HELZ_MOUSE
ID HELZ_MOUSE Reviewed; 1964 AA.
AC Q6DFV5; A1L4L4; A2AAU4; Q8BZZ6; Q8CHI3; Q8VDI3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable helicase with zinc finger domain;
DE EC=3.6.4.-;
GN Name=Helz; Synonyms=Kiaa0054;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Head, and Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 750-1964.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1763, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH SMYD2.
RX PubMed=20305823; DOI=10.1371/journal.pone.0009748;
RA Diehl F., Brown M.A., van Amerongen M.J., Novoyatleva T., Wietelmann A.,
RA Harriss J., Ferrazzi F., Bottger T., Harvey R.P., Tucker P.W., Engel F.B.;
RT "Cardiac deletion of Smyd2 is dispensable for mouse heart development.";
RL PLoS ONE 5:E9748-E9748(2010).
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 {ECO:0000250}.
CC -!- SUBUNIT: Interacts with POLR2A. Interacts with SMYD3; the interaction
CC may bridge SMYD3 and RNA polymerase II (By similarity). Interacts with
CC SMYD2. {ECO:0000250, ECO:0000269|PubMed:20305823}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6DFV5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6DFV5-2; Sequence=VSP_035796, VSP_035797;
CC Name=3;
CC IsoId=Q6DFV5-3; Sequence=VSP_035795;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41393.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB093209; BAC41393.1; ALT_INIT; mRNA.
DR EMBL; AL645947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021818; AAH21818.1; -; mRNA.
DR EMBL; BC076626; AAH76626.1; -; mRNA.
DR EMBL; AK033094; BAC28150.1; -; mRNA.
DR CCDS; CCDS25569.1; -. [Q6DFV5-3]
DR CCDS; CCDS88275.1; -. [Q6DFV5-1]
DR RefSeq; NP_938040.1; NM_198298.1. [Q6DFV5-3]
DR RefSeq; XP_006534567.1; XM_006534504.1. [Q6DFV5-3]
DR RefSeq; XP_006534568.1; XM_006534505.3. [Q6DFV5-3]
DR RefSeq; XP_006534569.1; XM_006534506.3. [Q6DFV5-3]
DR RefSeq; XP_006534570.1; XM_006534507.2.
DR AlphaFoldDB; Q6DFV5; -.
DR SMR; Q6DFV5; -.
DR BioGRID; 219414; 6.
DR IntAct; Q6DFV5; 1.
DR STRING; 10090.ENSMUSP00000074533; -.
DR iPTMnet; Q6DFV5; -.
DR PhosphoSitePlus; Q6DFV5; -.
DR EPD; Q6DFV5; -.
DR jPOST; Q6DFV5; -.
DR MaxQB; Q6DFV5; -.
DR PaxDb; Q6DFV5; -.
DR PeptideAtlas; Q6DFV5; -.
DR PRIDE; Q6DFV5; -.
DR ProteomicsDB; 269583; -. [Q6DFV5-1]
DR ProteomicsDB; 269584; -. [Q6DFV5-2]
DR ProteomicsDB; 269585; -. [Q6DFV5-3]
DR Antibodypedia; 31693; 89 antibodies from 14 providers.
DR DNASU; 78455; -.
DR Ensembl; ENSMUST00000075012; ENSMUSP00000074533; ENSMUSG00000020721. [Q6DFV5-3]
DR Ensembl; ENSMUST00000100305; ENSMUSP00000097878; ENSMUSG00000020721. [Q6DFV5-2]
DR Ensembl; ENSMUST00000106746; ENSMUSP00000102357; ENSMUSG00000020721. [Q6DFV5-1]
DR GeneID; 78455; -.
DR KEGG; mmu:78455; -.
DR UCSC; uc007mav.1; mouse. [Q6DFV5-3]
DR CTD; 9931; -.
DR MGI; MGI:1925705; Helz.
DR VEuPathDB; HostDB:ENSMUSG00000020721; -.
DR eggNOG; KOG1804; Eukaryota.
DR GeneTree; ENSGT00940000156686; -.
DR InParanoid; Q6DFV5; -.
DR OMA; REMAPEY; -.
DR OrthoDB; 286011at2759; -.
DR PhylomeDB; Q6DFV5; -.
DR TreeFam; TF323999; -.
DR BioGRID-ORCS; 78455; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Helz; mouse.
DR PRO; PR:Q6DFV5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6DFV5; protein.
DR Bgee; ENSMUSG00000020721; Expressed in embryonic post-anal tail and 251 other tissues.
DR ExpressionAtlas; Q6DFV5; baseline and differential.
