ID DYH17_MOUSE Reviewed; 4481 AA.
AC Q69Z23; O08820;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 24-JAN-2024, entry version 116.
DE RecName: Full=Dynein axonemal heavy chain 17 {ECO:0000305};
DE AltName: Full=Axonemal beta dynein heavy chain 17;
DE AltName: Full=Ciliary dynein heavy chain 17;
GN Name=Dnah17 {ECO:0000312|MGI:MGI:1917176}; Synonyms=Dnahc17, Kiaa3028;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1836-1936 (ISOFORM 1).
RC STRAIN=NMRI; TISSUE=Testis;
RX PubMed=9373155; DOI=10.1016/s0378-1119(97)00417-4;
RA Neesen J., Koehler M.R., Kirschner R., Steinlein C., Kreutzberger J.,
RA Engel W., Schmid M.;
RT "Identification of dynein heavy chain genes expressed in human and mouse
RT testis: chromosomal localization of an axonemal dynein gene.";
RL Gene 200:193-202(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2192-4479 (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Force generating protein component of the outer dynein arms
CC (ODAs) in the sperm flagellum. Produces force towards the minus ends of
CC microtubules. Dynein has ATPase activity; the force-producing power
CC stroke is thought to occur on release of ADP. Plays a major role in
CC sperm motility, implicated in sperm flagellar assembly and beating.
CC {ECO:0000250|UniProtKB:Q9UFH2}.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000250|UniProtKB:Q9UFH2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q69Z23-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69Z23-2; Sequence=VSP_032116, VSP_032117;
CC -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC (which binds cargo and interacts with other dynein components), and the
CC head or motor domain. The motor contains six tandemly-linked AAA
CC domains in the head, which form a ring. A stalk-like structure (formed
CC by two of the coiled coil domains) protrudes between AAA 4 and AAA 5
CC and terminates in a microtubule-binding site. A seventh domain may also
CC contribute to this ring; it is not clear whether the N-terminus or the
CC C-terminus forms this extra domain. There are four well-conserved and
CC two non-conserved ATPase sites, one per AAA domain. Probably only one
CC of these (within AAA 1) actually hydrolyzes ATP, the others may serve a
CC regulatory function (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; AL591204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z83807; CAB06061.1; -; mRNA.
DR EMBL; AK173343; BAD32621.1; -; mRNA.
DR SMR; Q69Z23; -.
DR STRING; 10090.ENSMUSP00000081864; -.
DR GlyGen; Q69Z23; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q69Z23; -.
DR PhosphoSitePlus; Q69Z23; -.
DR jPOST; Q69Z23; -.
DR MaxQB; Q69Z23; -.
DR PaxDb; 10090-ENSMUSP00000101915; -.
DR ProteomicsDB; 277641; -. [Q69Z23-1]
DR ProteomicsDB; 277642; -. [Q69Z23-2]
DR AGR; MGI:1917176; -.
DR MGI; MGI:1917176; Dnah17.
DR eggNOG; KOG3595; Eukaryota.
DR InParanoid; Q69Z23; -.
DR PhylomeDB; Q69Z23; -.
DR PRO; PR:Q69Z23; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q69Z23; Protein.
DR GO; GO:0097729; C:9+2 motile cilium; IBA:GO_Central.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0036157; C:outer dynein arm; ISS:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IEA:InterPro.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0060294; P:cilium movement involved in cell motility; IBA:GO_Central.
DR GO; GO:0036158; P:outer dynein arm assembly; ISS:UniProtKB.
DR Gene3D; 1.10.287.2620; -; 1.
DR Gene3D; 1.10.472.130; -; 1.
DR Gene3D; 1.10.8.1220; -; 1.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.20.1270.280; -; 1.
DR Gene3D; 1.20.58.1120; -; 1.
DR Gene3D; 1.20.920.20; -; 1.
DR Gene3D; 1.20.920.30; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 6.10.140.1060; -; 1.
DR Gene3D; 1.20.140.100; Dynein heavy chain, N-terminal domain 2; 1.
DR Gene3D; 3.20.180.20; Dynein heavy chain, N-terminal domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
DR InterPro; IPR041658; AAA_lid_11.
DR InterPro; IPR042219; AAA_lid_11_sf.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR041589; DNAH3_AAA_lid_1.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
DR InterPro; IPR041228; Dynein_C.
