ZBT40_HUMAN
ID ZBT40_HUMAN Reviewed; 1239 AA.
AC Q9NUA8; O75066; Q5TFU5; Q8N1R1;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 4.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Zinc finger and BTB domain-containing protein 40;
GN Name=ZBTB40; Synonyms=KIAA0478;
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 MRNA] (ISOFORM 1), AND VARIANTS CYS-595
RP AND MET-997.
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP MASS 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1066, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NUA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NUA8-2; Sequence=VSP_007757, VSP_007758, VSP_007759;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32323.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB007947; BAA32323.2; ALT_INIT; mRNA.
DR EMBL; AK095273; BAC04518.1; -; mRNA.
DR EMBL; AL035703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS224.1; -. [Q9NUA8-1]
DR RefSeq; NP_001077090.1; NM_001083621.1. [Q9NUA8-1]
DR RefSeq; NP_055685.3; NM_014870.3. [Q9NUA8-1]
DR RefSeq; XP_011540801.1; XM_011542499.2. [Q9NUA8-1]
DR AlphaFoldDB; Q9NUA8; -.
DR BioGRID; 115251; 19.
DR IntAct; Q9NUA8; 11.
DR MINT; Q9NUA8; -.
DR STRING; 9606.ENSP00000384527; -.
DR iPTMnet; Q9NUA8; -.
DR PhosphoSitePlus; Q9NUA8; -.
DR BioMuta; ZBTB40; -.
DR DMDM; 68847213; -.
DR EPD; Q9NUA8; -.
DR jPOST; Q9NUA8; -.
DR MassIVE; Q9NUA8; -.
DR MaxQB; Q9NUA8; -.
DR PaxDb; Q9NUA8; -.
DR PeptideAtlas; Q9NUA8; -.
DR PRIDE; Q9NUA8; -.
DR ProteomicsDB; 82658; -. [Q9NUA8-1]
DR ProteomicsDB; 82659; -. [Q9NUA8-2]
DR TopDownProteomics; Q9NUA8-2; -. [Q9NUA8-2]
DR Antibodypedia; 30081; 187 antibodies from 30 providers.
DR DNASU; 9923; -.
DR Ensembl; ENST00000375647.5; ENSP00000364798.4; ENSG00000184677.18. [Q9NUA8-1]
DR Ensembl; ENST00000404138.5; ENSP00000384527.1; ENSG00000184677.18. [Q9NUA8-1]
DR GeneID; 9923; -.
DR KEGG; hsa:9923; -.
DR MANE-Select; ENST00000375647.5; ENSP00000364798.4; NM_014870.4; NP_055685.3.
DR UCSC; uc001bft.2; human. [Q9NUA8-1]
DR CTD; 9923; -.
DR DisGeNET; 9923; -.
DR GeneCards; ZBTB40; -.
DR HGNC; HGNC:29045; ZBTB40.
DR HPA; ENSG00000184677; Low tissue specificity.
DR MIM; 612106; gene.
DR neXtProt; NX_Q9NUA8; -.
DR OpenTargets; ENSG00000184677; -.
DR PharmGKB; PA142670544; -.
DR VEuPathDB; HostDB:ENSG00000184677; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00930000151052; -.
DR InParanoid; Q9NUA8; -.
DR OMA; FHECDKC; -.
DR PhylomeDB; Q9NUA8; -.
DR TreeFam; TF350897; -.
DR PathwayCommons; Q9NUA8; -.
DR SignaLink; Q9NUA8; -.
DR BioGRID-ORCS; 9923; 13 hits in 1134 CRISPR screens.
DR ChiTaRS; ZBTB40; human.
DR GeneWiki; ZBTB40; -.
DR GenomeRNAi; 9923; -.
DR Pharos; Q9NUA8; Tbio.
DR PRO; PR:Q9NUA8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NUA8; protein.
DR Bgee; ENSG00000184677; Expressed in dorsal motor nucleus of vagus nerve and 201 other tissues.
DR ExpressionAtlas; Q9NUA8; baseline and differential.
