HELZ_HUMAN
ID HELZ_HUMAN Reviewed; 1942 AA.
AC P42694; I6L9H4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Probable helicase with zinc finger domain;
DE EC=3.6.4.-;
DE AltName: Full=Down-regulated in human cancers protein;
GN Name=HELZ; Synonyms=DRHC, KIAA0054;
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).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph;
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 [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND DISCUSSION OF SEQUENCE.
RX PubMed=10471385; DOI=10.1006/bbrc.1999.1208;
RA Wagner D.S., Gan L., Klein W.H.;
RT "Identification of a differentially expressed RNA helicase by gene
RT trapping.";
RL Biochem. Biophys. Res. Commun. 262:677-684(1999).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12691822; DOI=10.1016/s0304383502006882;
RA Nagai H., Yabe A., Mine N., Mikami I., Fujiwara H., Terada Y., Hirano A.,
RA Tsuneizumi M., Yokota T., Emi M.;
RT "Down-regulation in human cancers of DRHC, a novel helicase-like gene from
RT 17q25.1 that inhibits cell growth.";
RL Cancer Lett. 193:41-47(2003).
RN [6]
RP INTERACTION WITH SMYD3 AND POLR2A.
RX PubMed=15235609; DOI=10.1038/ncb1151;
RA Hamamoto R., Furukawa Y., Morita M., Iimura Y., Silva F.P., Li M.,
RA Yagyu R., Nakamura Y.;
RT "SMYD3 encodes a histone methyltransferase involved in the proliferation of
RT cancer cells.";
RL Nat. Cell Biol. 6:731-740(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 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1738 AND SER-1766, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1614, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; THR-1163; SER-1614;
RP SER-1645; SER-1738 AND SER-1741, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP IDENTIFICATION BY 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 [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1245, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May act as a helicase that plays a role in RNA metabolism in
CC multiple tissues and organs within the developing embryo.
CC -!- SUBUNIT: Interacts with SMYD2 (By similarity). Interacts with POLR2A.
CC Interacts with SMYD3; the interaction may bridge SMYD3 and RNA
CC polymerase II. {ECO:0000250, ECO:0000269|PubMed:15235609}.
CC -!- INTERACTION:
CC P42694; Q8IWL3: HSCB; NbExp=4; IntAct=EBI-1210654, EBI-1805738;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P42694-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42694-2; Sequence=VSP_054493, VSP_054494, VSP_054495;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in thymus and brain.
CC Expression is down-regulated in 28 of 95 tested cancer cell lines.
CC {ECO:0000269|PubMed:12691822}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06147.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D29677; BAA06147.3; ALT_INIT; mRNA.
DR EMBL; AC005544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094881; AAH94881.1; -; mRNA.
DR CCDS; CCDS42374.1; -. [P42694-1]
DR RefSeq; NP_055692.2; NM_014877.3. [P42694-1]
DR AlphaFoldDB; P42694; -.
DR SMR; P42694; -.
DR DIP; DIP-39352N; -.
DR IntAct; P42694; 36.
DR MINT; P42694; -.
DR STRING; 9606.ENSP00000351524; -.
DR iPTMnet; P42694; -.
DR PhosphoSitePlus; P42694; -.
DR BioMuta; HELZ; -.
DR DMDM; 221222452; -.
DR EPD; P42694; -.
DR jPOST; P42694; -.
DR MassIVE; P42694; -.
DR MaxQB; P42694; -.
DR PaxDb; P42694; -.
DR PeptideAtlas; P42694; -.
DR PRIDE; P42694; -.
DR ProteomicsDB; 55539; -. [P42694-1]
DR Antibodypedia; 31693; 89 antibodies from 14 providers.
DR DNASU; 9931; -.
DR Ensembl; ENST00000358691.10; ENSP00000351524.5; ENSG00000198265.12. [P42694-1]
DR Ensembl; ENST00000579953.5; ENSP00000463727.1; ENSG00000198265.12. [P42694-2]
DR GeneID; 9931; -.
