DYH1_RAT
ID DYH1_RAT Reviewed; 4516 AA.
AC Q63164;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Dynein axonemal heavy chain 1 {ECO:0000305};
DE AltName: Full=Axonemal beta dynein heavy chain 1;
DE AltName: Full=Ciliary dynein heavy chain 1;
GN Name=Dnah1 {ECO:0000312|RGD:621795}; Synonyms=Dlp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1756-1941 (ISOFORM 2), AND TISSUE
RP SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7657712; DOI=10.1242/jcs.108.5.1883;
RA Tanaka Y., Zhang Z., Hirokawa N.;
RT "Identification and molecular evolution of new dynein-like protein
RT sequences in rat brain.";
RL J. Cell Sci. 108:1883-1893(1995).
CC -!- FUNCTION: Force generating protein of cilia required for sperm
CC flagellum motility. 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. Required in spermatozoa
CC for the formation of the inner dynein arms and biogenesis of the
CC axoneme (By similarity). {ECO:0000250|UniProtKB:Q9P2D7}.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q9P2D7}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:E9Q8T7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q63164-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63164-2; Sequence=VSP_031309;
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:7657712}.
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; AABR03100255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03101829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03101330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D26492; BAA05500.1; -; mRNA.
DR PIR; I70171; I70171.
DR RefSeq; NP_001028827.2; NM_001033655.2.
DR SMR; Q63164; -.
DR STRING; 10116.ENSRNOP00000059841; -.
DR CarbonylDB; Q63164; -.
DR iPTMnet; Q63164; -.
DR PhosphoSitePlus; Q63164; -.
DR PaxDb; Q63164; -.
DR PRIDE; Q63164; -.
DR Ensembl; ENSRNOT00000035009; ENSRNOP00000032434; ENSRNOG00000026914. [Q63164-1]
DR Ensembl; ENSRNOT00000113143; ENSRNOP00000076750; ENSRNOG00000026914. [Q63164-2]
DR GeneID; 171339; -.
DR KEGG; rno:171339; -.
DR UCSC; RGD:621795; rat. [Q63164-1]
DR CTD; 25981; -.
DR RGD; 621795; Dnah1.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000154791; -.
DR HOGENOM; CLU_000038_0_0_1; -.
DR InParanoid; Q63164; -.
DR OMA; YWESAQK; -.
DR OrthoDB; 3185at2759; -.
DR PhylomeDB; Q63164; -.
DR PRO; PR:Q63164; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000026914; Expressed in testis and 4 other tissues.
DR ExpressionAtlas; Q63164; baseline and differential.
DR Genevisible; Q63164; RN.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0036156; C:inner dynein arm; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0036126; C:sperm flagellum; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0003341; P:cilium movement; IBA:GO_Central.
DR GO; GO:0060294; P:cilium movement involved in cell motility; ISO:RGD.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0036159; P:inner dynein arm assembly; ISO:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007288; P:sperm axoneme assembly; ISS:UniProtKB.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.10.8.720; -; 1.
DR Gene3D; 1.20.140.100; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 3.20.180.20; -; 1.
DR Gene3D; 3.40.50.300; -; 5.
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; 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; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF12774; AAA_6; 2.
