DYHC_CAEEL
ID DYHC_CAEEL Reviewed; 4568 AA.
AC Q19020;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Dynein heavy chain, cytoplasmic;
DE AltName: Full=Dynein heavy chain, cytosolic;
DE Short=DYHC;
GN Name=dhc-1 {ECO:0000312|WormBase:T21E12.4a};
GN ORFNames=T21E12.4 {ECO:0000312|WormBase:T21E12.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=8674131; DOI=10.1002/cm.970320104;
RA Lye R.J., Wilson R.K., Waterston R.H.;
RT "Genomic structure of a cytoplasmic dynein heavy chain gene from the
RT nematode Caenorhabditis elegans.";
RL Cell Motil. Cytoskeleton 32:26-36(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16996038; DOI=10.1016/j.brainres.2006.08.067;
RA Locke C.J., Williams S.N., Schwarz E.M., Caldwell G.A., Caldwell K.A.;
RT "Genetic interactions among cortical malformation genes that influence
RT susceptibility to convulsions in C. elegans.";
RL Brain Res. 1120:23-34(2006).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF LEU-1398.
RX PubMed=20510931; DOI=10.1016/j.cell.2010.04.011;
RA Ou C.Y., Poon V.Y., Maeder C.I., Watanabe S., Lehrman E.K., Fu A.K.,
RA Park M., Fu W.Y., Jorgensen E.M., Ip N.Y., Shen K.;
RT "Two cyclin-dependent kinase pathways are essential for polarized
RT trafficking of presynaptic components.";
RL Cell 141:846-858(2010).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20005871; DOI=10.1016/j.ydbio.2009.12.004;
RA Fridolfsson H.N., Ly N., Meyerzon M., Starr D.A.;
RT "UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope
RT during nuclear migration.";
RL Dev. Biol. 338:237-250(2010).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=20599902; DOI=10.1016/j.ydbio.2010.06.016;
RA Fortin S.M., Marshall S.L., Jaeger E.C., Greene P.E., Brady L.K.,
RA Isaac R.E., Schrandt J.C., Brooks D.R., Lyczak R.;
RT "The PAM-1 aminopeptidase regulates centrosome positioning to ensure
RT anterior-posterior axis specification in one-cell C. elegans embryos.";
RL Dev. Biol. 344:992-1000(2010).
RN [7]
RP FUNCTION.
RX PubMed=21205795; DOI=10.1242/dev.060939;
RA Aguirre-Chen C., Buelow H.E., Kaprielian Z.;
RT "C. elegans bicd-1, homolog of the Drosophila dynein accessory factor
RT Bicaudal D, regulates the branching of PVD sensory neuron dendrites.";
RL Development 138:507-518(2011).
RN [8]
RP FUNCTION.
RX PubMed=21609829; DOI=10.1016/j.neuron.2011.04.002;
RA Park M., Watanabe S., Poon V.Y., Ou C.Y., Jorgensen E.M., Shen K.;
RT "CYY-1/cyclin Y and CDK-5 differentially regulate synapse elimination and
RT formation for rewiring neural circuits.";
RL Neuron 70:742-757(2011).
RN [9]
RP FUNCTION.
RX PubMed=22699897; DOI=10.1523/jneurosci.0251-12.2012;
RA Goodwin P.R., Sasaki J.M., Juo P.;
RT "Cyclin-dependent kinase 5 regulates the polarized trafficking of
RT neuropeptide-containing dense-core vesicles in Caenorhabditis elegans motor
RT neurons.";
RL J. Neurosci. 32:8158-8172(2012).
RN [10]
RP FUNCTION.
RX PubMed=26483555; DOI=10.1083/jcb.201409035;
RA Bohr T., Nelson C.R., Klee E., Bhalla N.;
RT "Spindle assembly checkpoint proteins regulate and monitor meiotic synapsis
RT in C. elegans.";
RL J. Cell Biol. 211:233-242(2015).
RN [11]
RP FUNCTION.
RX PubMed=27697906; DOI=10.1242/dev.141192;
RA Bone C.R., Chang Y.T., Cain N.E., Murphy S.P., Starr D.A.;
RT "Nuclei migrate through constricted spaces using microtubule motors and
RT actin networks in C. elegans hypodermal cells.";
RL Development 143:4193-4202(2016).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=27864381; DOI=10.1242/dev.140921;
RA Wang X., Olson J.R., Rasoloson D., Ellenbecker M., Bailey J., Voronina E.;
RT "Dynein light chain DLC-1 promotes localization and function of the PUF
RT protein FBF-2 in germline progenitor cells.";
RL Development 143:4643-4653(2016).
