DMD_CAEEL
ID DMD_CAEEL Reviewed; 3674 AA.
AC Q9TW65; Q9TYG9; Q9U3H3;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Dystrophin-1;
GN Name=dys-1; ORFNames=F15D3.1;
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 [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=9933302; DOI=10.1007/s100480050053;
RA Bessou C., Giugia J.-B., Franks C.J., Holden-Dye L., Segalat L.;
RT "Mutations in the Caenorhabditis elegans dystrophin-like gene dys-1 lead to
RT hyperactivity and suggest a link with cholinergic transmission.";
RL Neurogenetics 2:61-72(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 INTERACTION WITH DYB-1 AND STN-1.
RX PubMed=10561496; DOI=10.1016/s0014-5793(99)01421-0;
RA Gieseler K., Abdel-Dayem M., Segalat L.;
RT "In vitro interactions of Caenorhabditis elegans dystrophin with
RT dystrobrevin and syntrophin.";
RL FEBS Lett. 461:59-62(1999).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10369883; DOI=10.1007/s100480050057;
RA Gieseler K., Bessou C., Segalat L.;
RT "Dystrobrevin- and dystrophin-like mutants display similar phenotypes in
RT the nematode Caenorhabditis elegans.";
RL Neurogenetics 2:87-90(1999).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10996789; DOI=10.1016/s0960-9822(00)00691-6;
RA Gieseler K., Grisoni K., Segalat L.;
RT "Genetic suppression of phenotypes arising from mutations in dystrophin-
RT related genes in Caenorhabditis elegans.";
RL Curr. Biol. 10:1092-1097(2000).
RN [6]
RP FUNCTION.
RX PubMed=12234669; DOI=10.1016/s0378-1119(02)00762-x;
RA Grisoni K., Martin E., Gieseler K., Mariol M.-C., Segalat L.;
RT "Genetic evidence for a dystrophin-glycoprotein complex (DGC) in
RT Caenorhabditis elegans.";
RL Gene 294:77-86(2002).
RN [7]
RP FUNCTION, INTERACTION WITH STN-2, AND DISRUPTION PHENOTYPE.
RX PubMed=21242290; DOI=10.1083/jcb.201006109;
RA Zhou S., Chen L.;
RT "Neural integrity is maintained by dystrophin in C. elegans.";
RL J. Cell Biol. 192:349-363(2011).
CC -!- FUNCTION: Plays a role in cholinergic transmission and as a functional
CC partner of dystrobrevin (dyb-1), necessary for muscle maintenance.
CC Required for neuronal positioning. {ECO:0000269|PubMed:10369883,
CC ECO:0000269|PubMed:10996789, ECO:0000269|PubMed:12234669,
CC ECO:0000269|PubMed:21242290, ECO:0000269|PubMed:9933302}.
CC -!- SUBUNIT: Component of the dystrophin glycoprotein complex (DGC).
CC Interacts with dyb-1 and stn-1 to form the DGC. Interacts with stn-2.
CC {ECO:0000269|PubMed:10561496, ECO:0000269|PubMed:21242290}.
CC -!- INTERACTION:
CC Q9TW65; Q9Y048: dyb-1; NbExp=4; IntAct=EBI-446952, EBI-322698;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q9TW65-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9TW65-2; Sequence=VSP_051614, VSP_051615;
CC -!- TISSUE SPECIFICITY: Expressed in body wall, head, pharyngeal and vulval
CC muscles, from late embryogenesis to adulthood (at protein level).
CC {ECO:0000269|PubMed:9933302}.
CC -!- DISRUPTION PHENOTYPE: Mutants display a phenotype of hyperactive
CC locomotion and are hypersensitive to the acetylcholinesterase inhibitor
CC aldicarb and are defective in maintaining neuronal positioning. Dys-1
CC and hlh-1 double mutants synergistically exhibit progressive myopathy.
CC {ECO:0000269|PubMed:10369883, ECO:0000269|PubMed:10996789,
CC ECO:0000269|PubMed:21242290, ECO:0000269|PubMed:9933302}.
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DR EMBL; AJ012469; CAA10033.1; -; mRNA.
DR EMBL; Z81063; CAB61012.2; -; Genomic_DNA.