DR InterPro; IPR043160; Dynein_C_barrel.
DR InterPro; IPR024743; Dynein_HC_stalk.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR013594; Dynein_heavy_tail.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45703:SF4; DYNEIN AXONEMAL HEAVY CHAIN 17; 1.
DR PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12775; AAA_7; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF17857; AAA_lid_1; 1.
DR Pfam; PF18198; AAA_lid_11; 1.
DR Pfam; PF08385; DHC_N1; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF18199; Dynein_C; 1.
DR Pfam; PF03028; Dynein_heavy; 1.
DR Pfam; PF12777; MT; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Coiled coil;
KW Cytoplasm; Cytoskeleton; Dynein; Flagellum; Kelch repeat; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..4481
FT /note="Dynein axonemal heavy chain 17"
FT /id="PRO_0000323750"
FT REPEAT 521..569
FT /note="Kelch 1"
FT REPEAT 1533..1566
FT /note="TPR 1"
FT REPEAT 1688..1722
FT /note="TPR 2"
FT REPEAT 2229..2275
FT /note="Kelch 2"
FT REPEAT 2782..2834
FT /note="Kelch 3"
FT REPEAT 4138..4173
FT /note="TPR 3"
FT REPEAT 4272..4321
FT /note="Kelch 4"
FT REPEAT 4339..4385
FT /note="Kelch 5"
FT REGION 1..1792
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1793..2014
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2074..2295
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2401..2649
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2747..2996
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3011..3297
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3389..3616
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3826..4059
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 759..826
FT /evidence="ECO:0000255"
FT COILED 3011..3071
FT /evidence="ECO:0000255"
FT COILED 3241..3293
FT /evidence="ECO:0000255"
FT BINDING 1831..1838
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2112..2119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2439..2446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2785..2792
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 3828..3852
FT /note="NFVEEKMGSKFVEGRSVEFSKSYKE -> EKTGIYHRQWETPQRVPGARTRG
FT GS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_032116"
FT VAR_SEQ 3853..4481
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_032117"
SQ SEQUENCE 4481 AA; 511603 MW; A64E53D65671224E CRC64;
MPDLRIDYLE TVSSVLLKFK ADKWGKLIGA EENMALLTEF FDKIDNPVLV LTLNAAGMII
