ARNT2_HUMAN
ID ARNT2_HUMAN Reviewed; 717 AA.
AC Q9HBZ2; B4DIS7; O15024; Q8IYC2;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Aryl hydrocarbon receptor nuclear translocator 2;
DE Short=ARNT protein 2;
DE AltName: Full=Class E basic helix-loop-helix protein 1;
DE Short=bHLHe1;
GN Name=ARNT2; Synonyms=BHLHE1, KIAA0307;
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 [GENOMIC DNA].
RX PubMed=12210012; DOI=10.1002/tera.10062;
RA Barrow L.L., Wines M.E., Romitti P.A., Holdener B.C., Murray J.C.;
RT "Aryl hydrocarbon receptor nuclear translocator 2 (ARNT2): structure, gene
RT mapping, polymorphisms, and candidate evaluation for human orofacial
RT clefts.";
RL Teratology 66:85-90(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-679.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hippocampus;
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 MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-694 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
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 [8]
RP FUNCTION, AND INVOLVEMENT IN WEDAS.
RX PubMed=24022475; DOI=10.1093/brain/awt218;
RA Webb E.A., AlMutair A., Kelberman D., Bacchelli C., Chanudet E., Lescai F.,
RA Andoniadou C.L., Banyan A., Alsawaid A., Alrifai M.T., Alahmesh M.A.,
RA Balwi M., Mousavy-Gharavy S.N., Lukovic B., Burke D., McCabe M.J.,
RA Kasia T., Kleta R., Stupka E., Beales P.L., Thompson D.A., Chong W.K.,
RA Alkuraya F.S., Martinez-Barbera J.P., Sowden J.C., Dattani M.T.;
RT "ARNT2 mutation causes hypopituitarism, post-natal microcephaly, visual and
RT renal anomalies.";
RL Brain 136:3096-3105(2013).
RN [9]
RP VARIANTS TRP-46; HIS-107; GLN-402 AND ARG-410, CHARACTERIZATION OF VARIANTS
RP TRP-46; HIS-107; GLN-402 AND ARG-410, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=24465693; DOI=10.1371/journal.pone.0085768;
RA Bersten D.C., Bruning J.B., Peet D.J., Whitelaw M.L.;
RT "Human variants in the neuronal basic helix-loop-helix/Per-Arnt-Sim
RT (bHLH/PAS) transcription factor complex NPAS4/ARNT2 disrupt function.";
RL PLoS ONE 9:E85768-E85768(2014).
CC -!- FUNCTION: Transcription factor that plays a role in the development of
CC the hypothalamo-pituitary axis, postnatal brain growth, and visual and
CC renal function (PubMed:24022475). Specifically recognizes the
CC xenobiotic response element (XRE). {ECO:0000269|PubMed:24022475}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein (By similarity). Heterodimer with NPAS4 (PubMed:24465693).
CC Heterodimer with SIM1 (By similarity). Heterodimer with the aryl
CC hydrocarbon receptor (AHR) or the SIM1 protein (By similarity).
CC Interacts with TACC3 (By similarity). {ECO:0000250|UniProtKB:Q61324,
CC ECO:0000269|PubMed:24465693}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:24465693}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HBZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HBZ2-2; Sequence=VSP_022687;
CC -!- DISEASE: Webb-Dattani syndrome (WEDAS) [MIM:615926]: A disorder
CC characterized by postnatal microcephaly with fronto-temporal lobe
CC hypoplasia, multiple pituitary hormone deficiency, global developmental
CC delay, seizures, severe visual impairment and abnormalities of the
CC kidneys and urinary tract. {ECO:0000269|PubMed:24022475}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36099.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAA20766.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF185610; AAG15310.1; -; Genomic_DNA.
DR EMBL; AF185593; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185594; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185595; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185596; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185597; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185598; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185599; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185600; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185601; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185602; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185603; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185604; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185605; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185606; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185607; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185608; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AF185609; AAG15310.1; JOINED; Genomic_DNA.
DR EMBL; AB002305; BAA20766.2; ALT_INIT; mRNA.
DR EMBL; AK295763; BAG58589.1; -; mRNA.
DR EMBL; BX647212; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471136; EAW99114.1; -; Genomic_DNA.
DR EMBL; BC036099; AAH36099.1; ALT_SEQ; mRNA.
DR CCDS; CCDS32307.1; -. [Q9HBZ2-1]
DR RefSeq; NP_055677.3; NM_014862.3. [Q9HBZ2-1]
DR AlphaFoldDB; Q9HBZ2; -.
DR SMR; Q9HBZ2; -.
DR BioGRID; 115244; 80.
DR IntAct; Q9HBZ2; 14.
DR STRING; 9606.ENSP00000307479; -.
DR GlyGen; Q9HBZ2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HBZ2; -.
DR PhosphoSitePlus; Q9HBZ2; -.
DR BioMuta; ARNT2; -.
DR DMDM; 125987793; -.
DR jPOST; Q9HBZ2; -.
DR MassIVE; Q9HBZ2; -.
DR MaxQB; Q9HBZ2; -.
DR PaxDb; Q9HBZ2; -.
DR PeptideAtlas; Q9HBZ2; -.
DR PRIDE; Q9HBZ2; -.
DR ProteomicsDB; 81615; -. [Q9HBZ2-1]
DR ProteomicsDB; 81616; -. [Q9HBZ2-2]
DR Antibodypedia; 3911; 297 antibodies from 32 providers.
DR DNASU; 9915; -.