DR Genevisible; Q6DFV5; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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..1964
FT /note="Probable helicase with zinc finger domain"
FT /id="PRO_0000354096"
FT ZN_FING 178..206
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1116..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1631..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1743..1964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 794..797
FT /note="DEAA box"
FT COMPBIAS 1307..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1781..1795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1802..1816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1823..1851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1869..1883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1897..1914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1945..1964
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:0000250|UniProtKB:P42694"
FT MOD_RES 1163
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P42694"
FT MOD_RES 1245
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P42694"
FT MOD_RES 1636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42694"
FT MOD_RES 1760
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42694"
FT MOD_RES 1763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42694"
FT VAR_SEQ 691
FT /note="T -> TS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035795"
FT VAR_SEQ 1598..1616
FT /note="FQDLLRELSHRDQGDTGEL -> YSSRPGPALITTCVWSASL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12465718"
FT /id="VSP_035796"
FT VAR_SEQ 1617..1964
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12465718"
FT /id="VSP_035797"
FT CONFLICT 963
FT /note="I -> T (in Ref. 4; BAC28150)"
FT /evidence="ECO:0000305"
FT CONFLICT 1193
FT /note="L -> P (in Ref. 4; BAC28150)"
FT /evidence="ECO:0000305"
FT CONFLICT 1496
FT /note="I -> N (in Ref. 4; BAC28150)"
FT /evidence="ECO:0000305"
FT CONFLICT 1746
FT /note="A -> V (in Ref. 3; AAH21818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1964 AA; 219880 MW; BED050BC57CFE065 CRC64;
MEDRRAERSC EQACASLQRQ DYDMALQHCT DALLSLGQYS MADFTGPCPV EVERIKIESL
LYRIASFLQL KNYGQADEDC RHVLGEGLAK GERAFRAVLC CMQLKGKLQL VSSILAKSLS
GESLNGMVTK DLTRLKTLLT ETETATSNVL SGCHVEDLDE GSCNGWHFRP PPRGITSSEE
YTLCKRFLEQ GICRYGAQCT SAHSQEELAE WQKRYASRLI KLKQQSENKQ LSGSYMETLI
EKWMSSLSPE KVLSECIEGV QVEHSPDLSV TVNTKKSHQT WTFALTCKPA RMLYRVALLY
DAHRPHFSII AISAGDSTTQ VSQEVPENCQ EWIGGKMAQN GLDHYVYKVG IAFNTEIFGT
FRQTIVFDFG LEPVLMQRVM IDAASTEDLE YLMHAKRQLV TTAKRWDSSS KTIVDFEPNE
TTDLEKSLLI RYQIPLSADQ LFTQSVLDKS LTKTNYQARL HDLLYIEEIA QYKEVSRFNL
KVQLQILASF MLTGVSGGAK YAQNGQLFGR FKLTETLSED TLAGRLVMTR VNAVYLLPVP
KEKLVQSQGT KEKVYEATIE EKTKDYVFLR ISRECCEELS LRPDCDIQVE LQFQLNRLPL
CEMHYALDRI KDNAVLFPDI SMTPTIPWSP NRQWDEQLDP RLNAKQKEAV LAITTPLSIQ
LPPVLIIGPY GTGKTFTLAQ AAKHILQQQE TRILICTHSN SAADLYIKDY LHPYVEAGNP
QARPLRVYFR NRWVKTVHPV VHQYCLISST QSTFQMPQKE DILKHRVVVV TLSTSQYLCQ
LDLEPGFFTH VLLDEAAQAM ECETIMPLAL ATKNTRIVLA GDHMQLSPFV YSEFARERNL
HVSLLDRLYE HYPAEFPCRI LLCENYRSHE AIINYTSELF YEGKLMASGK QPAHKDFYPL
TFFTARGEDV QEKNSTAFYN NAEVFEVVER VEELRRKWPV AWGKLDDGSI GVVTPYADQV
FRIRAELRKK RLSDVNVERV LNVQGKQFRV LFLSTVRTRH TCKHKQTPIK KKEQLLEDST
EDLDYGFLSN YKLLNTAITR AQSLVAVVGD PVALCSIGRC RKFWERFIAL CHENHSLHGI
TFEQIKAQLE ALELKKTYVL NPLAPEFIPR ALRLQHSGNS SRQQQSPPKV KSLYHPQSDH
FQSDGIVQPN PSVLIGNPIR AYTPPPPLGP HPNLGKSPSP VQRIDPHTGT SILYVPAVYG
GNVVMSVPLP VPWTGYQGRF AVDPRIITHQ AAMAYNMNLL HTHGRGSPIP YGLGHHPPVS
LGQPQSQHAE KDQQEQNRNG KTDTNNPGPE INKIRTPEKK PTEPKQVDLE SNPQNRSPES
RPGVVYSNTK FPRKDHLNPR HINNLPLPAP HAQYAIPSRH FHPLPQLPRP PFPASQPHTL
LNQQQNNLPE QPNQMAPQPN QVAPQPNQMT PQPNQVAPQP NQVVQQQSQA PPQAPQPAPQ
LSPAFQAGPT NAFFNNAVAH RPQSPAAEAV GPEQPPPPGL PDGHSPLRAI TQPGPILASP
LNNFVDESSP GLPIEEALDG VHGSVALETL RQQQARLQQW SEHHAYLSQG GIPYSHHHHP
HLPHLPHTPI GLHQPPVRAE WKVAGRADDE TETTFSRFQD LLRELSHRDQ GDTGELAEMP
PPQSRLLQYR QVQPRSPPAV PSPPSSTDHS SQFANFNDSS RDIEVANSPA FPQRLPPQLF
GSPFSLPSEH LAPPPLKYLA PEGAWNFANL QQNHLIGPGF PYGLPPLPPR PPQNPFIHIQ
NHQHAAGQEP FHPLSSRTVS ASSLPSLEEY EPRGPGRPLY QRRISSSSAQ PCVEEASAPQ
DSLAQGKESQ GHSNPPAFNF PAPESWANTT SSAPYQNIPC NGSSRTSQPR ELIAPPKTVK
PPEDQLKPES GEVSSSFNYS MLQHLGQFPP LMPNKQIAES ANCSSQQSPA GSKPAMSYAS
ALRAPPKPRP PPEQAKKGSD PLSLLQELSL GSSPGSNGFY SYFK
