPRLL LSGERGSGQT
SHLAPALLHT LERFSVHRLD LPALYSVSAK TPEESCAQIF REARRTVPSI VYMPHIGDWW
EAVSETVRAT FLTLLQDIPS FSPIFLLSTS ETMYSELPEE VKCIFRIQYE EVLYIQRPIE
EDRRKFFQEL ILNQASMAPP RRKHAALCAM EVLPLALPSP PRQLSESEKS RMEDQEENTL
RELRLFLRDV TKRLATDKRF NIFSKPVDIE EVSDYLEVIK EPMDLSTVIT KIDKHNYLTA
KDFLKDIDLI CSNALEYNPD KDPGDKIIRH RACTLKDTAH AIIAAELDPE FNKLCEEIKE
ARIKRGLSVT SEQINPHSTG ARKTETRVEE AFRHKQRNPM DVWHNSANKC AFRVRRKSRR
RSQWGKGIIK KRKVNNLKKD EEDTKFADYE NHTEDRKLLE NGEFEVSTDC HEENGEETGD
LSMTNDESSC DIMDLDQGQR LNNGAGTKEN FASTEEESSN ESLLVNSSSS LNPEQTSRKE
TFLKGNCLNG EASTDSFEGI PVLECQNGKL EVVSFCDSGD KCSSEQKILL EDQSKEKPET
STENHGDDLE KLEALECSNN EKLEPGSDVE VKDAELDKEG ASKVKKYRKL ILEQAKTTSL
ELVPEEPSEP VPPLIVDRER LKKLLDLLVD KSNNLAVDQL ERLYSLLSQC IYRHRKDYDK
SQLVEEMERT VHMFETFL