PCLGFPESLK SKGVYFIKMK PENITKDNYK THLIYGDISP TTVDQLIAVV EEVLYSLLNQ
SENMDGWPRV VSEDIVKQVH RLKNEMFVMG GKIKGKTLLP IPEHLGSLDG TLDSMERIPS
SMDNSLLHSI ETIIIDWSHQ IRDVLSKDSA QALLDGLHPL PRVEFEFWDA RLMNLQCIHE
QLNRPKVNKI VEILEKAKSC YWPALQNVYM NVTQGLKEAN GIVLYLKPLR ILLEEMEQAD
FTMLPSFIVK VLSTICFIWA TSEHYNTPSR VIVILREFCN QIIEMTRTYL SPDEVLKGLQ
GEIEEVLGNI SLSVSVLKGL FQAYDFCCAN MKLFFKDRPP VPWEFPSSLA FSRMNSFFHR
VQTIEDLYKT AIEFLKLEKI ELGGVWGNIL GNLVTQIYDE VFELVKVFAE CKYDPLDPGD
SSFDDDYSDF ETKIQDLDRR LATIFCQAFD DCNCMESSAK LLYMCGGLLE RPLILVEVVP
RYSVMLEMFN TELDNAKLMY DAQMAASADG QIPPIHKNMS PVSGQLKWSL ELQERLEVSM
KYLKHIEHPV MSSMEAKLIY DKYDEMMGLL QSCRMKKYQQ WVEGVDQDCH FNLGQPLIQR
DPFTSLIQVN FSKALVAVLR EVKYLNFQQQ KEIPESAEKL FSENETFRKF VGNLELIVGW
YNEIKTTVKD VEFPLIKSEL EAIDVKLLSA ETTLFWNGEN VMEYIQEMRE MLYNLQNRIQ
KAKQNVEGIT QAMQEWSANP LFERKDNKKE ALLDLDGRVA NLNKRYAAVK EAGVRIQAMV
VENAELFRAD TTSQSWKDYV NYIDTVVLDE FDRFIRKSLN YLMDNMTMDE SIAPLFEIRM
ELDKDGLTYN PSLEMGDEAG FLSLIEGLIN DLYNVARLIP RLAKGRLNYK SDLEDITDLI
EMREEVSSLV IGAMKVAEEY QDSFERYSYL WVDDLQEFMK NFLIFGHAPT PEELDTKTDD
TIPKTPPTLA QFQQQIDSYE KLYEEVSSCE NTKVFHGWLQ CDCRPFKQTL LNTIKRWSFL
FKRYLNNHVI NSLADLESFM NITRTALKKP LKEGDYDGLV EVMGHLMKVK ERQVATDSMF
EPLKQTIELL KSYGEEMPEE IYLKLQELPE QWTNTKKLAI QVKQNVAPLQ ANEVNILRRK
CQQFELKQHE FREKFRRDAP FSFSDPEPYK SLNKIYLLYG VMEALCKSAS LFEVTVPDYK
QLKACHREVR LLKELWDMIV MVNTSIDDWK TTKWKDINVE QMDIDCKKFA KDVRSLDKEM
KPWDAFVGLD NTVKNMITSL RAVSELQNPA IRDRHWQQLM QATQVKFEMS EETTLADLLQ
LNLHKYEDEV RNIVDKAVKE SGMEKVLKTL DITWTTMEFE HELHPRTGTM MLKSDEVLVE
TLEDNQVQLQ NLMMSKYLSH FLKEVTSWQQ KLSTADSVIS IWFEVQRTWS HLESIFIGSE
DIRAQLPEDS KRFDAIDQEF KALMEDAVKT PNVVEATNKP DLYNKLENLK MSLAVCEKAL
AEYLETKRLA FPRFYFVSSA DLLDILSNGN DPVEVSRHLS KLFDSLCKLK FRLDASGKPL
KFGLGMYSKE DEFVDFDKEC DLSGQVEVWL NRVLDRMRAT LRHEIPEAVV TYEEKPREQW
IFDYPAQIWW TTEVGLAFAR LEEGYENAIK DYNKKQISQL NALITLLIGN LTAGDRMKIM
TICTIDVHAR DVVAKMITVE SSQAFTWQSQ LRHRWDEEKK HCFANICDAQ IKYSYEYLGN
TPRLVITPLT DRCYITLTQS LHLIMGGAPA GPAGTGKTET TKDLGRALGT MVYVFNCSEQ
MDYKSCGNIY KGLAQTGAWG CFDEFNRISV EVLSVIAVQV KCVQDAIRAK KKKFNFLGEI
ISLVPTVGIF ITMNPGYAGR TELPENLKAL FRPCAMVVPD FELICEIMLV AEGFLDARLL
ARKFITLYTL CKELLSKQDH YDWGLRAIKS VLVVAGSLKR GDPTRAEDQV LMRALRDFNI
PKIVTDDLPV FMGLIGDLFP ALDVPRKRDL NFEKIIKQSI VELKLQAEDS FVLKVVQLEE
LLQVRHSVFV IGNAGSGKSQ VLKSLNKTYQ NLKRKPVAVD LDPKAVTCDE LFGIINPATR
EWKDGLFSTI MRDLANLTHE GPKWIVLDGD IDPMWIESLN TVMDDNKVLT LASNERIPLN
RTMRLVFEIS HLRTATPATV SRAGILYINP ADLGWNPVVS SWIERRKVQS EKANLIILFD
