DYHC_DROME
ID DYHC_DROME Reviewed; 4639 AA.
AC P37276; Q8IRA5; Q961M8; Q9VZ83;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Dynein heavy chain, cytoplasmic;
DE AltName: Full=Dynein heavy chain, cytosolic;
DE Short=DYHC;
GN Name=Dhc64C; Synonyms=cDhc; ORFNames=CG7507;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Embryo;
RX PubMed=8089180; DOI=10.1083/jcb.126.6.1475;
RA Li M., McGrail M., Serr M., Hays T.S.;
RT "Drosophila cytoplasmic dynein, a microtubule motor that is asymmetrically
RT localized in the oocyte.";
RL J. Cell Biol. 126:1475-1494(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1877-1998.
RX PubMed=8186464; DOI=10.1091/mbc.5.1.45;
RA Rasmusson K., Serr M., Gepner J., Gibbons I., Hays T.S.;
RT "A family of dynein genes in Drosophila melanogaster.";
RL Mol. Biol. Cell 5:45-55(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3758-4639 (ISOFORMS A/C).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Cytoplasmic dynein acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules.
CC Dynein has ATPase activity; the force-producing power stroke is thought
CC to occur on release of ADP.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P37276-1; Sequence=Displayed;
CC Name=C;
CC IsoId=P37276-2; Sequence=VSP_012085;
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 -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK92925.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L23195; AAA60323.1; -; mRNA.
DR EMBL; AE014296; AAF47942.3; -; Genomic_DNA.
DR EMBL; AE014296; AAN11615.2; -; Genomic_DNA.
DR EMBL; L25122; AAA28492.1; -; mRNA.
DR EMBL; AY051501; AAK92925.1; ALT_INIT; mRNA.
DR PIR; A54794; A54794.
DR RefSeq; NP_523929.2; NM_079205.4. [P37276-1]
DR RefSeq; NP_729034.2; NM_168103.3. [P37276-2]
DR SMR; P37276; -.
DR BioGRID; 64049; 39.
DR DIP; DIP-59317N; -.
DR IntAct; P37276; 5.
DR STRING; 7227.FBpp0304991; -.
DR PaxDb; P37276; -.
DR PRIDE; P37276; -.
DR EnsemblMetazoa; FBtr0073359; FBpp0073215; FBgn0261797. [P37276-1]
DR EnsemblMetazoa; FBtr0273370; FBpp0271878; FBgn0261797. [P37276-2]
DR GeneID; 38580; -.
DR KEGG; dme:Dmel_CG7507; -.
DR CTD; 38580; -.
DR FlyBase; FBgn0261797; Dhc64C.
DR VEuPathDB; VectorBase:FBgn0261797; -.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000156103; -.
DR InParanoid; P37276; -.
DR PhylomeDB; P37276; -.
DR Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-9646399; Aggrephagy.
DR BioGRID-ORCS; 38580; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38580; -.
DR PRO; PR:P37276; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0261797; Expressed in eye disc (Drosophila) and 25 other tissues.
DR ExpressionAtlas; P37276; baseline and differential.
DR Genevisible; P37276; DM.
DR GO; GO:1904115; C:axon cytoplasm; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:FlyBase.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; IPI:FlyBase.
DR GO; GO:0045169; C:fusome; TAS:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:0005875; C:microtubule associated complex; IDA:FlyBase.
DR GO; GO:0061803; C:posterior cell cortex; IDA:FlyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045505; F:dynein intermediate chain binding; ISS:FlyBase.
DR GO; GO:0051959; F:dynein light intermediate chain binding; ISS:FlyBase.
DR GO; GO:0003777; F:microtubule motor activity; IDA:FlyBase.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; ISS:FlyBase.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
DR GO; GO:0040003; P:chitin-based cuticle development; IGI:FlyBase.
DR GO; GO:0007282; P:cystoblast division; IMP:FlyBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IDA:FlyBase.
DR GO; GO:0051683; P:establishment of Golgi localization; IMP:FlyBase.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; TAS:FlyBase.
DR GO; GO:0051293; P:establishment of spindle localization; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:FlyBase.
DR GO; GO:0045478; P:fusome organization; TAS:FlyBase.
DR GO; GO:0048134; P:germ-line cyst formation; TAS:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR GO; GO:0008298; P:intracellular mRNA localization; TAS:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IMP:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IMP:UniProtKB.
DR GO; GO:0051237; P:maintenance of RNA location; IDA:FlyBase.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IDA:FlyBase.
DR GO; GO:0072382; P:minus-end-directed vesicle transport along microtubule; IBA:GO_Central.
DR GO; GO:0048311; P:mitochondrion distribution; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0007312; P:oocyte nucleus migration involved in oocyte dorsal/ventral axis specification; TAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0030723; P:ovarian fusome organization; IMP:FlyBase.
