PEO1_DROME
ID PEO1_DROME Reviewed; 613 AA.
AC Q9VL76; Q8MZH0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Mitochondrial DNA helicase {ECO:0000312|FlyBase:FBgn0032154};
DE AltName: Full=Twinkle mtDNA helicase {ECO:0000305};
DE AltName: Full=Twinkle protein, mitochondrial {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q96RR1};
DE Flags: Precursor;
GN Name=mtDNA-helicase {ECO:0000312|FlyBase:FBgn0032154};
GN Synonyms=Twinkle {ECO:0000303|PubMed:17272269,
GN ECO:0000312|FlyBase:FBgn0032154};
GN ORFNames=CG5924 {ECO:0000312|FlyBase:FBgn0032154};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAM27521.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM27521.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM27521.1};
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).
RN [4] {ECO:0000305}
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ALA-326;
RP ILE-334; ARG-341; LYS-388; TRP-441; ALA-442 AND ASP-483.
RX PubMed=17272269; DOI=10.1074/jbc.m610550200;
RA Matsushima Y., Kaguni L.S.;
RT "Differential phenotypes of active site and human autosomal dominant
RT progressive external ophthalmoplegia mutations in Drosophila mitochondrial
RT DNA helicase expressed in Schneider cells.";
RL J. Biol. Chem. 282:9436-9444(2007).
RN [5] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF CYS-63; CYS-68; CYS-71; LYS-193; ASP-232;
RP PHE-267; TRP-273; ASP-277; TRP-282; ARG-301 AND PRO-302.
RX PubMed=19063859; DOI=10.1016/j.bbabio.2008.11.005;
RA Matsushima Y., Kaguni L.S.;
RT "Functional importance of the conserved N-terminal domain of the
RT mitochondrial replicative DNA helicase.";
RL Biochim. Biophys. Acta 1787:290-295(2009).
RN [6] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF LYS-388; TRP-441 AND ALA-442.
RX PubMed=22952820; DOI=10.1371/journal.pone.0043954;
RA Sanchez-Martinez A., Calleja M., Peralta S., Matsushima Y.,
RA Hernandez-Sierra R., Whitworth A.J., Kaguni L.S., Garesse R.;
RT "Modeling pathogenic mutations of human twinkle in Drosophila suggests an
RT apoptosis role in response to mitochondrial defects.";
RL PLoS ONE 7:e43954-e43954(2012).
RN [7] {ECO:0000305}
RP COFACTOR, DOMAIN, AND MUTAGENESIS OF CYS-63; CYS-68; CYS-71; CYS-102;
RP CYS-105; CYS-245; CYS-248; CYS-260 AND CYS-297.
RX PubMed=25023283; DOI=10.1074/jbc.m114.587774;
RA Stiban J., Farnum G.A., Hovde S.L., Kaguni L.S.;
RT "The N-terminal domain of the Drosophila mitochondrial replicative DNA
RT helicase contains an iron-sulfur cluster and binds DNA.";
RL J. Biol. Chem. 289:24032-24042(2014).
CC -!- FUNCTION: Mitochondrial helicase involved in mtDNA replication
CC (PubMed:17272269, PubMed:19063859, PubMed:22952820, PubMed:25023283).
CC Might have a role in mtDNA repair (By similarity). Has DNA strand
CC separation activity needed to form a processive replication fork for
CC leading strand synthesis which is catalyzed by the formation of a
CC replisome complex with POLG and mtSDB (By similarity). Preferentially
CC unwinds DNA substrates with pre-existing 5'-and 3'- single-stranded
CC tails but is also active on a 5'- flap substrate (By similarity). Can
CC dissociate the invading strand of immobile or mobile D-loop DNA
CC structures irrespective of the single strand polarity of the third
CC strand (By similarity). In addition to its DNA strand separation
CC activity, also has DNA strand annealing, DNA strand-exchange and DNA
CC branch migration activities (By similarity).
CC {ECO:0000250|UniProtKB:Q96RR1, ECO:0000269|PubMed:17272269,
CC ECO:0000269|PubMed:19063859, ECO:0000269|PubMed:22952820,
CC ECO:0000269|PubMed:25023283}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q96RR1};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:25023283};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:25023283};
CC -!- SUBUNIT: Homohexamer (via C-terminus) which assembled in a ring-like
CC structure. Homoheptamer which assembled in a ring-like structure.
CC Oligomerization is Mg(2+), nucleotide and DNA-independent, however,
CC Mg(2+) and nucleotide stabilize the homohexameric form.
CC {ECO:0000250|UniProtKB:Q96RR1}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17272269}.
CC Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000250|UniProtKB:Q96RR1}. Note=Colocalizes with mtDNA in
CC mitochondrial nucleoids, a nucleoproteins complex consisting of a
CC number of copies of proteins associated with mtDNA, probably involved
CC in mtDNA maintenance and expression. {ECO:0000250|UniProtKB:Q96RR1}.