CC -!- FUNCTION: Cytoplasmic dynein acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules (By
CC similarity). Dynein has ATPase activity; the force-producing power
CC stroke is thought to occur on release of ADP (By similarity). May play
CC a role in nuclear migration in hypodermal precursor cells
CC (PubMed:20005871, PubMed:27697906). May be involved in the transport of
CC synaptic vesicle components towards the axon of the DA motor neuron
CC (PubMed:20510931). This function may involve the regulation of dynein
CC by pct-1 and/or cdk-5 (PubMed:20510931). Involved in the formation of
CC synapses in the dorsal region during synaptic remodeling of DD motor
CC neurons (PubMed:21609829). Required for anterograde trafficking of
CC dense-core vesicles in the DB motor neuron dendrites (PubMed:22699897).
CC Required for the formation of dendritic branches of PVD sensory neurons
CC (PubMed:21205795). May also play a role in GABAergic synaptic vesicle
CC localization in the ventral nerve cord (PubMed:16996038). May play a
CC role in the pairing of homologous chromosomes during meiosis
CC (PubMed:26483555). {ECO:0000250|UniProtKB:P36022,
CC ECO:0000269|PubMed:16996038, ECO:0000269|PubMed:20005871,
CC ECO:0000269|PubMed:20510931, ECO:0000269|PubMed:21205795,
CC ECO:0000269|PubMed:21609829, ECO:0000269|PubMed:22699897,
CC ECO:0000269|PubMed:26483555, ECO:0000269|PubMed:27697906}.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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 -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown prevents sperm-donated
CC centrosome from leaving the posterior cortex in 1-cell embryos
CC (PubMed:20599902). RNAi-mediated knockdown results in nuclear migration
CC defects in hyp7 hypodermal precursor cells (PubMed:20005871). RNAi-
CC mediated knockdown in a pam-1 mutant background restores anterior-
CC posterior polarity, par-1, par2 and par-6 asymmetric localization and
CC pseudocleavage formation (PubMed:20599902). RNAi-mediated knockdown
CC results in an abnormal distribution of GABAergic synaptic vesicles at
CC synaptic termini of the ventral nerve cord (PubMed:16996038). RNAi-
CC mediated knockdown in combination with exposure to pentylenetetrazole,
CC a GABA antagonist that induces seizures, results in an increased
CC convulsion incidence as compared to wild-type animals
CC (PubMed:16996038). RNAi-mediated knockdown in a fbf-2 loss of function
CC background results in sterility and the formation of small endomitotic
CC oocytes (PubMed:27864381). {ECO:0000269|PubMed:16996038,
CC ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:20599902,
CC ECO:0000269|PubMed:27864381}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; L33260; AAC37251.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD64267.1; -; Genomic_DNA.
DR PIR; D87755; D87755.
DR RefSeq; NP_491363.1; NM_058962.4.
DR SMR; Q19020; -.
DR BioGRID; 37511; 76.
DR STRING; 6239.T21E12.4; -.
DR iPTMnet; Q19020; -.
DR EPD; Q19020; -.
DR PaxDb; Q19020; -.
DR PeptideAtlas; Q19020; -.
DR PRIDE; Q19020; -.
DR EnsemblMetazoa; T21E12.4a.1; T21E12.4a.1; WBGene00000962.
DR GeneID; 172041; -.
DR KEGG; cel:CELE_T21E12.4; -.
DR UCSC; T21E12.4; c. elegans.
DR CTD; 172041; -.
DR WormBase; T21E12.4a; CE23997; WBGene00000962; dhc-1.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000156103; -.
DR HOGENOM; CLU_000038_7_0_1; -.
DR InParanoid; Q19020; -.
DR OMA; FIMDEAN; -.
DR OrthoDB; 26380at2759; -.
DR PhylomeDB; Q19020; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-9646399; Aggrephagy.
DR PRO; PR:Q19020; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000962; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q19020; baseline and differential.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0005819; C:spindle; IDA:WormBase.
DR GO; GO:0000922; C:spindle pole; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
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:1990048; P:anterograde neuronal dense core vesicle transport; IMP:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051296; P:establishment of meiotic spindle orientation; IMP:WormBase.