DR GO; GO:0007279; P:pole cell formation; IMP:FlyBase.
DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IMP:FlyBase.
DR GO; GO:1904801; P:positive regulation of neuron remodeling; IMP:FlyBase.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:FlyBase.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IMP:FlyBase.
DR GO; GO:0008090; P:retrograde axonal transport; IMP:FlyBase.
DR GO; GO:0098958; P:retrograde axonal transport of mitochondrion; IMP:FlyBase.
DR GO; GO:0050658; P:RNA transport; IMP:FlyBase.
DR GO; GO:0007051; P:spindle organization; IMP:FlyBase.
DR GO; GO:0034063; P:stress granule assembly; IMP:BHF-UCL.
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; 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; 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; 4.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Dynein; Microtubule; Motor protein; Nucleotide-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..4639
FT /note="Dynein heavy chain, cytoplasmic"
FT /id="PRO_0000114636"
FT REGION 1..1856
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1857..2084
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2166..2437
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2541..2790
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2884..3153
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3189..3478
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3539..3768
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3989..4205
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 530..565
FT /evidence="ECO:0000255"
FT COILED 774..794
FT /evidence="ECO:0000255"
FT COILED 1264..1368
FT /evidence="ECO:0000255"
FT COILED 3189..3261
FT /evidence="ECO:0000255"
FT COILED 3382..3478
FT /evidence="ECO:0000255"
FT COILED 3723..3782
FT /evidence="ECO:0000255"
FT BINDING 1895..1902
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2210..2217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2580..2587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2922..2929
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 3282..3344
FT /note="KSIRKQQLVEVRTMANPPSVVKLALESICLLLGENATDWKSIRAVIMRENFI
FT NSIVSNFGTEN -> SSIKKKHLAEVRSMANPPAVVKLALESVCELLNESATDWKAIRG
FT ILVKDSFISSIVNLETDK (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_012085"
FT CONFLICT 151
FT /note="A -> V (in Ref. 1; AAA60323)"
FT /evidence="ECO:0000305"
FT CONFLICT 2010
FT /note="R -> H (in Ref. 1; AAA60323)"
FT /evidence="ECO:0000305"
FT CONFLICT 2348
FT /note="V -> A (in Ref. 1; AAA60323)"
FT /evidence="ECO:0000305"
FT CONFLICT 2370
FT /note="S -> T (in Ref. 1; AAA60323)"
FT /evidence="ECO:0000305"
FT CONFLICT 2549
FT /note="S -> T (in Ref. 1; AAA60323)"
FT /evidence="ECO:0000305"