CC -!- DOMAIN: N-terminus enhances protein stability and hexamer formation,
CC which is important for DNA binding, and is required for DNA helicase
CC activity and, ultimately, for mtDNA replisome processivity.
CC {ECO:0000250|UniProtKB:Q96RR1}.
CC -!- CAUTION: The N-terminus contains a putative primase-like domain;
CC however the absence of the zinc binding domain and other motifs
CC important for catalysis suggests that mtDNA-helicase lacks primase
CC activity. {ECO:0000305|PubMed:19063859}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM27521.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF52820.1; -; Genomic_DNA.
DR EMBL; AY102692; AAM27521.1; ALT_INIT; mRNA.
DR RefSeq; NP_609318.1; NM_135474.3.
DR AlphaFoldDB; Q9VL76; -.
DR IntAct; Q9VL76; 4.
DR STRING; 7227.FBpp0079501; -.
DR PaxDb; Q9VL76; -.
DR EnsemblMetazoa; FBtr0079911; FBpp0079501; FBgn0032154.
DR GeneID; 34307; -.
DR KEGG; dme:Dmel_CG5924; -.
DR UCSC; CG5924-RA; d. melanogaster.
DR CTD; 34307; -.
DR FlyBase; FBgn0032154; mtDNA-helicase.
DR VEuPathDB; VectorBase:FBgn0032154; -.
DR eggNOG; KOG2373; Eukaryota.
DR GeneTree; ENSGT00390000004495; -.
DR HOGENOM; CLU_012336_1_0_1; -.
DR InParanoid; Q9VL76; -.
DR OMA; RCLLIRP; -.
DR OrthoDB; 212176at2759; -.
DR PhylomeDB; Q9VL76; -.
DR BRENDA; 3.6.4.12; 1994.
DR BioGRID-ORCS; 34307; 0 hits in 1 CRISPR screen.
DR ChiTaRS; mtDNA-helicase; fly.
DR GenomeRNAi; 34307; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032154; Expressed in adult abdomen and 19 other tissues.
DR ExpressionAtlas; Q9VL76; baseline and differential.
DR Genevisible; Q9VL76; DM.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:FlyBase.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:FlyBase.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:FlyBase.
DR GO; GO:0006264; P:mitochondrial DNA replication; ISS:UniProtKB.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:FlyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR027032; Twinkle-like.
DR PANTHER; PTHR12873; PTHR12873; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN 22..613
FT /note="Mitochondrial DNA helicase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000453172"
FT DOMAIN 351..602
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT REGION 24..333
FT /note="Binds to DNA"
FT /evidence="ECO:0000269|PubMed:25023283"
FT REGION 24..123
FT /note="ZBD domain"
FT /evidence="ECO:0000269|PubMed:25023283"
FT BINDING 68
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:25023283"
FT BINDING 71
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:25023283"
FT BINDING 102
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:25023283"
FT BINDING 105
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:25023283"
FT BINDING 382..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT MUTAGEN 63
FT /note="C->A: Does not affect ion and sulfide binding.
FT Results in a partial increase in mitochondrial DNA copy
FT number."
FT /evidence="ECO:0000269|PubMed:19063859,
FT ECO:0000269|PubMed:25023283"
FT MUTAGEN 68
FT /note="C->A: Loss of ion and sulfide binding, increased
FT protein instability, retains DNA binding, partial increase
FT in mitochondrial DNA copy number; when associated with A-
FT 71."
FT /evidence="ECO:0000269|PubMed:19063859,
FT ECO:0000269|PubMed:25023283"
FT MUTAGEN 71
FT /note="C->A: Loss of ion and sulfide binding, increased
FT protein instability, partial increase in mitochondrial DNA
FT copy number, retains DNA binding; when associated with A-
FT 68."
FT /evidence="ECO:0000269|PubMed:19063859,
FT ECO:0000269|PubMed:25023283"
FT MUTAGEN 102
FT /note="C->A: Loss of ion and sulfide binding and increased
FT protein instability, retains DNA binding; when associated
FT with A-105."
FT /evidence="ECO:0000269|PubMed:25023283"
FT MUTAGEN 105
FT /note="C->A: Loss of ion and sulfide binding and increased
FT protein instability, retains DNA binding; when associated
FT with A-102."
FT /evidence="ECO:0000269|PubMed:25023283"
FT MUTAGEN 193
FT /note="K->A: Partial increase in mitochondrial DNA copy
FT number."
FT /evidence="ECO:0000269|PubMed:19063859"
FT MUTAGEN 232
FT /note="D->A: Partial increase in mitochondrial DNA copy
FT number."
FT /evidence="ECO:0000269|PubMed:19063859"
FT MUTAGEN 245
FT /note="C->A: Loss of ion and sulfide binding; when
FT associated with A-248."