DR KEGG; hsa:9931; -.
DR MANE-Select; ENST00000358691.10; ENSP00000351524.5; NM_014877.4; NP_055692.3.
DR UCSC; uc002jfx.5; human. [P42694-1]
DR CTD; 9931; -.
DR DisGeNET; 9931; -.
DR GeneCards; HELZ; -.
DR HGNC; HGNC:16878; HELZ.
DR HPA; ENSG00000198265; Low tissue specificity.
DR MIM; 606699; gene.
DR neXtProt; NX_P42694; -.
DR OpenTargets; ENSG00000198265; -.
DR VEuPathDB; HostDB:ENSG00000198265; -.
DR eggNOG; KOG1804; Eukaryota.
DR GeneTree; ENSGT00940000156686; -.
DR HOGENOM; CLU_001451_0_0_1; -.
DR InParanoid; P42694; -.
DR OMA; REMAPEY; -.
DR OrthoDB; 286011at2759; -.
DR PhylomeDB; P42694; -.
DR TreeFam; TF323999; -.
DR PathwayCommons; P42694; -.
DR SignaLink; P42694; -.
DR BioGRID-ORCS; 9931; 32 hits in 1085 CRISPR screens.
DR ChiTaRS; HELZ; human.
DR GenomeRNAi; 9931; -.
DR Pharos; P42694; Tbio.
DR PRO; PR:P42694; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P42694; protein.
DR Bgee; ENSG00000198265; Expressed in colonic epithelium and 211 other tissues.
DR ExpressionAtlas; P42694; baseline and differential.
DR Genevisible; P42694; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Helicase; Hydrolase; Metal-binding;
KW Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1942
FT /note="Probable helicase with zinc finger domain"
FT /id="PRO_0000089185"
FT ZN_FING 178..206
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1117..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1386..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1729..1779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1792..1843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1870..1942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 794..797
FT /note="DEAA box"
FT COMPBIAS 1117..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1623..1637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1792..1826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1874..1892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1917..1942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 668..675
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1163
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1245
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 691
FT /note="T -> TS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054493"
FT VAR_SEQ 1130..1162
FT /note="GKSLHHTQNDHFQNDGIVQPNPSVLIGNPIRAY -> VKPLLMKLKRLKGEN
FT FAEVPKVYWDASYFKCWN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054494"
FT VAR_SEQ 1163..1942