FT CONFLICT 3864
FT /note="I -> N (in Ref. 1; AAA60323)"
FT /evidence="ECO:0000305"
FT CONFLICT 4073
FT /note="K -> N (in Ref. 5; AAK92925)"
FT /evidence="ECO:0000305"
FT CONFLICT 4369
FT /note="T -> A (in Ref. 1; AAA60323)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4639 AA; 530184 MW; 2A3D4F1F8BE52096 CRC64;
MGDSLENPDT SVDPIVNLSI ANYDAFANYL RKAVTILLPE DDVVPASLND ALDDPVNQDT
IRKFLSDPQV QALYVQRNCI KEDDSEQPAE GEDEKEQVTY QISNDVHFTN SRMASLACIK
RGLVVEADKS IHSQLRLINF SDGSPYETLH AFISKSLAPY FKSYVKESGR ADRDGDKMAP
SVEKKLAELE MGLLHLQQNI DIPEITLTAH QTVNNVIRKC AEENRKAKVA DFGDKVEDSS
FLNLLQNGVN RWIAEIKKVT KLNRDPGSGT ALQEISFWLN LERALYRIQE KRESPEVALT
LDILKHGKRF HATVSFDTDT GLKQALATVA DYNPLMKDFP INDLLSATEL EKIRPAVQQI
FAHLRKVRNT KYPIQRCLKL IEAISRDLSQ QLLKVLGTRR LMHIPFDEFE RVMNQCFEIF
SCWDDEYDKL QGLLRDIVKK KRDEHLKMVW RVSPAHKKLQ TRMEHMRKFR RQHEQLRTVI
LRVLRPTKPA VGDDGNVVET KQPYSLDAAD ANAIEEVNLA YENVKEVDCL DITKEGSEAW
EAAVKRYEEK IDRVETRITA HLRDQLGTAK NANEMFRIFS RFNALFVRPH IRGAIREYQT
QLIQRVKDDI EALHEKFKVQ YPQSKSCRLS SVRDLPPVAG SIIWARQIDN QLTMYLKRVE
DVLGKGWETH IEGQKLKADG DSFRAKLSIS DVFHEWARKV QERNFGSTGR IFTIESTRSR
IGRGNVLRLR VNFLPEIITL AKEVRNIKNL GFRVPLTIVN KAHQANQIYP YAISLIESVR
TYERTLEKIE DRASIVPLVA GLRKDVLNLV SEGIGLIWES YKLDPYVIRL SECVTQFQEK
VDDLLVVEEQ LDVDVRSLET CPYSAATFVE ILSKIQHAVD DLSLRQYSNL SVWVTRLDEE
VEKKLALRLQ AGIQAWTEAL TGNKKEVDTS MDTDAPAQPT HKLGGDPQIQ NAVHEIRITN
QQMYLYPSIE EARFQIMQQF FAWQAIVTSQ VRLQSTRYQV GLEKHVSQTY RNLLTKLPEG
KILENAYGAI EQKVSEVRNY VDEWLRYQSL WDLQADMLYG RLGEDVNLWI KCLNDIKQSR
TTFDTSDTRR AYGPIIIDYA KVQAKVTLKY DSWHKEALGK FGTLLGTEMT SFHSKVSKSR
TDLEMQSIEA ASTSDAVSFI TYVQSLKKDM IAWDKQVEVF REAQRILERQ RFQFPNTWLH
VDNIEGEWSA FNEIIKRKDT AIQTQVASLQ AKIVAEDKAV ETRTVDFLND WEKTKPTGGK
IRPDDALQQL QIFESKYSRL KEERDNVVKA KEALELQESA VPNNSAERMN VALEELQDLR
GVWSELSKVW TQIDETREKP WLSVQPRKLR QQLEAMMAQL KELPARLRMY ESYEYVKKLI
QSYIKVNMLI VELKSDALKE RHWKQLTKQL RVNWVLSDLS LGQVWDVNLQ KNEGIVKDII
LVAQGEMALE EFLKQVRESW QNYELDLINY QNKCRIIRGW DDLFNKVKEH INSVAAMKLS
PYYKVFEEEA LTWEEKLNRI NALFDVWIDV QRRWVYLEGI FSGSADIKTL LPVETSRFQS
ISSEFLGLMK KVTKSPKVMD VLNIPAVQRS LERLADLLGK IQKALGEYLE RERTSFPRFY
FVGDEDLLEI IGNSKNIARL QKHFKKMFAG VAAILLNEEN NVILGISSRE GEEVHFMNPV
STVEHPKINE WLSLVEKQMR FTLASLLAQA VQDIKQFRDG KIDPQAYMEW CDKYQAQIVV
LAAQILWSED VESALQQASE NNQSKPMQRV LGNVESTLNV LADSVLQEQP PLRRRKLEHL
INEFVHKRTV TRRLLNNGVT SPKSFQWLCE MRFYFDPRQT EVLQQLTIHM ANARFFYGFE
YLGVQDRLVQ TPLTDRCYLT MTQALESRLG GSPFGPAGTG KTESVKALGN QLGRFVLVFN
CDETFDFQAM GRIFVGLCQV GAWGCFDEFN RLEERMLSAC SQQIQTIQEA LKYEMDSNKE
SITVELVGKQ VRVSPDMAIF ITMNPGYAGR SNLPDNLKKL FRSLAMTTPD RQLIAEVMLF
SQGFRSAEKL ACKIVPFFKL CDEQLSNQSH YDFGLRALKS VLISAGNVKR DRIMKIKEQM
KQRGDENIDE ASVAENLPEQ EILIQSVCET MVPKLVAEDI PLLFSLLSDV FPNVGYTRAE
