DYH2_MOUSE
ID DYH2_MOUSE Reviewed; 4456 AA.
AC P0C6F1; B1AR18; O08826; Q8C0U5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Dynein axonemal heavy chain 2 {ECO:0000305};
DE AltName: Full=Axonemal beta dynein heavy chain 2;
DE AltName: Full=Ciliary dynein heavy chain 2;
GN Name=Dnah2 {ECO:0000312|MGI:MGI:107731}; Synonyms=Dnahc2;
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 1805-2008.
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 2794-4456.
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 [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).
RN [5]
RP FUNCTION, INTERACTION WITH DNAI4, AND SUBCELLULAR LOCATION.
RX PubMed=30060180; DOI=10.1093/jmcb/mjy043;
RA Zhang Y., Chen Y., Zheng J., Wang J., Duan S., Zhang W., Yan X., Zhu X.;
RT "Vertebrate Dynein-f depends on Wdr78 for axonemal localization and is
RT essential for ciliary beat.";
RL J. Mol. Cell Biol. 11:383-394(2019).
CC -!- FUNCTION: As part of the axonemal inner dynein arm complex plays a
CC central role in ciliary beat (PubMed:30060180). Expressed in sperm
CC flagellum, it is required for sperm motility (By similarity). Dyneins
CC are microtubule-based molecular motors possessing ATPase activities
CC that can convert the chemical energy of ATP into relative sliding
CC between adjacent microtubule doublets to generate ciliary bending
CC (PubMed:30060180). {ECO:0000250|UniProtKB:Q9P225,
CC ECO:0000269|PubMed:30060180}.
CC -!- SUBUNIT: Part of the axonemal inner dynein arm complex that consists of
CC at least two heavy chains and a number of intermediate and light chains
CC (PubMed:30060180). Interacts with DNAI4 (PubMed:30060180).
CC {ECO:0000269|PubMed:30060180}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:30060180}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000250|UniProtKB:Q9P225}.
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=BAC26619.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL596125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z83813; CAB06067.1; -; mRNA.
DR EMBL; AK029791; BAC26619.1; ALT_INIT; mRNA.
DR SMR; P0C6F1; -.
DR IntAct; P0C6F1; 1.
DR STRING; 10090.ENSMUSP00000104299; -.
DR iPTMnet; P0C6F1; -.
DR PhosphoSitePlus; P0C6F1; -.
DR EPD; P0C6F1; -.
DR PaxDb; P0C6F1; -.
DR PRIDE; P0C6F1; -.
DR ProteomicsDB; 277643; -.
DR Antibodypedia; 66685; 69 antibodies from 18 providers.
DR Ensembl; ENSMUST00000035539; ENSMUSP00000047329; ENSMUSG00000005237.
DR MGI; MGI:107731; Dnah2.
DR VEuPathDB; HostDB:ENSMUSG00000005237; -.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000157623; -.
DR HOGENOM; CLU_000038_9_0_1; -.
DR InParanoid; P0C6F1; -.
DR ChiTaRS; Dnah2; mouse.
DR PRO; PR:P0C6F1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P0C6F1; protein.
DR Bgee; ENSMUSG00000005237; Expressed in spermatocyte and 77 other tissues.
DR ExpressionAtlas; P0C6F1; baseline and differential.
DR Genevisible; P0C6F1; MM.
DR GO; GO:0005858; C:axonemal dynein complex; IDA:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0036156; C:inner dynein arm; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
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; 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; IMP:UniProtKB.
DR GO; GO:0060285; P:cilium-dependent cell motility; ISS:UniProtKB.
DR GO; GO:0036159; P:inner dynein arm assembly; ISS:UniProtKB.
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; 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 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; PF08385; DHC_N1; 2.