DR EMBL; Z81522; CAB61012.2; JOINED; Genomic_DNA.
DR EMBL; Z81522; CAB61004.1; -; Genomic_DNA.
DR PIR; T21635; T21635.
DR RefSeq; NP_492946.1; NM_060545.5. [Q9TW65-1]
DR RefSeq; NP_492947.1; NM_060546.6. [Q9TW65-2]
DR SMR; Q9TW65; -.
DR BioGRID; 38445; 6.
DR IntAct; Q9TW65; 3.
DR STRING; 6239.F15D3.1a; -.
DR TCDB; 8.A.66.1.1; the dystrophin (dystrophin) family.
DR iPTMnet; Q9TW65; -.
DR EPD; Q9TW65; -.
DR PaxDb; Q9TW65; -.
DR PeptideAtlas; Q9TW65; -.
DR PRIDE; Q9TW65; -.
DR EnsemblMetazoa; F15D3.1a.1; F15D3.1a.1; WBGene00001131. [Q9TW65-1]
DR EnsemblMetazoa; F15D3.1b.1; F15D3.1b.1; WBGene00001131. [Q9TW65-2]
DR GeneID; 173038; -.
DR UCSC; F15D3.1b; c. elegans. [Q9TW65-1]
DR CTD; 173038; -.
DR WormBase; F15D3.1a; CE27129; WBGene00001131; dys-1. [Q9TW65-1]
DR WormBase; F15D3.1b; CE24904; WBGene00001131; dys-1. [Q9TW65-2]
DR eggNOG; KOG4286; Eukaryota.
DR HOGENOM; CLU_000246_3_0_1; -.
DR InParanoid; Q9TW65; -.
DR OMA; NQRWDAI; -.
DR OrthoDB; 629209at2759; -.
DR PhylomeDB; Q9TW65; -.
DR PRO; PR:Q9TW65; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001131; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9TW65; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016014; C:dystrobrevin complex; IPI:WormBase.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015870; P:acetylcholine transport; IMP:UniProtKB.
DR GO; GO:0043056; P:forward locomotion; IMP:WormBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IMP:WormBase.
DR GO; GO:0045214; P:sarcomere organization; IGI:WormBase.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:UniProtKB.
DR CDD; cd00014; CH; 1.
DR CDD; cd00176; SPEC; 3.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 2.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00150; SPEC; 7.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Cytoskeleton; Membrane; Metal-binding; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..3674
FT /note="Dystrophin-1"
FT /id="PRO_0000076079"
FT DOMAIN 129..234
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 327..435
FT /note="Spectrin 1"
FT REPEAT 436..541
FT /note="Spectrin 2"
FT REPEAT 612..656
FT /note="Spectrin 3"
FT REPEAT 2576..2673
FT /note="Spectrin 4"
FT REPEAT 2725..2789
FT /note="Spectrin 5"
FT REPEAT 2792..2905
FT /note="Spectrin 6"
FT REPEAT 2926..3032
FT /note="Spectrin 7"
FT DOMAIN 3047..3081
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 3301..3357
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..39
FT /note="Actin-binding"
