DYH5_MOUSE
ID DYH5_MOUSE Reviewed; 4621 AA.
AC Q8VHE6; E9QKD7; Q8BWG1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Dynein axonemal heavy chain 5 {ECO:0000305};
DE AltName: Full=Axonemal beta dynein heavy chain 5;
DE Short=mDNAH5;
DE AltName: Full=Ciliary dynein heavy chain 5;
GN Name=Dnah5 {ECO:0000312|MGI:MGI:107718}; Synonyms=Dnahc5;
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 [MRNA], AND DISEASE.
RC STRAIN=C57BL/6J X CBA/J;
RX PubMed=11912187; DOI=10.1093/hmg/11.6.715;
RA Ibanez-Tallon I., Gorokhova S., Heintz N.;
RT "Loss of function of axonemal dynein Mdnah5 causes primary ciliary
RT dyskinesia and hydrocephalus.";
RL Hum. Mol. Genet. 11:715-721(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] OF 2481-3749.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11788826; DOI=10.1038/ng817;
RA Olbrich H., Haeffner K., Kispert A., Voelkel A., Volz A., Sasmaz G.,
RA Reinhardt R., Hennig S., Lehrach H., Konietzko N., Zariwala M., Noone P.G.,
RA Knowles M., Mitchison H.M., Meeks M., Chung E.M.K., Hildebrandt F.,
RA Sudbrak R., Omran H.;
RT "Mutations in DNAH5 cause primary ciliary dyskinesia and randomization of
RT left-right asymmetry.";
RL Nat. Genet. 30:143-144(2002).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15269178; DOI=10.1093/hmg/ddh219;
RA Ibanez-Tallon I., Pagenstecher A., Fliegauf M., Olbrich H., Kispert A.,
RA Ketelsen U.-P., North A., Heintz N., Omran H.;
RT "Dysfunction of axonemal dynein heavy chain Mdnah5 inhibits ependymal flow
RT and reveals a novel mechanism for hydrocephalus formation.";
RL Hum. Mol. Genet. 13:2133-2141(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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 Required for structural and functional integrity of the cilia of
CC ependymal cells lining the brain ventricles.
CC {ECO:0000269|PubMed:15269178}.
CC -!- SUBUNIT: Interacts with DNAL1 (By similarity). Consists of at least two
CC heavy chains and a number of intermediate and light chains.
CC {ECO:0000250|UniProtKB:M0R8U1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q8TE73}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in lung and kidney and weaker
CC expression seen in brain, heart and testis. In the brain, expressed in
CC ependymal cells lining the brain ventricles and the aqueduct.
CC {ECO:0000269|PubMed:11788826, ECO:0000269|PubMed:15269178}.
CC -!- DEVELOPMENTAL STAGE: Embryos show a weak expression confined to the
CC node from 7.0 to 8.25 dpc. {ECO:0000269|PubMed:11788826}.
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.
CC -!- DISEASE: Note=Defects in Dnah5 are the cause of primary ciliary
CC dyskinesia (PCD). PCD is characterized by recurrent respiratory
CC infections, situs inversus and ciliary immotility and hydrocephalus.
CC {ECO:0000269|PubMed:11912187}.
CC -!- DISRUPTION PHENOTYPE: Mice display defects in motility of the ependymal
CC cells lining the brain ventricles and aqueduct. This results in
CC impaired flow of cerebrospinal fluid through the cerebral aqueduct and
CC gives rise to closure of the aqueduct and subsequent formation of
CC triventricular hydrocephalus during early postnatal brain development.
CC {ECO:0000269|PubMed:15269178}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; AF466704; AAL69993.1; -; mRNA.
DR EMBL; AC131997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK052643; BAC35077.2; -; mRNA.
DR CCDS; CCDS27404.1; -.
DR RefSeq; NP_579943.3; NM_133365.3.
DR SMR; Q8VHE6; -.
DR BioGRID; 225282; 3.
DR IntAct; Q8VHE6; 1.
DR STRING; 10090.ENSMUSP00000069751; -.
DR iPTMnet; Q8VHE6; -.
DR PhosphoSitePlus; Q8VHE6; -.
DR EPD; Q8VHE6; -.
DR MaxQB; Q8VHE6; -.
DR PaxDb; Q8VHE6; -.
DR PeptideAtlas; Q8VHE6; -.
DR PRIDE; Q8VHE6; -.
DR ProteomicsDB; 277647; -.
DR Antibodypedia; 50446; 62 antibodies from 15 providers.
DR DNASU; 110082; -.
DR Ensembl; ENSMUST00000067048; ENSMUSP00000069751; ENSMUSG00000022262.
DR GeneID; 110082; -.
DR KEGG; mmu:110082; -.