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 ATP-binding; Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Dynein; Flagellum; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..4456
FT /note="Dynein axonemal heavy chain 2"
FT /id="PRO_0000322543"
FT REPEAT 1439..1474
FT /note="TPR 1"
FT REPEAT 2750..2783
FT /note="TPR 2"
FT REPEAT 3101..3134
FT /note="TPR 3"
FT REPEAT 4101..4134
FT /note="TPR 4"
FT REPEAT 4135..4169
FT /note="TPR 5"
FT REGION 1..1795
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1794..2015
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2075..2302
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2407..2654
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2751..3003
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3018..3301
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3387..3617
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3833..4052
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 1218..1274
FT /evidence="ECO:0000255"
FT COILED 3041..3078
FT /evidence="ECO:0000255"
FT COILED 3245..3333
FT /evidence="ECO:0000255"
FT COILED 3552..3596
FT /evidence="ECO:0000255"
FT BINDING 1832..1839
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2113..2120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2445..2452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2791..2798
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 1893
FT /note="V -> L (in Ref. 2; CAB06067)"
FT /evidence="ECO:0000305"
FT CONFLICT 1895
FT /note="S -> P (in Ref. 2; CAB06067)"
FT /evidence="ECO:0000305"
FT CONFLICT 1898
FT /note="A -> P (in Ref. 2; CAB06067)"
FT /evidence="ECO:0000305"
FT CONFLICT 1900
FT /note="Q -> K (in Ref. 2; CAB06067)"
FT /evidence="ECO:0000305"
FT CONFLICT 1909
FT /note="T -> S (in Ref. 2; CAB06067)"
FT /evidence="ECO:0000305"
FT CONFLICT 2004
FT /note="F -> Y (in Ref. 2; CAB06067)"
FT /evidence="ECO:0000305"
FT CONFLICT 2006
FT /note="L -> M (in Ref. 2; CAB06067)"
FT /evidence="ECO:0000305"
FT CONFLICT 2007
FT /note="R -> S (in Ref. 2; CAB06067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4456 AA; 511565 MW; C57E71F45BDC3C58 CRC64;
MASKAEKKRK VAGRGGARAG RVVRAPQSTA GPGATEASLL PDGQEPEPES GKEDSVLGLQ
AFASWRLTPA LHGEANTPPT LLHPQPLFHR RLTTLNLILS CSRAGTRDLA LKPFFLSRTM
LTGLADATWT GEHDMVLEHF VQDPAVPALT IFIDPVFGLK LELGMPVQTQ NQIVYFIRQA
