DYH3_MOUSE
ID DYH3_MOUSE Reviewed; 4083 AA.
AC Q8BW94; O08829; Q7TT83;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Dynein axonemal heavy chain 3;
DE AltName: Full=Axonemal beta dynein heavy chain 3;
DE AltName: Full=Ciliary dynein heavy chain 3;
GN Name=Dnah3; Synonyms=Dnahc3;
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 1381-1584 (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 2388-4083 (ISOFORM 3).
RC TISSUE=Olfactory epithelium;
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 2980-4083 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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=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 of respiratory cilia. Produces force
CC towards the minus ends of microtubules. Dynein has ATPase activity; the
CC force-producing power stroke is thought to occur on release of ADP.
CC Involved in sperm motility; implicated in sperm flagellar assembly (By
CC similarity). {ECO:0000250}.
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:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BW94-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BW94-2; Sequence=VSP_031929, VSP_031930;
CC Name=3;
CC IsoId=Q8BW94-3; Sequence=VSP_031926, VSP_031927, VSP_031928;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35298.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC122853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z83816; CAB06070.1; -; mRNA.
DR EMBL; BC051401; AAH51401.1; -; mRNA.
DR EMBL; AK053178; BAC35298.1; ALT_INIT; mRNA.
DR SMR; Q8BW94; -.
DR STRING; 10090.ENSMUSP00000042857; -.
DR iPTMnet; Q8BW94; -.
DR PhosphoSitePlus; Q8BW94; -.
DR MaxQB; Q8BW94; -.
DR PaxDb; Q8BW94; -.
DR PRIDE; Q8BW94; -.
DR ProteomicsDB; 277644; -. [Q8BW94-1]
DR ProteomicsDB; 277645; -. [Q8BW94-2]
DR ProteomicsDB; 277646; -. [Q8BW94-3]
DR Antibodypedia; 67049; 29 antibodies from 6 providers.
DR Ensembl; ENSMUST00000046993; ENSMUSP00000042857; ENSMUSG00000052273. [Q8BW94-1]
DR MGI; MGI:2683040; Dnah3.
DR VEuPathDB; HostDB:ENSMUSG00000052273; -.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000154959; -.
DR HOGENOM; CLU_000038_0_0_1; -.
DR InParanoid; Q8BW94; -.
DR PhylomeDB; Q8BW94; -.
DR TreeFam; TF316836; -.
DR ChiTaRS; Dnah3; mouse.
DR PRO; PR:Q8BW94; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BW94; protein.
DR Bgee; ENSMUSG00000052273; Expressed in spermatid and 21 other tissues.
DR ExpressionAtlas; Q8BW94; baseline and differential.
DR GO; GO:0097729; C:9+2 motile cilium; IEA:UniProt.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0036156; C:inner dynein arm; ISM:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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:0007018; P:microtubule-based movement; IBA:GO_Central.
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; IPR003593; AAA+_ATPase.
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; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10676; PTHR10676; 1.
DR Pfam; PF12774; AAA_6; 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; 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 SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Coiled coil;
KW Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..4083
FT /note="Dynein axonemal heavy chain 3"