FT REGION 265..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1796..1833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2387..2466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3481..3522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3568..3645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1796..1827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2388..2427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2430..2448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2449..2466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3481..3501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3502..3522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3568..3606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT VAR_SEQ 1..3410
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_051614"
FT VAR_SEQ 3411..3446
FT /note="ADTSQMTAHLAKLSAEHGGGAEHMEPVQSPLQIINQ -> MCSLLKLLKISG
FT KSVSDDDPIERYIKCEQCKCKRHW (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_051615"
SQ SEQUENCE 3674 AA; 417427 MW; 793FD9E5A81008FF CRC64;
MLFSGASTAK PKKDEKKDKK SDRDPKNELQ EWVFVRWANH LLGTERLTDY KSLQDGSNAI
FVYQAIIGQT MAVLGNPSDD WPNVLQNIGD SKTNPQEVME GQQKAVLSAW WQLVQFFWKN
NAPVQLREEK LSEAIKQWCI EVMKSYEEID VYDFTSSFRD GHAFNYLIHS YDRKLINLTK
TAEMSAIDRI ENAFAVAEKT WNVPRLLNPK DLHSDQLDSH SVLCYLMSLY LAMISTSKIE
TELEAQQIQQ QKVAALLASH KMLSSQPSTS SSSALQIPPQ TPPTAHHQAM LDRGKSFEQS
AEGEVRSRKS SSSSQKSGKS KKARREEQLA EFKSCIEQVL TWLLEAEDEL TTLTQMPRVE
LASVRSQFSD FESFMSSLTD SQDTVGRVLL RGQMLSNKSE SEEEKESIGA NLHLVNTRWE
ALREQAMQEQ AVLQQQIHLL QQSELDTISQ WLDAAELEIE SFGPLAADSS QALRQIELHT
KFQQKLNDFQ ETIDKLESFV AVVDEENDAS VATLEDALSA VSVRWGHVCE WAEKRATKLD
GLADLLDKTN EVFENLSGWL AERENELMTG LKSAHHLENE EQVAQQVRRL QKTEEQLEQE
HASFVRLSQL SCELVGRLDD SNGAAANAVR LSLDSITQRW DNLVARIEEH GKTLVKSGKA
DVKQVQESQN EQKEQPASSE GLSTDTEGEE QKNQLVDKFL LHISKLSHEL EPLQDWSEKF
EVSRKKDDIR KMMNTCQEKL IQIKEQEARV NRLQLELEHL HVAKLNARQL KRANDAFEQF
AKGWARIVTK ISEAMNVLTG QEAGGNGNGS EEAAVAAKIE QWIEAVDKVI NELSQLPVNE
RRSRIDKLEQ QLQVQDKNVG FIEKDLLKKA ILKKGLEIAG KRLAALKVEE KPVEKEEQLV
LSNSEEPEAE KHVTFVQETT EKPAPLQEPT SEAQLLEELD GPWSRVGDVV AIEHDLLRAK
RAVDTARNSQ MSNETVEKAE TRKAEMEEKR RVTMSARSKF RMAEETLEEI ERNLDRLQVS
DLEIADLVRG LEQEAAKLGE RVSQRKEAER TAEKILSMDD DEISQEIVIK TKDSTEKLIK
RWNQLELDLE ENLRKAKRDQ DVFIQKRLRE GEEALNEIKT AIEGKRESLD AETAAENLDH
LESSLDNISS LFGEIGSLPM DDNSREKLSK LAKAKDQITA RANEALAALT RTVSECEDFE
KQIMLFQNWS ARIGFLLQAR KSADISAFDI PHEYHEDLGN EAELIPKLSR EFEEWTVKLN
EMNSTATEKD DSARMREQLN HANETMAELK RKFNEFKRPK GFEEKLEKVI TTLSNVEMGL
DDTTGIDGSE CGGALMEVRA LVRMLDGAQE KWKDLAENRE QLVKDRVLDE ETSKETLQKL