DR GO; GO:0051293; P:establishment of spindle localization; IMP:CACAO.
DR GO; GO:0051661; P:maintenance of centrosome location; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0072382; P:minus-end-directed vesicle transport along microtubule; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0016322; P:neuron remodeling; IMP:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:1904811; P:positive regulation of dense core granule transport; IMP:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:WormBase.
DR GO; GO:1902473; P:regulation of protein localization to synapse; IMP:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; IMP:WormBase.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IMP:WormBase.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:WormBase.
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; 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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Microtubule;
KW Motor protein; Neurogenesis; Nucleotide-binding; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..4568
FT /note="Dynein heavy chain, cytoplasmic"
FT /id="PRO_0000114634"
FT REGION 1..1826
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1827..2049
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2118..2394
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2498..2747
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2842..3111
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3132..3432
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3496..3725
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3954..4169
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 587..652
FT /evidence="ECO:0000255"
FT COILED 814..844
FT /evidence="ECO:0000255"
FT COILED 1241..1274
FT /evidence="ECO:0000255"
FT COILED 1324..1340
FT /evidence="ECO:0000255"
FT COILED 1559..1591
FT /evidence="ECO:0000255"
FT COILED 3132..3229
FT /evidence="ECO:0000255"
FT COILED 3339..3432
FT /evidence="ECO:0000255"
FT COILED 3707..3739
FT /evidence="ECO:0000255"
FT COILED 4359..4386
FT /evidence="ECO:0000255"
FT BINDING 1865..1872
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2163..2170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2537..2544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2880..2887
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 1398
FT /note="L->F: In wy622; mislocalization of synaptic vesicles
FT to the dendrites is rescued in cdk-5 mutants."
FT /evidence="ECO:0000269|PubMed:20510931"