FT /id="PRO_0000322545"
FT REGION 1..1357
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1579
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 1639..1870
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2003..2251
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2362..2613
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2628..2927
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3012..3242
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3455..3679
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 1026..1052
FT /evidence="ECO:0000255"
FT COILED 1108..1133
FT /evidence="ECO:0000255"
FT COILED 2651..2714
FT /evidence="ECO:0000255"
FT COMPBIAS 111..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1396..1403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1677..1684
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2041..2048
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2401..2408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 2523..2530
FT /note="GTNRAYFS -> VRKNLHIV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031926"
FT VAR_SEQ 2720..2737
FT /note="KNECEGDLAEAMPALEAA -> KVCDQARGAQGANTAKRM (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031927"
FT VAR_SEQ 2738..4083
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031928"
FT VAR_SEQ 3921..3957
FT /note="EWIDKGPPVVFWISGFYFTQSFLTGVSQNYARKYTIP -> VPGNLGNWIPG
FT SSLRWRRHCGVAEQKLGTRVGSCVAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031929"
FT VAR_SEQ 3958..4083
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031930"
FT CONFLICT 1506..1509
FT /note="AELP -> SDLQ (in Ref. 2; CAB06070)"
FT /evidence="ECO:0000305"
FT CONFLICT 1514
FT /note="A -> P (in Ref. 2; CAB06070)"
FT /evidence="ECO:0000305"
FT CONFLICT 1520
FT /note="A -> P (in Ref. 2; CAB06070)"
FT /evidence="ECO:0000305"
FT CONFLICT 1570..1571
FT /note="MR -> IS (in Ref. 2; CAB06070)"
FT /evidence="ECO:0000305"
FT CONFLICT 3182
FT /note="P -> T (in Ref. 4; BAC35298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4083 AA; 467777 MW; 4E72F4B2EFF4A3CB CRC64;
MSDTNCSAQK LDKSDSVHHM SHSQARPELP PLPVSANEEP SELYKTVMSH SFYPPLMQRT
SWTLAVPFKE QDHHRGPSDS IGNNYSLTAR DMKLKDLLKV YQPVTISIPR DKTSQGLPLG
TSSKTSTEPS KKKMKFNLKA KDDVTGMPFV CKFSSSLSIK NTTDSSVTHP ESRPMSPEQQ
MDVMLQQEME IESKEQKPSE LDLERYYYYL TNGIRKDMIA PENEEVMMRI YKLIPKTLLT
TPALEPLQVS LRSEKESDYY YSLMKSIVDY ILMDPMEKKR LFIKSIPRLF PHRVIRAPVP
WHNIYQSTKK WNEEHLHTVN PMMYKLKELW FAEFQNLRFV RTADLLAGKL PLLPHEYKEV
VQKHCREARH ILLTKWIPTC AQLFVTQKEH WVHFAPKNDY DSSRNIEEYF ASVASFMSLQ
LRDLVIKSLR DLVSFFMIHK DGNDFKEPYQ EMDFFIPQLI MIKLEVRDPI IVFNPTFDDC
WQLIKNSFLE IIKNSDGIPK VYLCWKPLAS YICVSPHLRM TSVLQVESIL FPDLKGYNMI
LGTVNPEESL VSDFLDQTLE VFKKNQVGPY KYLNVYKKYD DLLDNMAEKG ISEFLKEKHE
IEDFVTSINS IKKRKNEIAS MHITVPLAMF CLDAVFLNYD LCERAQNLKD NLILYQVDVN
RETNTSICNQ YSTIADKVSE IPANTAELVA LIEYLKKSSD VTVFKLRRQL RDASERLEFL
MDYADLPSES IEDVFESSRN LLMSKRDQAE MDLIKRCSEF ESRLEGYSKE LEMFRKREVM
TTEEMKNNVE KLHDLSKNLD LALTEFELIN KEEELLEKEK SSFPLLQTLM INKIPYEQLW
VTAYEFSTKS EEWMNGPLYL MNAEQIAEEI GNMWRTTYKL TKTLIDVPAP KRLAENVKLK
IEKFKQHIPI LNIACNPGMK DRHWQQISDI VGYEIKPTET TCLANMLEYG FGKFVDKLEP
IGAAASKEYS LEKNLEKMKA DWVNMCFSFV KYRDTDTSIL CAVDDIQLIL DDHVIKTQTM
CGSVFIKPIE AECRKWEEKL VRVQENLDAW LKCQVTWLYL EPIFSSEDII AQMPEEGKKF