DR Genevisible; Q9NUA8; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0030282; P:bone mineralization; NAS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR030404; ZBTB40.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24394:SF0; PTHR24394:SF0; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1239
FT /note="Zinc finger and BTB domain-containing protein 40"
FT /id="PRO_0000047745"
FT DOMAIN 24..87
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 807..830
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 836..858
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 864..887
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 893..915
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 921..944
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 950..973
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 978..1000
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1006..1029
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1046..1069
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1075..1098
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1104..1127
FT /note="C2H2-type 11; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1135..1158
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 130..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CROSSLNK 1066
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 116..162
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007757"
FT VAR_SEQ 270..281
FT /note="EIKGPQKEMIVK -> NCCVPVEAVPIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007758"
FT VAR_SEQ 282..1239
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007759"
FT VARIANT 225
FT /note="A -> T (in dbSNP:rs6659222)"
FT /id="VAR_052920"
FT VARIANT 267
FT /note="M -> I (in dbSNP:rs36115661)"
FT /id="VAR_052921"
FT VARIANT 595
FT /note="Y -> C (in dbSNP:rs209729)"
FT /evidence="ECO:0000269|PubMed:9455484"
FT /id="VAR_052922"
FT VARIANT 997
FT /note="V -> M (in dbSNP:rs209720)"
FT /evidence="ECO:0000269|PubMed:9455484"
FT /id="VAR_052923"
FT CONFLICT 218
FT /note="A -> P (in Ref. 1; BAA32323)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1239 AA; 138118 MW; 1B35528EB104052C CRC64;
MELPNYSRQL LQQLYTLCKE QQFCDCTISI GTIYFRAHKL VLAAASLLFK TLLDNTDTIS
IDASVVSPEE FALLLEMMYT GKLPVGKHNF SKIISLADSL QMFDVAVSCK NLLTSLVNCS
VQGQVVRDVS APSSETFRKE PEKPQVEILS SEGAGEPHSS PELAATPGGP VKAETEEAAH
SVSQEMSVNS PTAQESQRNA ETPAETPTTA EACSPSPAVQ TFSEAKKTST EPGCERKHYQ
LNFLLENEGV FSDALMVTQD VLKKLEMCSE IKGPQKEMIV KCFEGEGGHS AFQRILGKVR
EESLDVQTVV SLLRLYQYSN PAVKTALLDR KPEDVDTVQP KGSTEEGKTL SVLLLEHKED
LIQCVTQLRP IMESLETAKE EFLTGTEKRV ILNCCEGRTP KETIENLLHR MTEEKTLTAE
GLVKLLQAVK TTFPNLGLLL EKLQKSATLP STTVQPSPDD YGTELLRRYH ENLSEIFTDN
QILLKMISHM TSLAPGEREV MEKLVKRDSG SGGFNSLISA VLEKQTLSAT AIWQLLLVVQ
ETKTCPLDLL MEEIRREPGA DAFFRAVTTP EHATLETILR HNQLILEAIQ QKIEYKLFTS
EEEHLAETVK EILSIPSETA SPEASLRAVL SRAMEKSVPA IEICHLLCSV HKSFPGLQPV
MQELAYIGVL TKEDGEKETW KVSNKFHLEA NNKEDEKAAK EDSQPGEQND QGETGSLPGQ
QEKEASASPD PAKKSFICKA CDKSFHFYCR LKVHMKRCRV AKSKQVQCKE CSETKDSKKE
LDKHQLEAHG AGGEPDAPKK KKKRLPVTCD LCGREFAHAS GMQYHKLTEH FDEKPFSCEE
CGAKFAANST LKNHLRLHTG DRPFMCKHCL MTFTQASALA YHTKKKHSEG KMYACQYCDA
VFAQSIELSR HVRTHTGDKP YVCRDCGKGF RQANGLSIHL HTFHNIEDPY DCKKCRMSFP
TLQDHRKHIH EVHSKEYHPC PTCGKIFSAP SMLERHVVTH VGGKPFSCGI CNKAYQQLSG
LWYHNRTHHP DVFAAQNHRS SKFSSLQCSS CDKTFPNTIE HKKHIKAEHA DMKFHECDQC
KELFPTPALL QVHVKCQHSG SQPFRCLYCA ATFRFPGALQ HHVTTEHFKQ SETTFPCELC
GELFTSQAQL DSHLESEHPK VMSTETQAAA SQMAQVIQTP EPVAPTEQVI TLEETQLAGS
QVFVTLPDSQ ASQASSELVA VTVEDLLDGT VTLICGEAK