SQ SEQUENCE 4568 AA; 521579 MW; 028E52684F381676 CRC64;
MDSGNESSII QPPNLKTAAE GDVKEYIVQV VTSHFGLSPR DQTTLDVELT AATTFITDFI
NEADKNVIVV DRVVAREQGD QPAGAESGGE ESAPATFQVH DGLFMTDRGQ AMMFVKQSNV
IEAEKKIATQ VSAFPLNGGS AWEQLHFLMS RLLNPYCKSF IGQSGRGERD GDKLAPTVQK
CFTEAEAALL HLQQNIDIPE INLVVNQHIL DAIEQAGKEN RRAKIEDLGD LVEDANFLNA
LQSGCNRWVK EIRKVTQLER DPSSGTSLQE MTFWLNLERA LLKISQKRDG EEVTLTLEAL
KCGKRFHATV GFDSDNGLKQ KLAVVQDYNT LMKEFPLSEL VSATDVPKLM HAVVGIFLHL
RKLRSTKYPL QRALRLVEAI SRDLNSQLLK VLSSYNLMRT PIAEFNEIMS QCQALFSKWD
DEYDKFIALL RDINKKKRDD PSKLSWKVTA VHKRLETRLM QILQFRKQHE QFRTVIERVL
RPVGNGSRER EQLMIDSSEG EKSPDEQVDI AYEFLKNVDF LDVDSPAWEN AFKRYEDQIG
VVETAITTRL KSQLESSRNS NEMFSIFSRY NALFIRPRIR GAIYEYQTRL INRVKEDINE
LQARFTKARG EQGVKIMQTV GLPPFSAKIM WIRNYERQLQ RYMKRVEDVL GKQWENHVDG
RQLKADGDNF KVKLNTQPMF DEWVESVQSQ NWTLPNKILT VDRVQVDGRM QLQLKINYHS
DSSVLYKEVS HLKSMGFRVP LKIVNWAHQA NQMRPSATSL IEAARTFASV NAALASVQGV
DSLLASYKKD IQNQLIEGAT LGWDSYKVDQ YQLKLAETVN TYQERCEELL NVVRIVNADL
NVLKSCRYDK ETIENLLTSI QKGVDQLSLG NYSNLAQWVN TLDRQIETIL ARRVEDAIRV
WTLVFSQSEE VEELRERQVV LPTVKNVVVD LCMTAQTLYI SPSTRETREK ILEQLYEWHS
VCTAQMRISG KRFQMVMNEE IEPETYHNIL NVMPEGQACL EKAYDCVNGI MSDLEEYLSE
WLSYQSLWVL QAEQLFEMLG TSLSKWMKTL MEIRKGRLVF DTQDTRKVIF PVSVEYGKAQ
QKILFKYDYW HKEMLVKFGA VVGDEMQKFF NSVSKWRNVL ETQSVDGGST SDTIGLISFV
QSLKKQTKSG QDAVDLYRSS QRLLNQQRYQ FPAQWLYSEN VEGEWSAFTE ILSLRDASIQ
TQMMNLQTKF AQEDELVEKR TVETLTEWNK SKPVEGAQRP QEALNVITAF EAKLNKLTEE
RNKMRKARVA LDLSDSAHAP SEGDKLTVAT EELAAMKDVW KALQPVYTGI DEAKEKTWLS
VQPRKIRQSL DELMNQLKQL PVKCRTYKSY EHVKQMLHTY GKMNMLVAEL KSEALKERHW
HQMMKEMRVN WNLSDLTLGQ VWDADILRHE HTIKKILLVA QGEMALEEFL REMREYWQNY
EVELVNYQNK TRLIKGWDDL FNKLKEHQNS LSAMKLSPYY KQFEESAQSW DEKLNKINAM
FDVWIDVQRR WVYLEGLFSG SAEISTLLPF ESSRFATITT DVLALMKKVA ASPRILDVVN
MQGAQRLLER LADMLAKIQK ALGEYLERER SSFPRFYFVG DEDLLEIMGN SKDITRIQKH
LKKMFAGITA IDINEEDRSI TAFHSREGEK VDLVKIVSTK DVRINDWLQA LEAEMKHTLA
RQLAASLTHF SKMNIQTMTT DDYVEWLDKF PAQVITLTAE IWWCDEMEKT LADGKGAENV
EQAVVKTLEL LADSVLKEQP PIRRKKMEAL ITELVHKRDT CRKLVSMKIR AANDFGWLQC
MRFYFDPKQV DPVRCCVVKM ANSQFFYGFE YLGIQERLVR TPLTDRCYLT MTQALHSRLG
GSPFGPAGTG KTESVKALGH QLGRFVLVFN CDETFDFQAM GRILVGLCQV GAWGCFDEFN
RLEERMLSAV SQQIQTIQEA VRAGGDMSVD LVGKRLNVNS NIGIFITMNP GYSGRSNLPD
NLKQLFRSLA MTQPDRQLIA QVMLFSQGFR TAETLANKIV PLFILCKEQL SDQCHYDFGL
RALKYVLVSA GNIKRDKLDK MGSAALEDVA EQQMLIQSVC ETLVPKLVNE DIALLFSLLS
DVFPGIHYTA NQMRELRQQL STVCDEHLLI YSDVQGEMGS MWLDKVLQLY QITNLNHGLM
LVGSSGSGKT MAWKVLLKAL ERWENVEGVA HVIDAKAMSK DSLYGVMDPN TREWTDGLFT
SVIRKIIDNV RGEADRRQWI IFDGDVDPEW VENLNSVLDD NKLLTLPNGE RLSIPPNVRI