QYAKTKSKEL YERSSTCIER LEDCVEMYQR LKMESDEIER FLEEMEGKLD QYAASDRPEE
AEIVNELISE WNRNEAAMKN AEHLQRQLNE RAIKIPDDVL SLKRLRADAL KNRLNSWCRT
IQEMSEDDES ALLEIDELHQ NLEKELKLVS DKEPSKIAEK LRFLRADRDR LSSRTRKLAA
KNPRLAATSS DVLAGLNQKW KELEVKASAE KAPAPELRDA RLSSPSEQPF DKRVQELCDL
FENLEAQLDF NGSPVSMVTE YQKRVENLDE YLDEYRPALD DTIEEGRKIA ETGRLELQTH
SAIEKLDELT NRIEQVEVEL DKHRDKVPSL VEQHEQLKKD IDSFLLVLDV FTDRNLDDVD
IAKSTRKELA ERDSHIVSLT SRATAIHCAL PGKGPQLHDV TLDKLRDRIE KLEARLSATE
KKPVETVKST IPDRPEVPEE PEKSSPDRTS RSSLQLAMEA YGTATEDDSV ISEAVTVGQK
SVDQVDPVEQ LEPVEPVEPK LEVKQLKDEA TEEEEKRTII LPDETEKVIE TIPAARPSAG
PSEGTVAEVS TSEILKARPA QESIERTVRE VPVDEYEETA NISSGDELQD HKISSAVPDS
ESEIASMFEV LDSIEDSHTN FEEFPFDYLD SADDDLKKTL LKLESCEKTL AKNEMTINIA
QAENARERIT MLRQMALQRK DKLPKFNEEW NAMQELIQLA DALVDEAERY ESDQIPQMDR
KSAPNVLGEL RKRVANAEGP VIDLVKKLSQ LVPRMQEDSP KSQDIRQKVY GIEDRFRRVG
QAEGAAISKA LSSALTEPEL KLELDEVVRW CEMAEKEAAQ NVNSLDGDGL EKLDGRLAQF
TKELQERKDD MVQLEMAKNM IIPSLKGDAH HDLRRNFSDT AKRVAMVRDE LSDAHKWVAT
SRDTCDTFWA DIDSLEQLAR DVVRRANGIR MAVIYTPSRE NVEGVLRDVQ RLKMSIGDVK
KRVQTANLPP AIKLAGKNAK RVVQVLTETA TTIADCHDIP TYLIDEMNDS GGDTTESRST
VVEMTSVHTK QSSSSSSNKT PSAGGESDDA HTLNGDDEQS EEDQKIYSRE SSSTLPRGVS
SLGSTGSSGV LDPVAVQLTH TRHWLHDVER DASITVDLAQ WQPARELWQS IQGIIDEIRL
RSVHVTGAHD ASPNRQVRQQ AAQLLTEMRR TIENCEKRCL ILNQISDIAR QNEASRNEME
LWLKSASDVI GERRVEELSE EVVRQELQVL ERVVEQLTER KDKMAEINSQ ANKIVDTYTK
DEAHNLSHLL SRLNMSWTKF NDNIRIRRAV LEASLRSRRD FHSALSEFEK WLSRQEDNCS
KLSADTSNHQ AIKDTSKRKN WTQSFKTLNA ELNAHEDVMK SVEKMGKMLA ESLESGNEKV
ELLKRVGETT RRWTALRKTT NEIGERLEKA EQEWEKLSDG LADLLSWVEA KKQAIMDEQP
TGGSLSAVMQ QASFVKGLQR EIESKTANYK STVEEAHSFL MQHDLRPKLH SPHVLDDDYE
KEELANLEQR RRGLEINANC ERLKKNWAEL GIEVESWDKL VQHAMQRLQE LERNLAECQL
HLTSSENEIE TMKAVEKIHL EDLKIAREET DQISKRIDEV RLFVDDVNDA AARLLAEDLK
LDEHAKGQIE HVNKRYSTLK RAIRIRQAAV RNAASDFGPT SEHFLNQSVT LPWQRAISKS
NLLPYYIEQT SEKTQWEHPV WVEIVKELSQ FNRVKFLAYR TAMKLRALQK RLCLDLVDLT
LLEKAFVRLK GLSAEECPGL EGMVCALLPM YEALHAKYPN QVQSVSLAVD ICINFLLNLF
DQSRDGIMRV LSFKIAMIVF SNIPLEEKYR YLFKLVSQDG HATQKQIALL LYDLIHIPRL
VGESAAFGGT NVEPSVRSCF ETVRLAPTIS EGAFIDWVKK EPQSIVWLAV MHRLVISEST
KHASKCNVCK MFPIIGIRYR CLTCFNCDLC QNCFFSQRTA KSHRTNHPMQ EYCEKTTSSD
DARDFAKMIR NKFRASKRQK GYLPIDVAEE GIPLTCPPAK VTNQATEQMN ADTSQMTAHL
AKLSAEHGGG AEHMEPVQSP LQIINQVEQL QRDEMDQMLH RLQFENKQLR KELEWKRGAA
STMEIDRSSK RHQERHQSES RGGTLPLRNG RSVVSLKSTQ SQNDVMDEAK ALRLHKQRLE
HRSRILEQQN EQLEMQLQRL KKVIDAQKQQ APLSTNSLLR GSHHQPWSPE RARSGSASTL
DRGLIVSSRH QEQAEAAGGG AEDSSDEAGG AGGGPRGSSV GQMQNLMTAC DDLGKAMESL
VVSVVYDSDD EEND