FT /evidence="ECO:0000269|PubMed:25023283"
FT MUTAGEN 248
FT /note="C->A: Loss of ion and sulfide binding; when
FT associated with A-245."
FT /evidence="ECO:0000269|PubMed:25023283"
FT MUTAGEN 260
FT /note="C->A: Does not affect ion and sulfide binding."
FT /evidence="ECO:0000269|PubMed:25023283"
FT MUTAGEN 267
FT /note="F->A: No increase in mitochondrial DNA copy number."
FT /evidence="ECO:0000269|PubMed:19063859"
FT MUTAGEN 273
FT /note="W->A: No increase in mitochondrial DNA copy number."
FT /evidence="ECO:0000269|PubMed:19063859"
FT MUTAGEN 277
FT /note="D->A: No increase in mitochondrial DNA copy number."
FT /evidence="ECO:0000269|PubMed:19063859"
FT MUTAGEN 282
FT /note="W->L: Modest reduction in mitochondrial DNA copy
FT number."
FT /evidence="ECO:0000269|PubMed:19063859"
FT MUTAGEN 297
FT /note="C->A: Does not affect ion and sulfide binding."
FT /evidence="ECO:0000269|PubMed:25023283"
FT MUTAGEN 301
FT /note="R->Q: Reduces mitochondrial DNA copy number."
FT /evidence="ECO:0000269|PubMed:19063859"
FT MUTAGEN 302
FT /note="P->L: Modest reduction in mitochondrial DNA copy
FT number."
FT /evidence="ECO:0000269|PubMed:19063859"
FT MUTAGEN 326
FT /note="A->T: No effect on mitochondrial transcription."
FT /evidence="ECO:0000269|PubMed:17272269"
FT MUTAGEN 334
FT /note="I->T: Loss of mitochondrial transcription."
FT /evidence="ECO:0000269|PubMed:17272269"
FT MUTAGEN 341
FT /note="R->Q: No effect on mitochondrial transcription."
FT /evidence="ECO:0000269|PubMed:17272269"
FT MUTAGEN 388
FT /note="K->A: In vitro, loss of hexamer formation. Loss of
FT mitochondrial transcription. In vivo, results in
FT significant decrease in complex IV activity, increase in
FT apoptosis and a decrease in cell proliferation."
FT /evidence="ECO:0000269|PubMed:17272269,
FT ECO:0000269|PubMed:22952820"
FT MUTAGEN 441
FT /note="W->C: In vitro, no effect on mitochondrial
FT transcription. In vivo, moderate decrease in mtDNA levels
FT in the third instar larval stage and slight decrease in
FT longevity in the adult."
FT /evidence="ECO:0000269|PubMed:17272269"
FT MUTAGEN 442
FT /note="A->P: In vitro, loss of mitochondrial transcription.
FT In vivo, significant decrease in complex IV activity,
FT increase in apoptosis and a decrease in cell proliferation.
FT In vivo, results in significant decrease in complex IV
FT activity, increase in apoptosis and a decrease in cell
FT proliferation."
FT /evidence="ECO:0000269|PubMed:17272269,
FT ECO:0000269|PubMed:22952820"
FT MUTAGEN 483
FT /note="D->A: Loss of hexamer formation. Loss of
FT mitochondrial transcription."
FT /evidence="ECO:0000269|PubMed:17272269"
SQ SEQUENCE 613 AA; 70068 MW; 289E551726900436 CRC64;
MRRAGLIKPL LRINNEKQRV WRKNYATQVV SGLEECSLDP KEYVDFKRQL RQLNLPHKDG
HTCLQLECRL CDRNRQPVTN AQKGTDHGLL AYVNKRTGAF ICPNCDVKTS LTSALLSYQL
PKPVGYKQPL QRQPVYESRF PHLAVVTPEA CAALGIKGLK EDQLNAIGAQ WEPQQQLLHF
KLRNAAQVEV GEKVLYLGDR REEIFQSSSS SGLLIHGAMN KTKAVLVSNL IDFIVLATQN
IETHCVVCLP YELKTLPQEC LPALERFKEL IFWLHYDASH SWDAARAFAL KLDERRCLLI
RPTETEPAPH LALRRRLNLR HILAKATPVQ HKAITTFGAM RNDILSELQN IEKVNGVKWK
RFPVLNKLLK GHRRGELTIL TGPTGSGKTT FMSEYSLDLA MQGVNTLWGS FEIRNTRLAA
TLLRQYVGYP LDDRLHEFNH WAAEFERLPL YFMTFHGQQP LKPVLEAIEH ASYVHDVMHV
IIDNLQFMMG VSTFRGDKFF EQDSIIAAFR SFATKHNVHV TLVMHPRKER QEDELTTSSV
FGTAKATQEA DNVLIIQDKR LTSVRGKKYL QIAKNRYSGD LGIMPLEFDK DGLSYSTQIQ
NAKRKREKTP SEN