DR UCSC; uc007vjy.1; mouse.
DR CTD; 1767; -.
DR MGI; MGI:107718; Dnah5.
DR VEuPathDB; HostDB:ENSMUSG00000022262; -.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000155533; -.
DR HOGENOM; CLU_000038_9_1_1; -.
DR InParanoid; Q8VHE6; -.
DR OMA; RNFSNMK; -.
DR OrthoDB; 6295at2759; -.
DR PhylomeDB; Q8VHE6; -.
DR TreeFam; TF316836; -.
DR BioGRID-ORCS; 110082; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Dnah5; mouse.
DR PRO; PR:Q8VHE6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8VHE6; protein.
DR Bgee; ENSMUSG00000022262; Expressed in olfactory epithelium and 18 other tissues.
DR Genevisible; Q8VHE6; MM.
DR GO; GO:0097728; C:9+0 motile cilium; IDA:MGI.
DR GO; GO:0097729; C:9+2 motile cilium; IDA:MGI.
DR GO; GO:0005858; C:axonemal dynein complex; IMP:MGI.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0036157; C:outer dynein arm; IDA:MGI.
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:0003777; F:microtubule motor activity; IMP:MGI.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0003341; P:cilium movement; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0021670; P:lateral ventricle development; IMP:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0036158; P:outer dynein arm assembly; ISO:MGI.
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; IPR013594; Dynein_heavy_tail.
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; 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 SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Ciliopathy; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Dynein; Microtubule; Motor protein; Nucleotide-binding;
KW Primary ciliary dyskinesia; Reference proteome; Repeat.
FT CHAIN 1..4621
FT /note="Dynein axonemal heavy chain 5"
FT /id="PRO_0000114631"
FT REGION 1..1938
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 901..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1939..2161
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2221..2440
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2547..2800
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2913..3167
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3182..3479
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3564..3794
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 4009..4223
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 260..305
FT /evidence="ECO:0000255"
FT COILED 803..825
FT /evidence="ECO:0000255"
FT COILED 1065..1094
FT /evidence="ECO:0000255"
FT COILED 1433..1462
FT /evidence="ECO:0000255"
FT COILED 3186..3299
FT /evidence="ECO:0000255"
FT COILED 3423..3490
FT /evidence="ECO:0000255"
FT COILED 3729..3814
FT /evidence="ECO:0000255"
FT COILED 4389..4417
FT /evidence="ECO:0000255"
FT COMPBIAS 904..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1977..1984