IFEVADLKYA TLATVSRCGM VWFSEEVVTS EMLFERYLSI IRRVPLDSDS AISFSSSSAP
VNLIGEDAKP TRSIEIQRTA ALALQTHFSP DGIVPGSLKY AVSELEHIMP PTPQRLLSSF
FSMMSYSIRK IVSHDEGLID DSVEIDQIQS FVLRSMLTNL VWAFSGDGKW KSREMMSDFI
RQATTISLPP NQQACLIDYE VQLSGDWQPW LSKVPTMEIE SHRVAAADLV VPTIDTVRHE
MLLAAWLAEH KPLVLCGPPG SGKTMTLLAA LRSQQEMEVV NVNFSSSTTP ELLLRTFDHY
CEYRRTPNGV VLAPVQLSQW LVIFCDEINL PAPDKYGTQR VISFLRQLVE LNGFYRTSDH
SWVSLERIQF VGACNPPTDP GRHPMTSRFL RHVPIVYVDY PGQTSLQQIY GTFNRAMLKM
TPAVRGLADQ LTNAMVDVYL ASQEHFTQDD QPHYVYSPRE LTRWVRGISE AITPLESLSA
EQLVRLWAHE AIRLFQDRLV TEEEREWTDK LVDTTAERYF GNACRLDEAL KRPLLYSCWL
SRNYVPVTRE ELQDYVSARL KGFYEEELDV KLVLFDQMLD HVLRIDRIYR QSQGHLLLIG
TAGAGKTTLS RFVAWLNGLS VFQLKVHSKY TAADFDEDMR TVLRRAGCRN EKLCFIMDES
NMLDTGFLER LNTLLANGEV PGLFEGDEHT TLMTQIKEGA QRQGLILDSH DELYKWFTQQ
VMRNLHVVFT MNPSGSGLRE RASTSPALFN RCVLNWFGDW SENALYQVGS ELTRTMDLDR
TDYEGSVRLT PSCELVPSQP TYRDAVVNTL CLVHKTVQKF NEMETKKGHR VMACTPRHFL
DFIKQFMSLF HEKRSDLEEE KIHLNIGLNK ISETEEQVKE LQKSLKLKSN ELQEKKEAAN
LKLKEMLGDQ QKAEEEKKFS EQLQKELAEQ LKQMAEKKTF VENDLAQVEP AVAEAQTAVQ
GIKKSQLVEV KSMSSPPVTV KLTLEAICIL LGENVGTDWK AIRQVMMKDD FMTRILQFDT
ELLTPEILKQ MEKYIQNPDW EFDKVNRASV ACGPMVKWAR AQLLYSTMLH KVEPLRNELK
RLEQEAAKKT QEGKVVDVRI TELEESIGKY KEEYAQLIGQ AENIKQDLLS VQEKVNRSTE
LLSSLRSERD RWSSGSAGFS QQMDSLVGDA LLSSAFLAYA GYYDQMLRDE IFHKWFNHVV
NAGLHFRHDL ARIEYLSTVD DRLQWQLNSL PVDDLCTENA IMLHRFNRYP LIIDPSGQAV
EYIMKQFAGK NIQKTSFLDE SFRKNLESAL RFGNSLLVQD VEAYDPILNP VLNREVKRAG
GRVLITIGDQ DIDLSPSFQI FMITRDSTVE FSPDICSRVT FVNFTVTSSS LASQCLNQVL
RSERPDVDKK RNDLLKLQGE FAVRLRHLEK ALLAALNESK GKILDDNSVI ETLEKLKNEA
AEVAQKSAET DKVMAEVDAV SAQYQRLSTA CSHIYHTLQQ LNEIHFLYHY SLDFLVEIFT
HVLKTPELSS TTDYAKRLRI ITTSLFQTVF RRVSRGMLHT DKVLLALLLM RIHIRSNPSA
PAYEQHFDLL LGRSDFVAKN DEADSTIPGG LDFLTVENKK SIAKARKVVG FENVFAHLQH
NSAAVTSWLT NDNPESNVPV VWDDADGKLS PLCIAMNSLI VVHALRPDRL MASAHRVVST
AFDDHFMQQD KVVDILSIVD NEVSPSEPVL LCSATGYDAS GKIEDLAVET NRQLTSIAIG
SAEGFNQADS ALGTATKSGR WVLLKNVHLA PSWLAQLEKR LHSMKPHAQF RLFLTAEIHP
KLPSSILRAS RVVVFEPATG LKANLLRSLS SIPPQRLTKA PTERSRLYLL VCWLHALVQE
RLRYTPLGWS TAYEFSDADL RVACDTLDAA VDAVAQGRPN VEPERLPWTT LRTLLSQCIY
GGKIDNQFDQ VLLDCVLENL FTAKSFEQDH VLIPKYDGDD SLFTPNMSKK DQMIGWVEEL
KNEQLPAWLG LPNNAEKVLL TKRGESMLRN MLKVTDEELA FNEDGKEEVK PQWMAQLGEL
AKQWLQLLPK EIVKMRRTVE NIKDPLFRFF EREVNLGSQL LKDIRRDLNE ISAVCRAEKK
QNNETRALAA SLQKGEVPTG WKRYTVPREV TVMDWMTDLN ERLKQLIRIG GADNLKRETF
WLGGTFSPEA YITATRQQVA QANTWSLEQL NLHIHIGRTD STDVFRISGI DIRGAKSVGG
NKLELCELVK SECDIVEFSW KQDVADGTRL PLYLYGDRRQ LISPLAFHLS SATVFYQRGV
ALVANSTL