PVPITPENFE ETVQYGTVRG AYIPALLRLL SGVYVPQIFM NKSWPESIRN HFVSHLHRFL
ASLTDTRYKL EGHTVLYIPA EAVQMDPEVV VKDKELVQRL ETSMIHWTRQ IKEVLSAQES
VETGENLGPL EEIEFWHNRC MDLSSISKQL VKKGVKHIES ILFLAKSSYL TPFRKLAQQI
QDGSRQAQSN LTFLSILREP YQELAFMKPK DISEKLPKLI SLIRIIWVNS PHYNTRERLT
ALFRKVCECQ YHFARWEDGK QGPLPCFFGA QGPQITRNLL EIEDIFHKNL QTLRAVRGGI
LDVKNTSWHE DYNKFRGGIK DLEVMTQNLI TSAFELVRDV EHGVLLLDTF HRLATREAIM
RTYEKKAVDL YMLFNSELAL VNRELNKKWP YLEPYMTQYS GQAHWVRILR RRIDRVMNCL
SGAHFLPHIG TGEESIHTYQ QMAQAIDEMV RKTFQEWTAT LDKDCIRRLD MSLLRISQEK
VGMLDVNFDK TLLILFAEID YWERLLFETP HYVMNVAERA EDLRILRENL LLVARDYNRI
IAMLSPDEQA LFKERIRFLD KKIHPGLKKL NWALKGASAF FITECRMHAS KVQMIVNDFK
ASTLTIGWKA QEMSELLLVH ITGKQVYRDL EFEEAQREHR MAAQQKLVKL HQDVVNIMTN
SYEVFKNDGP EIQQQWLLYT IRLDHMMEDA LRLNVKWSLL ELSKAINGDG KTTPNPLFRV
LVILQNDVRG GGSQVEFSPT LQTLASVVND IGSHLFATIS VFRHLPDILT KRKMNREPIY
VLVERDEDIR KIQAQISSGM TNNASLLQNY LKTWDMYREI WEINKDSFIR RYQRLNPPVS
SFDADIARYT EVANNVQKEE TVLNIQFVML DCSHLKFSLV QHCNEWQNKF TTLLKEMAAG
RLADLHSYLK DNAEKISHPP QTLEELGVSL QLMDTLQHDL PNLETQIPPI HEQFTILEKY
EVPVPDTVLE MLESLNGEWL TFQQILLDSE QMLKKHKEKF KTGLIHAADD FKKKAHNLLE
DFEFKGPFTS TVGHTAALDQ IAQMRAMLMA MRDEENNLRS NLGIFKIEQP VSKDLQILEK
ELDALQQVWE ITRDWEESWN QWKMGCFQTL QTEAMESMAH GLFRRLTRLA KEYKDRNWEI
IETTRSKIEQ FKRTMPLISD LRNPALRERH WDQVKEEVQR EFDQESESFT LEQIVKLGMD
QHVEKIAEIS ASATKELAIE VGLQNIAKTW DSTQLDIVPY KDKGHHRLRG TEEVFQALED
NQVALSTMKA SRFVKAFEKD VDHWERCLSL ILEVIEMVLT VQRQWMYLEN IFLGEDIRKQ
LPNESALFDQ VNNNWKAIMD RMNKDNNALR STHYPGLLET LIEMNAILED IQKSLDMYLE
TKRHIFPRFY FLSNDDLLEI LGQSRNPEAV QPHLKKCFDN IKLLKIQKVG GSSSKWEAVG
MFSGDGEYID FLHPVLLEGP VESWLGDVER AMRMTLRDLL RNCRVALKKF LNKRDKWVKD
WAGQVVITAS QIQWTADVTK CLMTAKERSD KKILKVSILN KYSEAIRGNL TKIMRLKIVA
LVTIEIHARD VLEKLYKSGL MDVSSFDWLS QLRFYWEKDV DDCIIRQTNT QFQYGYEYLG
NSGRLVITPL TDRCYMTLTT ALHLHRGGSP KGPAGTGKTE TVKDLGKALG IYVIVVNCSE
GLDYKSMGRM YSGLAQSGAW GCFDEFNRIN IEVLSVVAQQ ILSILSALTA NLTRFYFEGF
EINLVWSCGI FITMNPGYAG RTELPENLKS MFRPIAMVVP DSTLIAEIIL FGEGFGNCKI
LAKKVYTLYS LAVQQLSRQD HYDFGLRALT SLLRYAGKKR RLQPDLSDEE VLLLSMRDMN
IAKLTSVDVP LFNAIVQDLF PNIELPVIDY GKLRDTIEQE IREMGLQITP FTLTKVLQLY
ETKNSRHSTM IVGGTGSSKT TSWKILQASL TSLCRAGEPN YNIVREFPLN PKALSLGELY
GEYDLNTNEW TDGILSSVMR VACADEKPDE KWILFDGPVD TLWIESMNSV MDDNKVLTLI
NGERIAMPEQ VSLLFEVENL AVASPATVSR CGMVYTDYVD LGWKPYVQSW LEKRPKTEVE
PLQRMFEKFI NKILSFKKDN CNELVPVPEY SGIISLCKLY TVLATPENGV NPADAENYSF