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2259..2266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 892
FT /note="V -> A (in Ref. 1; AAL69993)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="A -> S (in Ref. 1; AAL69993)"
FT /evidence="ECO:0000305"
FT CONFLICT 3854..3858
FT /note="RSVKS -> SLSRA (in Ref. 1; AAL69993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4621 AA; 527558 MW; CC6F243FF149B214 CRC64;
MFRIGRRQLW KQSVTRVLTQ RLKEEKEAKR ARLDGRHDYL FAIVASCLDL NKPEVEDALL
EGNQIERMDQ LFAVGGLRHL MFYYQDVEGA EAGHCGSSGG VNPASGKMKK PKVFVTEGKD
VALMGACVFF IRSDPSKAIT PENIHREVSF NTLDTADGGL LNSVRRLLSD IFIPALRASS
HGWGELEGLQ DASSIRQEFL SSLEGFVGIL SGAQNSLKEK VNLQKCDIIE LKSLKEPTDY
LALASNPETV EKVECCMRVW IKQMEQILAE NSQLRKEADD VGPRAELEHW KQRLSRFNYL
LDQLKSPDVK AALALLAAAK SKLLKVWRDT DIRITDAANE AKDNVKYLYT LEKCCDPLYS
SDPVTMIDAI PTLINAIKMV YSISHYYNTS EKITSLFVKV TNQMISACKA HITNNGTATI
WSQPQEIVMQ KIAAVIKLKQ GYQSCFQETK QKLKQNPSEK QFDFSEMYIF GKFETFHRRL
AKIMDIFTTF KTYSVLQDSK IEGLEDMATK YQDIVAAIKK KEYNFLDQRE MDFDQDYEEF
CKRINELHND LQRFMDITFE KIPSTRQALS TLKKFERLNI PNLGIEEKYQ IIFQNFATDI
DTISKLYTKQ KYDPPLARNQ PPIAGKILWA RQLFHRLEQP MQLFQQHPFV LRTAEAKPVI
RSYNRIAKVL LEFEVLYHRA WLQQIEEIHA GLEASLLVKA PGTGELFVNF DPQILVLFRE
TQCMSQLGLP VSPFAAALFQ KRDMFKKNFS DMKMMLSEYE RVKLKMPPAI EQLMFPHLAR
VDEALQPGLA VLTWTSLNIG GYLENAFAKI KDLELLLDRV NDLIEFRIHA ILEEMSSMAL
CQLPQDDPLT CEEFLQMTKD LCVSGAQLLH FKSSLVEEAV NELINMLLDV DVPPEEAAEN
VCHENASPSG NTSGRREGHS EALASSFNAG ASSLPLTATA RKKKETEVLE EARELLSHFN
HQNTDALLKV TRNTLEAIRR RIHFSHMINF RDSNDASKAK QNHLPIFRAS VTLAIPNIAM
TPALEDIQQT LNKAVECIIS VPKGVRQWSS ELLSKRKMHE RKMAAVKNNE DSDSDAEVEE
NELQETLEIA SINLPIPVQT QNYYKNISDN KEIVKLVSVL STVISSTKKE VITSMDRFKR
YNHIWQKEKE DTIMTFIAQN PLLPEFESRI LYFQSLEQEI NAEPEYIRVG SIALYTADLK
LSLTAETKAW MAVIGRHCNR KYRAEMENIL TVVEESQKKL SRPIKDLDDI RIAMAALKEI
REQQISTDFQ VGPIEESYAL LNKYGLLVAK EEMDKVDTLR YAWEKLLARA SDVQNELGAL
QPSFRKELIS TVEVFLQDCQ QFYLDYDLNG PMASGLKPQE ASGRLIIFQN QFDNIYRKYI
TYTGGEELFG LPVTPYPQLL EIKRQLNLLQ KIYSLYNNVI ETVNSYQDTL WSDVNIEKIN
NELLEFQNRC RKLPRALKDW QAFLDLKKTI DDFSECCPLL EYMASNAMVE RHWQRITALT
GHSLDVGNET FKLRNIMEAP LLKYKEEIED ICISAVKERD IEQKLRQVIN EWDNKTLTFS
GFKTRGELLL RGDSTSEVIA SMEDSLMLLG SLLSNRYNMP FKAQIQKWVQ CLSNSTDIIE
NWMTVQNLWI YLEAVFVGGD IAKQLPKEAK RFSNIDKSWV KIMTRAHEIP NVVQCCVGDE
TMGQLLPHLL DQLEICQKSL TGYLEKKRLC FPRFFFVSDP ALLEILGQAS DSHTIQAHLL
NVFDNIKTVK FHDKIYDRIL SISSREGETI ELDKPVMAEG NVEVWLNSLL EESQSSLHLV
IRQAAANIQE PGFQLIEFLS SFPAQVGLLG IQMLWTRDSE EALRNAKFDK KIMQKTNQAF
LELLNMLIEI TTKDLSSMER VKYETLITIH VHQRDIFDDL CHMHVKSPTD FEWLKQCRFY
FKEDSDKTMI HITDVAFIYQ NEFLGCTDRL VITPLTDRCY ITLAQALGMS MGGAPAGPAG
TGKTETTKDM GRCLGKYVVV FNCSDQMDFR GLGRIFKGLA QSGSWGCFDE FNRIDLPVLS
VAAQQISIIL TCKKEHKKSF IFTDGDNVTM NPEFGLFLTM NPGYAGRQEL PENLKINFRS
VAMMVPDRQI IIRVKLASCG FIDNVVLARK FFTLYQLCEE QLSKQVHYDF GLRNILSVLR