MKGLKEEIRK VCQEDYLVCG EGDEQGAAWM EKVLQLYQIS NLNHGLMMVG PSGSGKSTAW
KTLLKALERF EGVEGVAHVI DPKAISKEAL YGVLDPNTRE WTDGLFTHIL RKIIDNVRGE
INKRQWIIFD GDVDPEWVEN LNSVLDDNKL LTLPNGERLS LPPNVRVMFE VQDLKFATLA
TVSRCGMVWF SEDVLSTEMI FENYLSRLRS IPLEDGDEDF VGVIKPAKDK EEEVSPSLQV
QRDIALLLLP FFSADGIVVR TLEYAMDQEH IMDFTRLRAL SSLFSMLNQA ARNVLTFNAQ
HPDFPCSADQ LEHYIPKALV YSVLWSFAGD AKLKVRIDLG DFVRSVTTVP LPGAAGAPII
DYEVNMSGDW VPWSNKVPVI EVETHKVASP DIVVPTLDTV RHESLLYTWL AEHKPLVLCG
PPGSGKTMTL FSALRALPDM EVVGLNFSSA TTPELLLKTF DHYCEYRKTP NGVVLSPVQI
GKWLVLFCDE INLPDMDSYG TQRVISFLRQ LVEHKGFYRA SDQAWVSLER IQFVGACNPP
TDPGRKPLSH RFLRHVPIIY VDYPGETSLK QIYGTFSRAM LRLMPALRGY AEPLTNAMVE
FYLASQDRFT QDMQPHYVYS PREMTRWVRG ICEAIRPLDS LPVEGLVRLW AHEALRLFQD
RLVDDSERRW TNENIDLVGQ KHFPGINQEE ALQRPILYSN WLSKDYMPVN REELREYVHA
RLKVFYEEEL DVPLVLFDEV LDHVLRIDRI FRQPQGHLLL IGVSGAGKTT LSRFVAWMNG
LSIFQIKVHN KYTSEDFDED LRCVLRRSGC KDEKIAFILD ESNVLDSGFL ERMNTLLANG
EVPGLFEGDE YTTLMTQCKE GAQREGLMLD SSDELYKWFT QQVMRNLHVV FTMNPSTDGL
KDRAATSPAL FNRCVLNWFG DWSDSALFQV GKEFTTRVDL EKPNWHAPDF FPSVCPLVPA
NPTHRDAVIN SCVYVHQTLH QANARLAKRG GRTMAVTPRH YLDFIHHFVK LYNEKRSDLE
EQQLHLNVGL NKIAETVEQV EEMQKSLAVK KQELQAKNEA ANAKLKQMFQ DQQEAEKKKI
QSQEIQIRLA DQTVKIEEKR KYVMADLAQV EPAVIDAQAA VKSIRKQQLV EVRTMANPPS
VVKLALESIC LLLGENATDW KSIRAVIMRE NFINSIVSNF GTENITDDVR EKMKSKYLSN
PDYNFEKVNR ASMACGPMVK WAIAQIEYAD MLKRVEPLRE ELRSLEEQAD VNLASAKETK
DLVEQLERSI AAYKEEYAQL ISQAQAIKTD LENVQAKVDR SIALLKSLNI ERERWESTSE
TFKSQMSTII GDVLLSAAFI AYGGYFDQHY RLNLFTTWSQ HLQAASIQYR ADIARTEYLS
NPDERLRWQA NALPTDDLCT ENAIMLKRFN RYPLIIDPSG QATTFLLNEY AGKKITKTSF
LDDSFRKNLE SALRFGNPLL VQDVENYDPI LNPVLNRELR RTGGRVLITL GDQDIDLSPS
FVIFLSTRDP TVEFPPDICS RVTFVNFTVT RSSLQSQCLN QVLKAERPDI DEKRSDLLKL
QGEFRLRLRQ LEKSLLQALN DAKGKILDDD SVITTLETLK KEAYDINQKV DETDKVIAEI
ETVSQQYLPL SVACSNIYFT MDSLNQVHFL YQYSLKMFLD IFSTVLYNNP KLEGRTDHSE
RLGIVTRDLF QVCYERVARG MIHIDRLTFA LLMCKIHLKG TSESNLDAEF NFFLRSREGL
LANPTPVEGL SAEQIESVNR LALRLPIFRK LLEKVRSIPE LGAWLQQSSP EQVVPQLWDE
SKALSPIASS VHQLLLIQAF RPDRVIAAAH NVVNTVLGED FMPNAEQELD FTSVVDKQLN
CNTPALLCSV PGFDASGRVD DLAAEQNKQI SSIAIGSAEG FNQAERAINM ACKTGRWVLL
KNVHLAPQWL VQLEKKMHSL QPHSGFRLFL TMEINPKVPV NLLRAGRIFV FEPPPGIRAN
LLRTFSTVPA ARMMKTPSER ARLYFLLAWF HAIVQERLRY VPLGWAKKYE FNESDLRVAC
DTLDTWIDTT AMGRTNLPPE KVPWDALVTL LSQSIYGGKI DNDFDQRLLT SFLKKLFTAR
SFEADFALVA NVDGASGGLR HITMPDGTRR DHFLKWIENL TDRQTPSWLG LPNNAEKVLL
TTRGTDLVSK LLKMQQLEDD DELAYSVEDQ SEQSAVGRGE DGRPSWMKTL HNSATAWLEL
LPKNLQVLKR TVENIKDPLY RYFEREVTSG SRLLQTVILD LQDVVLICQG EKKQTNHHRS
MLSELVRGII PKGWKRYTVP AGCTVIQWIT DFSNRVQQLQ KVSQLVSQAG AKELQGFPVW
LGGLLNPEAY ITATRQCVAQ ANSWSLEELA LDVTITDAGL KNDQKDCCFG VTGLKLQGAQ
CKNNELLLAS TIMMDLPVTI LKWIKISSEP RISKLTLPVY LNSTRTELLF TVDLAVAAGQ
ESHSFYERGV AVLTSTALN