MVEMTFVFSM IWSVCASVDE DGRKKIDSYL REIEGSFPNK DTVYEYYVNP KMRTWTSFEE
KLPKSWRYPP NAPFYKIMVP TVDTVRYNYL VSTLVANQNP VLLVGPVGTG KTSIAQSVLQ
SLPSSQWSVL VVNMSAQTTS NNVQSIIESR VEKRTKGVYV PFGGKSMITF MDDLNMPAKD
MFGSQPPLEL IRLWIDYGFW YDRVKQSIKH IRDMFLMAAM GPPGGGRTVI SPRLQSRFNI
INMTFPTESQ IIRIFGTMIN QKLQDFEEEV KPIGNVVTEA TLDVYNTVVQ RFLPTPAKIH
YLFNLRDISK VFQGMLRANK DFHDTKASIT RLWIHECFRV FSDRLVDTAD MEAFMGILSD
KLGTFFDLTF HHLCPNKRPP IFGDFLKEPK VYEDLVDLTV LKTAMETALN EYNLSPSVVP
MQLVLFREAI EHITRIVRVI GQPRGNMLLV GIGGSGRQSL ARLASSICDY NTFQIEVTKH
YRKQEFRDDI KRLYRQAGVE LQTTSFLFVD TQIADESFLE DINNILSSGE VPNLYKSDEF
EEIQNHIIDQ ARAEQIPESS DSLFAYLIER VRNNLHIVLC LSPVGDPFRN WIRQYPALVN
CTTINWFSEW PREALLEVAE KYIIGVDLGT QENIHRKVAQ IFVTMHWSVA QYSQKMLLEL
RRYNYVTPTN YLELVSGYKK LLGEKRQELL DQANKLRTGL FKIDETREKV EVMSLELEDA
KKKVAEFQKQ CEEYLVIIVQ QKREADEQQK AVTANSEKIA IEEVKCQALA DNAQKDLEEA
LPALEEAMRA LESLNKKDIG EIKSYGRPPA QVEIVMQAVM ILRGNEPTWA EAKRQLGEQN
FIKSLINFDK DNISDKVLKK IGAYCAQPDF QPDIIGRVSL AAKSLCMWVR AMELYGRLYR
VVEPKRIRMN AAMAQLQEKQ AALAEAQEKL REVAEKLEML KKQYDEKLAQ KEELRKKSEE
MELKLERAGM LVSGLAGEKA RWEETVQGLE EDLGYLVGDC LIAAAFLSYM GPFLTNYRDE
IINQIWIRKI RELQVPCSPR FAIDNFLTNP TKVRDWNIQG LPSDAFSTEN GIIVTRGNRW
ALMIDPQGQA LKWIKNMEGN QGLKIIDLQM HDYLRVLEHA IQFGFPVLLQ NVQEYLDPTL
NPVLNKSVAR IGGRMLIRIG DKEVEYNPNF RFYLTTKLSN PHYNPETSAK TTIVNFAVKE
QGLEAQLLGI VVRKERPELE EQKDSLVINI AAGKRKLKEL EDEILRLLNE ATGSLLDDVQ
LVNTLQTSKI TATEVTEQLE TSETTEINID LAREAYRPCA QRASVLFFVL NDMGRIDPMY
QFSLDAYIGL FILSIDKSHR SNKLEDRIEY LNDYHTYAVY RYTCRTLFER HKLLFSFHMC
AKILETSGKL NMDEYNFFLR GGVVLDREGQ MDNPCTSWLA DAYWDNITEL DKLTNFHGLM
NSFEQYPRDW HLWYTNSSPE KAMLPGEWEN ACNEMQRMLI VRSLRQDRVA FCVTSFIVSN
LGSRFIEPPV LNMKSVMEDS TPRSPLVFIL SPGVDPTSAL LQLAEHTGMA HRFHALSLGQ
GQAPIAARLL REGVNQGHWV FLANCHLSLS WMPNLDKLVE QLQVEDPHPS FRLWLSSSPH
PDFPISILQA SIKMTTEPPK GLKANMTRLY QLMTEAQFTH CSKPAKYKKL LFALCFFHSI
LLERKKFLQL GWNIIYGFND SDFEVSENLL SLYLDEYEET PWDALKYLIA GVNYGGHVTD
DWDRRLLTTY INDYFCDLSL TTPFYRLSVL DTYYIPKDGS LASYKEYISM LPSMDPPEAF
GQHPNADVAS QITEARTLFE TLLSLQPQIT PTRVGGQSRE EKVLELAADV KQKIPEMIDY
EGTRKLLALD PSPLNVVLLQ EIQRYNKLMK TILFSLTDLE KGIQGLIVMS TSLEEIFNCI
FDAHVPPLWG KVYPSQKPLA SWTRDLAVRV EQFETWASRA RPPVLFWLSG FTFPTGFLTA
VLQSAARQNN ISVDSLSWEF IVSTVDDSNL VYPPKDGVWV RGLYLEGAGW DRKNSCLVEA
EPMQLVCLMP TIHFRPAESR KKSAKGMYSC PCYYYPNRAG STDRASFVIG IDLRSGSMTS
DHWIKRGTAL LMSLDS