TLGAAKRASP TDTESTIVMR VLRDMNLSKL IDEDEPLFLS LIEDLFPNIL LDKAGYPELE
TAISKQVEEA GLINHPPWKL KVIQLFETQR VRHGMMTLGP SGSGKTTCIH TLMKAMTDCG
KPHREMRMNP KAITAPQMFG RLDVATNDWT DGIFSTLWRK TLKAKKGEHI WIVLDGPVDA
IWIENLNSVL DDNKTLTLAN GDRIPMAPNC KIVFEPHNID NASPATVSRN GMVFMSSSVL
DWSPILEGFL KRRSPQEAEI LRQLYAETFP DLYRFSIQNL EFKMEVLEAF VITQSTHMLQ
GLIPPKEQAG EVDPEHLGRL FVFAMMWSVG AVLELEGRRR MELWLRSREG PTLHLPQLTD
AGDTMFDYYV APNGTWRHWS LCTPEYVYPP DTTPEYGSIL VPNVDNVRTD FLIKTIAKQG
KAVLLIGEQG TAKTVIIKGF MSKFDPESHM VKNLNFSSAT TPVMFQRTIE SYVDKRMGTT
YGPPAGKKMA VFIDDLNMPV INEWGDQVTN EIVRQLMEQS GFYNLEKPGE FTSIVDIQFL
AAMIHPGGGR NDIPQRLKRQ FSIFNCTLPS DASMDKIFGV IGAGYYCAQR GFSEEVQDAL
IKLVPLTRRL WQMTKLKMLP TPAKFHYVFN LRDLSRIWQG MLNITSEVIK DTDELLRLWK
HECKRVIADR FSMSSDVTWF DKAVVSLVEE EFGEEKAPVV DCGVDAYFVD FLRDAPEATG
ETPEEADAEM PKLYEPIASL NHLRERLSVF LQLYNESIRG TGMDMVFFID AMVHLVKISR
VIRTPRGNAL LVGVGGSGKQ SLTRLASFIA GYTSFQITLT RSYNTSNLME DLKVLYRTAG
QQGKGITFIF TDNEIKEESF LEYMNNVLSS GEVSNLFARD EIDEINSDLT PIMKKEHPRR
PPTNDNLYEY FMSRVRGNLH IVLCFSPVGE KFRNRALKFP ALISGCTIDW FSRWPKDALV
AVSEHFLSSY TIDCTAEIKK ELVQCMGSFQ DGVAEKCADY FQRFRRSTHV TPKSYLSFIQ
GYKFIYEEKH MEVQSLANRM NTGLEKLKEA SESVAALSKE LAGKEKELQV ANEKADTVLK
EVTMKAQAAE KVKAEVQKVK DKAQAIVDSI SKDKAIAEEK LEAAKPALEE AEAALQTIKP
SDIATVRTLG RPPHLIMRIM DCVLLLFQRR VNAVKIDVDK GCTMPSWQES LKLMTAGNFL
QNLQQFPKDT INEEVIEFLN PYFEMSDYNI ETAKRVCGNV AGLCSWTKAM ASFFSINKEV
LPLKANLIVQ ENRHILAMQD LQKAQAELDA KQAELDVVQA EYEQAMAEKQ TLLEDADRCR
HKMQTASTLI SGLAGEKERW TEQSKEFAAQ TKRLVGDVLL ATAFLSYSGP FNQEFRDLLL
HDWKKEMKAR KIPFGNGLNL NEMLIDAPTI SEWNLQGLPN DDLSIQNGII VTKASRYPLL
IDPQTQGKIW IKNKESQNEL QITSLNHKYF RNHLEDSLSL GRPLLIEDVG EELDPALDNV
LEKNFIKTGS TFKVKVGDKE VDVMDGFKLY ITTKLPNPAY TPEISARTSI IDFTVTVKGL
EDQLLGRVIL TEKQELEKER THLLEDVTAN KRRMKELEDN LLYRLTSTQG SLVEDESLII
VLSNTKKTAE EVTQKLEISG ETEIQINSAR EEYRPVATRG SILYFLITEM RLVNEMYQTS
LRQFLGLFDL SLARSVKSPI TSKRIANIIE HMTYEVFKYA ARGLYEEHKF LFTLLLTLKI
DIQRNLVKHE EFLTLIKGGA SLDLKACPPK PSKWILDMTW LNLVELSKLK QFSDILDQIS
RNEKMWRVWF DKENPEEEPL PNAYDKSLDC FRRLLLIRSW CPDRTIAQAR KYIMDSMGEN
YAEGVILDLE KTWEESDPRT PLICLLSMGS DPTDSIIALG KRLKIETRYV SMGQGQEVHA
RKLLHQTMAN GGWVLLQNCH LGLDFLDELM DVVTETETVH DTFRLWITTE VHKQFPITLL
QMSIKFANEP PQGLRAGLRR TYGGVSQDLL DVSVGAQWKP MLYAVAFLHS TVQERRKFGP
LGWNIPYEFN QADFNATVQF IQNHLDDMDV KKGVSWTTVR YMIGEIQYGG RVTDDYDKRL
LNTFAKVWFS ENMFGPDFTF YQGYNIPKCS TVDGYLQYIQ SLPAYDSPEV FGLHPNADIT
YQSKLAKDVL DTILGIQPKD SSGGGDETRE AVVARLADDM LEKLPEDYSP FEVKERLQKM
GPFQPMNIFL RQEIDRMQRV LSLVRSTLTE LKLAVDGTII MSENLRDALD CMFDARIPAR
WKKASWVSST LGFWFTELLE RNCQFTSWVS NGRPHCFWMT GFFNPQGFLT AMRQEITRAN
KGWALDNMVL CNEVTKFMKD DISAPPTEGV YVYGLYLEGA GWDKRNMKLI ESKPKVLFEL
MPVIRIFAEN NTARDPRLYC CPIYKKPVRT DLNYIAAVDL KTAQAPEHWV LRGVALLCDV
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