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054495"
FT VARIANT 48
FT /note="C -> R (in dbSNP:rs2302669)"
FT /id="VAR_057273"
FT VARIANT 74
FT /note="V -> M (in dbSNP:rs8080100)"
FT /id="VAR_057274"
FT VARIANT 1530
FT /note="A -> V (in dbSNP:rs11653020)"
FT /id="VAR_057275"
SQ SEQUENCE 1942 AA; 218970 MW; B2EA41681C1A327D CRC64;
MEDRRAEKSC EQACESLKRQ DYEMALKHCT EALLSLGQYS MADFTGPCPL EIERIKIESL
LYRIASFLQL KNYVQADEDC RHVLGEGLAK GEDAFRAVLC CMQLKGKLQP VSTILAKSLT
GESLNGMVTK DLTRLKTLLS ETETATSNAL SGYHVEDLDE GSCNGWHFRP PPRGITSSEE
YTLCKRFLEQ GICRYGAQCT SAHSQEELAE WQKRYASRLI KLKQQNENKQ LSGSYMETLI
EKWMNSLSPE KVLSECIEGV KVEHNPDLSV TVSTKKSHQT WTFALTCKPA RMLYRVALLY
DAHRPHFSII AISAGDSTTQ VSQEVPENCQ EWIGGKMAQN GLDHYVYKVG IAFNTEIFGT
FRQTIVFDFG LEPVLMQRVM IDAASTEDLE YLMHAKQQLV TTAKRWDSSS KTIIDFEPNE
TTDLEKSLLI RYQIPLSADQ LFTQSVLDKS LTKSNYQSRL HDLLYIEEIA QYKEISKFNL
KVQLQILASF MLTGVSGGAK YAQNGQLFGR FKLTETLSED TLAGRLVMTK VNAVYLLPVP
KQKLVQTQGT KEKVYEATIE EKTKEYIFLR LSRECCEELN LRPDCDTQVE LQFQLNRLPL
CEMHYALDRI KDNGVLFPDI SMTPTIPWSP NRQWDEQLDP RLNAKQKEAV LAITTPLAIQ
LPPVLIIGPY GTGKTFTLAQ AVKHILQQQE TRILICTHSN SAADLYIKDY LHPYVEAGNP
QARPLRVYFR NRWVKTVHPV VHQYCLISSA HSTFQMPQKE DILKHRVVVV TLNTSQYLCQ
LDLEPGFFTH ILLDEAAQAM ECETIMPLAL ATQNTRIVLA GDHMQLSPFV YSEFARERNL
HVSLLDRLYE HYPAEFPCRI LLCENYRSHE AIINYTSELF YEGKLMASGK QPAHKDFYPL
TFFTARGEDV QEKNSTAFYN NAEVFEVVER VEELRRKWPV AWGKLDDGSI GVVTPYADQV
FRIRAELRKK RLSDVNVERV LNVQGKQFRV LFLSTVRTRH TCKHKQTPIK KKEQLLEDST
EDLDYGFLSN YKLLNTAITR AQSLVAVVGD PIALCSIGRC RKFWERFIAL CHENSSLHGI
TFEQIKAQLE ALELKKTYVL NPLAPEFIPR ALRLQHSGST NKQQQSPPKG KSLHHTQNDH
FQNDGIVQPN PSVLIGNPIR AYTPPPPLGP HPNLGKSPSP VQRIDPHTGT SILYVPAVYG
GNVVMSVPLP VPWTGYQGRF AVDPRIITHQ AAMAYNMNLL QTHGRGSPIP YGLGHHPPVT
IGQPQNQHQE KDQHEQNRNG KSDTNNSGPE INKIRTPEKK PTEPKQVDLE SNPQNRSPES
RPSVVYPSTK FPRKDNLNPR HINLPLPAPH AQYAIPNRHF HPLPQLPRPP FPIPQQHTLL
NQQQNNLPEQ PNQIPPQPNQ VVQQQSQLNQ QPQQPPPQLS PAYQAGPNNA FFNSAVAHRP
QSPPAEAVIP EQQPPPMLQE GHSPLRAIAQ PGPILPSHLN SFIDENPSGL PIGEALDRIH
GSVALETLRQ QQARFQQWSE HHAFLSQGSA PYPHHHHPHL QHLPQPPLGL HQPPVRADWK
LTSSAEDEVE TTYSRFQDLI RELSHRDQSE TRELAEMPPP QSRLLQYRQV QSRSPPAVPS
PPSSTDHSSH FSNFNDNSRD IEVASNPAFP QRLPPQIFNS PFSLPSEHLA PPPLKYLAPD
GAWTFANLQQ NHLMGPGFPY GLPPLPHRPP QNPFVQIQNH QHAIGQEPFH PLSSRTVSSS
SLPSLEEYEP RGPGRPLYQR RISSSSVQPC SEEVSTPQDS LAQCKELQDH SNQSSFNFSS
PESWVNTTSS TPYQNIPCNG SSRTAQPREL IAPPKTVKPP EDQLKSENLE VSSSFNYSVL
QHLGQFPPLM PNKQIAESAN SSSPQSSAGG KPAMSYASAL RAPPKPRPPP EQAKKSSDPL
SLFQELSLGS SSGSNGFYSY FK