TTVDTYWKSL MAQAVNDTRV MVAADQPRMT EKLQEANVLL EDIQRGLNDY LEKKRLFFPR
FFFLSNDELL EILSETKDPL RVQPHLKKCF EGIAKLEFTD NLEIKGMISS EKETVPFIQT
IYPVKAKGMV EKWLQQVEQV MLASMRQVIE NGIEAYVQVP RNAWVLEWPG QVVICVSSIF
WTREVSEALV EDTLTDFLKK SNDQIAQIVE LVRGKLSSGA RLTLGALTVI DVHARDVVAK
LRHDHINSLN DFQWISQLRY YWTEKNVHVQ MITTEALYGY EYLGNSPRLV ITPLTDRCYR
TLMGALKLNL GGAPEGPAGT GKTETTKDLA KALAKQCVVF NCSDGLDYKA MGKFFKGLAQ
AGAWACFDEF NRIEVEVLSV VAQQILSIQQ AIIRKLKRFI FEGTELSLNP TCAVFITMNP
GYAGRAELPD NLKALFRTVA MMVPDYALIG EISLYSMGFL DSRSLAQKIV ATYRLCSEQL
SSQHHYDYGM RAVKSVLTAA GNLKLKYPEE NESVLLLRAL LDVNLAKFLA QDVPLFQGII
SDLFPGVVLP KPDYEVFLEA LNNNIRKMKL QPVPWFIGKI IQIYEMMLVR HGYMIVGDPM
GGKTSAYKVL AAALGDLHAA NQMEEFAVEF KIINPKAITM GQLYGCFDAV SHEWTDGVLA
NAFREQASSI TDDRKWIIFD GPVDAVWIEN MNTVLDDNKK LCLMSGEIIQ MSSKMSLIFE
PADLEQASPA TVSRCGMIYM EAHQLGWKPL KDSYMDTLPR CLTKEHTELV EDMFTWLVQP
CLDFSRLHCK FVVQTSPIHL AFSMMRLYSS LLDEIRDIQE EEMEIYEGLS SQQIFLWLQG
LFLFSLVWTL AGTINAESRK KFDVFFRNLI MGMDDRNPRP KSVKLTKNNI FPERGSIYDF
YFLKQGGGHW NAWTEYITKE EETIPANAKV SDLIIPTMET ARQSFFLKTY LDHEIPILFV
GPTGTGKSAI TNDFLLHLPK NVYQPNFINF SARTSANQTQ DIIMSKLDRR RKGLFGPPIG
KKAVVFVDDL NMPAKEVYGA QPPIELLRQW IDHGYWFDKK DTNRLDIVDV LLVTAMGPPG
GGRNDITGRF TRHLNIISIN AFEDEILTKI FSSIADWHFG KGFDVMFLRY GKMLVQATQT
IYRAAVENFL PTPSKSHYVF NLRDFSRVIQ GVLLCPHTHL QDLEKFIRLW IHEVYRVFYD
RLIDNDDRQT FFNLVKETTS NCFKQTMEKV LIHLSPTGKI TDDNIRSLFF GDYLKPESDQ
KIYDEIIDLR GLTVVMEYYL DEFNSVSKAP MSLVMFKFAI EHISRICRVL KQKKGHLLLV
GIGGSGRQSA TKLSTFMNSY ELYQIEITKN YTNSDWREDL KKIMLQSGVA TKSTVFLFSD
NQIKHESFVE DINMLLNTGD VPNIFPADEK ADLVEKMQTA ARTEGEKVEA TPLSMYNFFI
ERGTNRAYFS LAMSPIGDAF RTRLRMFPSL INCCTIDWFQ SWPTDALELV ANKFLEDVEL
DDNIRAEVVS MCKYFQESVK KLSVDYYNTL LRHNYVTPTS YLELILTFKT LLNSKRQEVD
TIRNRYLAGL QKLEFASSQV AVMQVELTAL QPQLIQTSED TAMMMVKIEL ETKEADAKKL
LVQADEKEAN AAAAISQAIK NECEGDLAEA MPALEAALAA LDTLNPSDIT LVKSMQNPPG
PVKLVMESIC VMKGLKPERK PDPSGSGKMI EDYWGVSRKI LGDLKFLESL KTYDKDNIPS
VIMKRIRERF IDHPDFQPAV IKNVSSACEG LCKWVRAMEV YDRVAKVVAP KRERLREAEG
KLEIQMQKLN QKRAELKLVE DRLQDLNDEF ELMNRKKNSL EKNIEICSQK LVRAEKLISG
LGGEKDRWTE AARQLGIRYD NLTGDVLLAS GTVAYLGAFT VDYRAQCQNE WLVSCKDKVI
PGSVDFSLSN TLGDPIKIRA WQIAGLPVDS FSVDNGIIVS NSRRWPLMID PQGQANKWVK
NMEKTNKLSV IKFSDTNYVR TLENALQFGT PVLLENVGEE LDAFIEPILL KATFKQQGVE
YMRLGENIIE YSREFKFYIT TRLRNPHYLP EVAVKVCLLN FMITPLGLQD QLLGIVAAKE
KPELEEKKNK LILESAQNKK QLKEIEDKIL EVLSLCEGNI LEDETAIKIL SSSKVLSEEI
SEKQEIASVT ETQIDETRMG YKPVAVHSAA IFFCISDLAH IEPMYQYSLT WFINLYVQSL
ANSNKSDELD LRIEYIIEHF TLSIYNNVCR SLFEKDKLLF SLLLTVGLLK ERKAIDEEVW
YFLLTGGVAL DNPFPNPAPE WLSEKSWGEI VRASSLQKLK GLMEDVMQNI KVWKDIYDSA
WPHEESLPSP WFFLQTLEKI AILRCLRPDK IVPAIQNFIC ETMGKIFIEA PTFDLQGSYG
DSSCCVPLIF ILSPGADPMA GLLKFADDVS MGGTKTQTIS LGQGQGPIAA NMINKAIHEG
TWVVLQNCHL ATSWMPALEK ICEEVIVPEN TNSEFRLWLT SYPSEKFPVS ILQNGIKMTN
EPPKGLRANL LRSYLNDPIS DPLFFQSCTK PVIWQKLLFG LCFFHAIVQE RRNYGALGWN
IPYEFNESDL RISMRQIQMF LNDYEEVPFE ALTYLTGECN YGGRVTDDKD RRLLLSLLSM
FYCKEIETDN YHIAPGDAYV IPPYGSYQSY IEYLRTLPIT AHPEVFGLHE NADITKDNQE
TNQLFQGVLL TLPRQSGGSG KSPQEVVEEL AQDILSKLPN DFNLEEVMKK YPVVYKESMN
TVLRQELIRF NRLTKVVRRS LIDLGRAIKG QVLMSSELEE VFNSMLVGKV PAMWAAKSYP
SLKPLGGYVA DLLARLTFFQ EWIDKGPPVV FWISGFYFTQ SFLTGVSQNY ARKYTIPIDH
IGFEFEVTPK ETTMENIPED GAYIKGLFLE GARWDRSTSQ IGESLPKILY DPLPIIWLKP
GESASFLHQD IYVCPVYKTS ARRGILSTTG HSTNYVLSIE LPTDMPQKHW INRGVASLCQ
LDN