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; 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; SSF52540; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Coiled coil;
KW Cytoplasm; Cytoskeleton; Dynein; Flagellum; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..4516
FT /note="Dynein axonemal heavy chain 1"
FT /id="PRO_0000318937"
FT REGION 1..1748
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 78..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1749..1956
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2016..2249
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2422..2682
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2780..2972
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2987..3285
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3388..3618
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3831..4050
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 3293..3394
FT /evidence="ECO:0000255"
FT MOTIF 1787..1794
FT /note="GPAGTGKT motif"
FT MOTIF 1837..1843
FT /note="CFDEFNR motif"
FT /evidence="ECO:0000250"
FT BINDING 1787..1794
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2054..2061
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2460..2467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2819..2826
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1867..1890
FT /note="SREYIKSLGGAVMCLPFLCVLYVQ -> VERFMFEGVEIPLVPSCAVFITMN
FT PGYAGRTELPDNLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7657712"
FT /id="VSP_031309"
SQ SEQUENCE 4516 AA; 515021 MW; F46AC5E8DCCC0BAF CRC64;
MVTLSISDTL HTPAFVENRH LAITGMPTRK ANNGFPSPDD NNVWGQFWKD LQTPLLVVVY
VHGAQCQLLL PIENRRVSSG SDKSLKNGME ECDKEEASTS SQGPGYCPAN VPENHDLEKM
LKESSRNPEK TSPNPELKTP PLPLSDLGQP RKSPLAGTDK KYPIMKQRGF YSDILSPGTL
DQLGDVCCGP YLSQNLIRQA DLDKFTPKGQ CHEHWAAESF VIPEDFQERV EQQSIGTTTR
LLTQTDFPLQ SYEPKVQVPF QVLPGRCPRK IEIERRKQQY LRLDIEQLLA NEGIDSNKLM
PRHPDLQQPQ TIEQGRDPLF PIYLPLKVFD NEEFDCRTPT EWLNMGLEPD AQYRKPVPGK
ALLPTDDALG HVHRAGCKQV SFSKCINTGI SLPEAGKKQS VSFTLDSNDR NNLTKLSPVL
QCLAIKPWEQ GHVKCTEFQL PRFTGALALS RNTRAKRGSQ EASTRDHLDF EDPKSQELDY
RWCEVGVLDY DEEKKLYLVQ KTDKRGLVRD EMGMPIVNGG VTPEGRPPLL DTQYWVPRIQ
LLFCAEDPRV FTQRVVQANA LRKNTEALLL YNLYVDCMPT EGQRVINEQS LSKIKQWALS
TPRMRKGPSV LEHLSSLARE VNLDYERSMN KINFDQIVSS KPETFSFVTL PEKEEEKVPN
QGLVSVPEYP FREQKEDFTF VSLLTRSEVI TALSKVRAEC NKVTSMSLFH SNLSKYSRLE
EFEQIQSQTF SQVQMFLKDS WISTLKVAMR SSLRDMSKGW YNLYETNWEV YLMSKLRKLM
ELIKYMLQDT LRFLVQDSLG SFAQFIGDAC CSVLECIDDM DWGEDLINSP YKPRKNPLFI
VDLVLDNTGV HYSTPLEQFE VILLNLFDKG ILATHAVPQL EKLVMEDIFI SGDPLLESVG
LHEPLVEELR ANITNAMHKA MIPLQAYAKE YRKTYQTQCP SAEEVREVVI THLKEKEILD
NSLPSSIIIG PFYINVDNVK QSLSKKRKAL ATSMLDILAK NLHNEVDSIC EEFRSISRKI
YEKPNSIEEL AELRDWMKGI PEKLVILEVR QALALAARSL VEPEVGPALE IPFNNPLPSM
TRHFLLMQER IVKVMSDYEV MDEFFYNLTT DDFNDKWAAN NWPTKILGQI DMVRQQHVED
EEKFRKIQLM DQNNFQEKLE GLQLVVAGFS THVEIARAHE IANEVRRVKK QLKDCQQLAM
LYNNRERIFG LPITNYDKLS RMVKEFQPYL DLWTTASDWL RWSESWMNDP LSAIDAEQLE
KNVIESFKTM HKCVKQFKDI PACQDVALDI RARIDEFKPY IPLIQGLRNP GMRNRHWEVL
SNEININVRP KANLTFARCL EMNLQDYIES ISKVAEVAGK EYAIEQALDK MEKEWASILF
NVLPYKETDT YILKSPDEAS QLLDDHIVMT QSMSFSPYKK PFEQRINSWE TKLKLTQEVL
EEWLNCQRSW LYLEPIFSSE DITRQLPVES KRYQTMERIW RKIMKNAYEN REVINVCSDQ