DR Ensembl; ENST00000303329.9; ENSP00000307479.4; ENSG00000172379.22. [Q9HBZ2-1]
DR Ensembl; ENST00000527771.5; ENSP00000453792.1; ENSG00000172379.22. [Q9HBZ2-2]
DR Ensembl; ENST00000533983.5; ENSP00000453651.1; ENSG00000172379.22. [Q9HBZ2-2]
DR GeneID; 9915; -.
DR KEGG; hsa:9915; -.
DR MANE-Select; ENST00000303329.9; ENSP00000307479.4; NM_014862.4; NP_055677.3.
DR UCSC; uc010unm.3; human. [Q9HBZ2-1]
DR CTD; 9915; -.
DR DisGeNET; 9915; -.
DR GeneCards; ARNT2; -.
DR HGNC; HGNC:16876; ARNT2.
DR HPA; ENSG00000172379; Group enriched (brain, choroid plexus).
DR MalaCards; ARNT2; -.
DR MIM; 606036; gene.
DR MIM; 615926; phenotype.
DR neXtProt; NX_Q9HBZ2; -.
DR OpenTargets; ENSG00000172379; -.
DR Orphanet; 3157; Septo-optic dysplasia spectrum.
DR PharmGKB; PA24995; -.
DR VEuPathDB; HostDB:ENSG00000172379; -.
DR eggNOG; KOG3561; Eukaryota.
DR GeneTree; ENSGT00940000158198; -.
DR InParanoid; Q9HBZ2; -.
DR OMA; MRPFSAN; -.
DR PhylomeDB; Q9HBZ2; -.
DR TreeFam; TF319983; -.
DR PathwayCommons; Q9HBZ2; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR Reactome; R-HSA-211976; Endogenous sterols.
DR Reactome; R-HSA-211981; Xenobiotics.
DR Reactome; R-HSA-8937144; Aryl hydrocarbon receptor signalling.
DR SignaLink; Q9HBZ2; -.
DR BioGRID-ORCS; 9915; 16 hits in 1095 CRISPR screens.
DR ChiTaRS; ARNT2; human.
DR GeneWiki; ARNT2; -.
DR GenomeRNAi; 9915; -.
DR Pharos; Q9HBZ2; Tbio.
DR PRO; PR:Q9HBZ2; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9HBZ2; protein.
DR Bgee; ENSG00000172379; Expressed in lateral globus pallidus and 167 other tissues.
DR ExpressionAtlas; Q9HBZ2; baseline and differential.
DR Genevisible; Q9HBZ2; HS.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001067; Nuc_translocat.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00785; NCTRNSLOCATR.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Methylation; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..717
FT /note="Aryl hydrocarbon receptor nuclear translocator 2"
FT /id="PRO_0000127122"
FT DOMAIN 63..116
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 134..209
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 323..393
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 398..441
FT /note="PAC"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61324"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9205841"
FT /id="VSP_022687"
FT VARIANT 46
FT /note="R -> W (decreased transcription factor activity due
FT to impaired localization to the nucleus;
FT dbSNP:rs140468271)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076841"
FT VARIANT 107
FT /note="R -> H (decreased transcription factor activity;
FT dbSNP:rs371290912)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076842"
FT VARIANT 402
FT /note="R -> Q (does not affect the transcription factor
FT activity; dbSNP:rs141193900)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076843"
FT VARIANT 410
FT /note="W -> R (does not affect the transcription factor
FT activity; dbSNP:rs150964641)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076844"
FT VARIANT 679
FT /note="G -> S (in dbSNP:rs4072568)"
FT /evidence="ECO:0000269|PubMed:9205841"
FT /id="VAR_049538"
FT CONFLICT 28
FT /note="A -> V (in Ref. 4; BX647212)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="R -> K (in Ref. 2; BAA20766)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="S -> P (in Ref. 4; BX647212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 78691 MW; AC7524E97F617252 CRC64;
MATPAAVNPP EMASDIPGSV TLPVAPMAAT GQVRMAGAMP ARGGKRRSGM DFDDEDGEGP
SKFSRENHSE IERRRRNKMT QYITELSDMV PTCSALARKP DKLTILRMAV SHMKSMRGTG
NKSTDGAYKP SFLTEQELKH LILEAADGFL FVVAAETGRV IYVSDSVTPV LNQPQSEWFG
STLYEQVHPD DVEKLREQLC TSENSMTGRI LDLKTGTVKK EGQQSSMRMC MGSRRSFICR
MRCGNAPLDH LPLNRITTMR KRFRNGLGPV KEGEAQYAVV HCTGYIKAWP PAGMTIPEED
ADVGQGSKYC LVAIGRLQVT SSPVCMDMNG MSVPTEFLSR HNSDGIITFV DPRCISVIGY
QPQDLLGKDI LEFCHPEDQS HLRESFQQVV KLKGQVLSVM YRFRTKNREW MLIRTSSFTF
QNPYSDEIEY IICTNTNVKQ LQQQQAELEV HQRDGLSSYD LSQVPVPNLP AGVHEAGKSV
EKADAIFSQE RDPRFAEMFA GISASEKKMM SSASAAGTQQ IYSQGSPFPS GHSGKAFSSS
VVHVPGVNDI QSSSSTGQNM SQISRQLNQS QVAWTGSRPP FPGQQIPSQS SKTQSSPFGI
GTSHTYPADP SSYSPLSSPA TSSPSGNAYS SLANRTPGFA ESGQSSGQFQ GRPSEVWSQW
QSQHHGQQSG EQHSHQQPGQ TEVFQDMLPM PGDPTQGTGN YNIEDFADLG MFPPFSE