KYLPTCLDKL RIGFKRITPV PEITVIQTIL YLLECLLTEK NAPPDSPKEL YELYFVFACF
WAFGGAMFQD QLIDYRVEFS KWWINEFKTI KLPSQGTIFD YYIDPETKKF LPWTDKVPNF
ELDPDIPLQA SLVHTTETIR IRYFIDLLME KAWPVMLVGN AGTGKSVLMG DKLENLSTDD
YLVQAVPFNF YTTSAMLQGV LEKPLEKKSG RNYGPPGTKK LIYFIDDMNM PEVDKYGTVA
PHTLIRQHMD HRHWYDRQKL TLKDVHNCQY VACMNPTSGS FTIDPRLQRH FCVFAVSFPG
QEALTSIYNT ILAQHLSFRS APLVIQRLSS HLVTAALALH QKVSATFLPT AIKFHYIFNL
RDLSNIFQGI LFSTAEILKT PLDLVRLWLH EAERVYGDKM VDEKDQETLH RVTIASVKKF
FDDLGEENLF AKPNIFCHFT QGIGDPKYFP VTDVAQLNKL LKDVLDSYNE VNAVMNLVLF
EDAVAHICKI NRILESPRGN ALLVGVGGSG KQSLSRLAAY ISALDVFQIT LKKGYAIPDL
KMDLATQYIK SAVKNVPSVF LMTDSQVAEE QFLVLINDLL ASGEIPGLFG DEDLENIISS
MRPQVKSLGI ADTREACWKF FIEKVRRQLK VILCFSPVGS VLRVRARKFP AVVNCTAINW
FHEWPEDALV SVSARFLEET EGIEPEVKTS ISLFMAYVHT TVNEMSKIYL TIERRYNYTT
PKTFLEQIKL YQNLLAKKRM ELVAKIERLE NGLMKLQSTA SQVDDLKAKL AVQETELKQK
NENADKLIQV VGVETEKVSK EKAIADEEEM KVEVINKNVT EKQKACETDL AKAEPALLAA
QEALDTLNKN NLTELKSFGS PPDAVVNVTA AVMILTAPGG KIPKDKSWKA AKIMMGKVDT
FLDSLKKFDK EHIPEACLKA FKPYQGNPTF DPEFIRSKST AAAGLCSWCI NIVRFYEVYC
DVAPKRQALE EANAELAEAQ EKLSRIKNKI AELNANLSNL TSAFEKATAE KIKCQQEADA
TNRVISLANR LVGGLASENV RWAESVENFK SQGVTLCGDV LLISAFVSYV GYFTKKYRNE
LMEKFWIPYI NKLKVPIPIT EGLDPLTLLT DDADVATWNN QGLPSDRMST ENATILCNTE
RWPLIVDAQL QGIKWIKNKY GSDLQAIRLG QKSYLDIIEQ AISAGDTLLI ENIGETVDPV
LDPLLGRNTI KKGRFIKIGD KEVEYHPSFR LILHTKYFNP HYKPEMQAQC TLINFLVTRD
GLEDQLLAAV VAKERPDLEQ LKANLTKSQN EFKIVLKELE DSLLARLSAA SGNFLGDTAL
VENLETTKHT ANEIEEKVQE AKITEVKINE ARENYRPAAE RASLLYFILN DLNKINPIYQ
FSLKAFNVVF EKAIQKTAPA DEVKQRVINL TDEITYSVYM YTARGLFERD KLIFLAQVTF
QVLSMKKELN PVELDFLLRF PFKAGVVSPV DFLQHQSWGG IKALSEMDEF KNLDSDIEGS
AKRWKKLVES EAPEKEIFPK EWKNKTALQK LCMVRCMRPD RMTYAVKNFV EEKMGSKFVE
GRSVEFSKSY KESSPSTPIF FILSPGVDPL KDVEALGKKL GFTIDNGKLH NVSLGQGQEV
VAENALDVAA EKGHWVILQV RGSLPQNIHL VARWLGILDK KVERYSSGSH EDYRVFISAE
PAPTAETHII PQGILENAIK ITNEPPTGMY ANLHKALDLF TQDTLEMCTK EIEFKCILFA
LCYFHAVVAE RRKFGAQGWN RSYPFNNGDL TISINVLYNY LEANSKVPWD DLRYLFGEIM
YGGHITDDWD RRLCRTYLAE YIRVEMLEGE VLLAPGFQIP PNLDYKGYHE YIDENLPPES
PYLYGLHPNA EIGFLTVTSE KLFRTVLEMQ PKETDSGAGT GVSREEKVGA VPVPEGSLGS
EGSLGTIGLP GTGFQVKAVL DDILEKIPET FNMAEIMAKA AEKTPYVVVA FQECERMNIL
TNEMRRSLKE LNLGLKGELT ITTDMEDLST ALFYDTVPDT WVARAYPSMM GLAAWYADLL
QRIRELESWT TDFALPTTVW LAGFFNPQSF LTAIMQSMAR KNEWPLDKMC LSVEVTKKNR
EDMTAPPREG SYVYGLFMEG ARWDTQTGVI AEARLKDLTP VMPVIFIKAI PVDRMETKNI
YECPVYKTRI RGPTYVWTFN LKTKEKAAKW ILAAVALLLQ V
//
