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   27-MAR-2024, entry version 140.
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};
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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; 7.
DR   IntAct; Q6DFV5; 1.
DR   STRING; 10090.ENSMUSP00000074533; -.
DR   GlyGen; Q6DFV5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6DFV5; -.
DR   PhosphoSitePlus; Q6DFV5; -.
DR   EPD; Q6DFV5; -.
DR   jPOST; Q6DFV5; -.
DR   MaxQB; Q6DFV5; -.
DR   PaxDb; 10090-ENSMUSP00000074533; -.
DR   PeptideAtlas; Q6DFV5; -.
DR   ProteomicsDB; 269583; -. [Q6DFV5-1]
DR   ProteomicsDB; 269584; -. [Q6DFV5-2]
DR   ProteomicsDB; 269585; -. [Q6DFV5-3]
DR   Pumba; Q6DFV5; -.
DR   Antibodypedia; 31693; 122 antibodies from 14 providers.
DR   DNASU; 78455; -.
DR   Ensembl; ENSMUST00000075012.8; ENSMUSP00000074533.2; ENSMUSG00000020721.17. [Q6DFV5-3]
DR   Ensembl; ENSMUST00000100305.8; ENSMUSP00000097878.2; ENSMUSG00000020721.17. [Q6DFV5-2]
DR   Ensembl; ENSMUST00000106746.8; ENSMUSP00000102357.2; ENSMUSG00000020721.17. [Q6DFV5-1]
DR   GeneID; 78455; -.
DR   KEGG; mmu:78455; -.
DR   UCSC; uc007mav.1; mouse. [Q6DFV5-3]
DR   AGR; MGI:1925705; -.
DR   CTD; 9931; -.
DR   MGI; MGI:1925705; Helz.
DR   VEuPathDB; HostDB:ENSMUSG00000020721; -.
DR   eggNOG; KOG1804; Eukaryota.
DR   GeneTree; ENSGT00940000156686; -.
DR   InParanoid; Q6DFV5; -.
DR   OMA; KREMAPE; -.
DR   OrthoDB; 5405202at2759; -.
DR   PhylomeDB; Q6DFV5; -.
DR   TreeFam; TF323999; -.
DR   BioGRID-ORCS; 78455; 2 hits in 77 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 254 other cell types or tissues.
DR   ExpressionAtlas; Q6DFV5; baseline and differential.
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:regulatory ncRNA-mediated post-transcriptional gene silencing; IBA:GO_Central.
DR   CDD; cd18077; DEXXQc_HELZ; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR049569; HELZ_DEAD-box_1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10887:SF365; HELICASE WITH ZINC FINGER DOMAIN-RELATED; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   Genevisible; Q6DFV5; MM.
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
//