RLLDSLRDCN KLLDLVQKGL SEYLETKRTA FPRFYFLSDD ELLEILSQTK DPTAVQPHLR
KCFENIARLL FQEDLEITHM YSAEGEEVKL SFSIYPSSNV EDWLLEVERS MKASVHDIIE
MAIKAYPTML RTEWVLSWPG QVTIAGCQTY WTLEVAQALE ASSISSSLFP QLSKQLSDLV
ALVRGKLSRM QRMVLSALIV IEVHAKDVVS KLIDENVVSV HDFEWISQLR YYWTNNDLYI
RAVNAEFIYG YEYLGNSGRL VITPLTDRCY LTLTGALHLK FGGAPAGPAG TGKTETTKDL
GKALAIQTVV FNCSDQLDFM AMGKFFKGLA SAGAWACFDE FNRIDIEVLS VVAQQITTIQ
KAQQQRSREY IKSLGGAVMC LPFLCVLYVQ ALFRPVAMMV PDYAMIAEIS LYSFGFNEAN
VLAKKITTTF KLSSEQLSSQ DHYDFGMRAV KTVISAAGNL KRENPTMNEE LICLRAIRDV
NVPKFLQEDL KLFSGIVSDL FPTTKEEETD YGILDQAIRK ACEKNNLKDV EGFLIKCIQL
YETTVVRHGL MLVGPTGSGK SNCYRILAAA MTSLKGKPSI SGGVYEAVNY YVLNPKSITM
GQLYGEFDLL THEWTDGIFP SLIRAGAIAS DTNKKWYMFD GPVDAVWIEN MNTVLDDNKK
LCLSSGEIIK LTEAMTMMFE VQDLAVASPA TVSRCGMVYL EPSILGLMPF VECWLKHLPS
IIKPYEEQFK TLFVKFLESS IAFVRTTVKE VVASTNSNLT MSLLKLLDCF FKPFLPREGL
KKIPSEKLSH IPELIEPWFI FSLVWSVGAT GDHSSRLNFS QWLKIKMVFE QIKLAFPEEG
LVYDYRLDDA GISSTEDDDE DDEESKQVAT ALPAQEGGMV KPPGLWDLPP RDSGHLEKAT
LTASRSEAVA WVKWMDYSVP FTMMPDTNYC NIIVPTMDTM QMSYLLGMLI TNHKPVLCIG
PTGTGKTLTV SNKLLKNLPL EYISHFLTFS ARTSANQTQD LIDSKLDKRR KGVFGPPLGR
NFIFFIDDLN MPALETYGAQ PPIELLRQWM DHGGWYDRKI IGAFKNLVDI NFVCAMGPPG
GGRNAITPRL TRHFNYLSFI EMDEVSKKRI FSIILGCWMD GLLGEKSYRE PVPGAPNIVH
MTEPLVNATI SIYAIITSQL LPTPAKSHYT FNLRDLSKVF QGILMAEPAK VEDKVQLLRL
WYHENCRVFR DRLVNEEDRG WFDGLLEMKM EDLGVAFNKV CPFQPILYGD FMSPGSDVKS
YELITSENKM MQVIEEYMED YNQINTAKLK LVLFVDAMSH ICRISRTLRQ ALGNALLLGV
GGSGRSSLTR LASHMAEYEC FQVELSKNYG MSEWREDVKK ILLKAGMQNL PITFLFSDTQ
IKNESFLEDI NNILNSGDIP NLYSADEQDQ IVNTMRPYIQ EQGLQPTKAN LMAAYTGRVR
NNIHMVLCMS PIGEVFRARL RQFPSLVNCC TIDWFNEWPA EALQSVATRF LHEIPELECS
SEVIEGLIHV CVYIHQSVAK KCVEYLAELA RHNYVTPKSY LELLNIFSIL IGQKKMELKT
AKHRMKSGLD KLLRTSEDVA KMQEELEIMR PLLEEAAKDT LLTMDQIKVD TAIAEETRKS
VQAEEIKANE KASKAQAIAD DAQKDLDEAL PALDAALASL RNLNKNDVTE VRAMQRPPPG
VKLVIEAVCI MKGIKPKKVP GEKPGSKVDD YWEPGKGLLQ DPGRFLESLF KFDKDNIGEA
VIKAIQPYID NEEFQPAAIA KVSKACTSIC QWVRAMHKYH FVAKAVEPKR QALREAQDDL
EVTQRILEEA KHHLREVEDG ISTLQAKYRE CVTKKEELEM KCEQCEQRLG RADKSQSPGQ
PPGAHPTRLL LQLINGLADE KVRWQDTVEN LENMLDNIFG DVLVAAGFVA YLGPFTGQYR
AALYEYWVNQ LTVYGVPHTS KPTLISTLGN PVKIRSWQIA GLPNDTLSVE NGVINQFSQR
WTHFIDPQGQ ANKWIKNMEK ESGLDVFKLS DRDFLRSMEN AIRFGKPCLL ENVGEELDPA
LEPVLLKQTY KQQGNTVLKL GDTVIPYHED FRMYITTKLP NPHYSPEVST KLTLINFTLS
PSGLEDQLLG QVVAEERPDL EEAKNQLIIS NAKMRQELKD IEDQILYRLS SSEGNPVDDV
ELIKVLEASK MKAAEIQAKV RIAEQTEKDI DLTRMEYIPV AVRTQILFFC VSDLANVDPM
YQYSLEWFLN IFLSGIANSE RADNLKKRIV NINRYLTFSL YSNVCRSLFE KHKLMFAFLL
CVRIMMNEGK INQGEWRYLL SGGSIQTMSE NPAPHWLSDR AWRDILALSN LPAFSTFSTD
FVQHLPKFQA IFDSAEPHRE PLPGIWNTYL DEFQKLLILR CLRGDKVTNA MQDFVANHLE
PRFIEPQTAN LSAVFKESNS TTPLIFVLSP GTDPAADLYK FAEEMKFSKK LSAISLGQGQ
GPRAEAMMRN SIERGKWVFF QNCHLAPSWM PALERLIEHI NPDKVHRDFR LWLTSLPSNK
FPVSILQNGS KMTIEPPRGV KANLLKSYNS LSDDFLHSCQ KVVEFKSLLL SLCLFHGNAL
ERRKFGPLGF NIPYEFTDGD LRICISQLKM FLDEYEDIPY KVLKYTAGEI NYGGRVTDDW
DRRCVMNILE DFYNPAVLSP EHRYSKSGIY HQIPPTYDLN GYLSYIKSLP LNDMPEIFGL
HDNANITFAQ NETFALFGAI LQLQPKSSSM GGQSREELVE DVAEDILVQV PKPVDLEEVV
NKYPVLYEES MNTVLVQEVI RYNKLLMVIT QTLSDMLKAI KGLVVMSLEL ELMSTSLYNN
AVPELWKSKA YPSLKPLASW IMDLLQRLNF LHSWIKNGIP SVFWISGFFF PQAFLTGTLQ
NFARKFVISI DTITFDFKVL SYASSEIAER PSTGCYIYGL FLEGARWDPF DFQLAESRPK
ELYTEMAVIW LLPVANRKVQ NQDFYLCPIY KTLTRAGTLS TTGHSTNYVI AVEIPSNQPQ
RHWIKRGVAL ICALDY