GARS_DROME
ID GARS_DROME Reviewed; 765 AA.
AC Q9VUK8; C9QP25; Q961R8;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Glycine--tRNA ligase {ECO:0000305};
DE EC=6.1.1.14 {ECO:0000250|UniProtKB:P41250};
DE AltName: Full=Diadenosine tetraphosphate synthetase {ECO:0000305};
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P41250};
DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000312|FlyBase:FBgn0027088};
DE Flags: Precursor;
GN Name=GlyRS {ECO:0000312|FlyBase:FBgn0027088};
GN Synonyms=aaRS(Gly) {ECO:0000312|FlyBase:FBgn0027088},
GN Aat-gly {ECO:0000312|FlyBase:FBgn0027088},
GN Aats-gly {ECO:0000303|PubMed:17529987, ECO:0000312|FlyBase:FBgn0027088},
GN gars {ECO:0000303|PubMed:17529987, ECO:0000312|EMBL:AAN11786.1},
GN GRS {ECO:0000312|FlyBase:FBgn0027088}, team {ECO:0000303|PubMed:17529987,
GN ECO:0000312|FlyBase:FBgn0027088};
GN ORFNames=CG6778 {ECO:0000312|FlyBase:FBgn0027088};
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:AAK92837.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK92837.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAK92837.1};
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:0000312|EMBL:ACX32978.1, ECO:0000312|EMBL:AFA28448.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACX32978.1, ECO:0000312|EMBL:AFA28448.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION (ISOFORMS A AND B), AND MUTAGENESIS OF
RP MET-87 AND PRO-98.
RX PubMed=17529987; DOI=10.1038/nn1910;
RA Chihara T., Luginbuhl D., Luo L.;
RT "Cytoplasmic and mitochondrial protein translation in axonal and dendritic
RT terminal arborization.";
RL Nat. Neurosci. 10:828-837(2007).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION (ISOFORM A), AND MUTAGENESIS OF PRO-320 AND GLY-326.
RX PubMed=24807208; DOI=10.1016/j.nbd.2014.04.020;
RA Ermanoska B., Motley W.W., Leitao-Goncalves R., Asselbergh B., Lee L.H.,
RA De Rijk P., Sleegers K., Ooms T., Godenschwege T.A., Timmerman V.,
RA Fischbeck K.H., Jordanova A.;
RT "CMT-associated mutations in glycyl- and tyrosyl-tRNA synthetases exhibit
RT similar pattern of toxicity and share common genetic modifiers in
RT Drosophila.";
RL Neurobiol. Dis. 68:180-189(2014).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION (ISOFORM A), AND MUTAGENESIS OF 97-ALA--PHE-163;
RP PRO-320 AND GLY-326.
RX PubMed=25972375; DOI=10.1093/hmg/ddv176;
RA Grice S.J., Sleigh J.N., Motley W.W., Liu J.L., Burgess R.W., Talbot K.,
RA Cader M.Z.;
RT "Dominant, toxic gain-of-function mutations in gars lead to non-cell
RT autonomous neuropathology.";
RL Hum. Mol. Genet. 24:4397-4406(2015).
RN [8] {ECO:0000305}
RP SUBCELLULAR LOCATION (ISOFORM A), AND MUTAGENESIS OF PRO-320.
RX PubMed=29520219; DOI=10.3389/fnmol.2018.00055;
RA Grice S.J., Sleigh J.N., Zameel Cader M.;
RT "Plexin-Semaphorin Signaling Modifies Neuromuscular Defects in a Drosophila
RT Model of Peripheral Neuropathy.";
RL Front. Mol. Neurosci. 11:55-55(2018).
CC -!- FUNCTION: Catalyzes the ATP-dependent ligation of glycine to the 3'-end
CC of its cognate tRNA, via the formation of an aminoacyl-adenylate
CC intermediate (Gly-AMP). Also produces diadenosine tetraphosphate
CC (Ap4A), a universal pleiotropic signaling molecule needed for cell
CC regulation pathways, by direct condensation of 2 ATPs. Thereby, may
CC play a special role in Ap4A homeostasis (By similarity). Required for
CC terminal arborization of both dendrites and axons during development
CC (PubMed:17529987). {ECO:0000250|UniProtKB:P41250,
CC ECO:0000269|PubMed:17529987}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H(+) = diphosphate + P(1),P(4)-bis(5'-adenosyl)
CC tetraphosphate; Xref=Rhea:RHEA:34935, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58141;
CC Evidence={ECO:0000250|UniProtKB:P41250};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34936;
CC Evidence={ECO:0000250|UniProtKB:P41250};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC EC=6.1.1.14; Evidence={ECO:0000250|UniProtKB:P41250};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16014;
CC Evidence={ECO:0000250|UniProtKB:P41250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P41250}.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Mitochondrion
CC {ECO:0000269|PubMed:17529987}.
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm
CC {ECO:0000269|PubMed:17529987, ECO:0000269|PubMed:24807208,
CC ECO:0000269|PubMed:25972375}. Cell projection, axon
CC {ECO:0000269|PubMed:24807208, ECO:0000269|PubMed:25972375}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0027088};
CC IsoId=Q9VUK8-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0027088};
CC IsoId=Q9VUK8-2; Sequence=VSP_060972;
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000250|UniProtKB:P41250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014296; AAF49668.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN11786.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94560.1; -; Genomic_DNA.
DR EMBL; AY051413; AAK92837.1; -; mRNA.
DR EMBL; BT133207; AFA28448.1; -; mRNA.
DR EMBL; BT099907; ACX32978.1; -; mRNA.
DR RefSeq; NP_001261867.1; NM_001274938.1. [Q9VUK8-1]
DR RefSeq; NP_648746.1; NM_140489.3. [Q9VUK8-2]
DR RefSeq; NP_730022.1; NM_168605.2. [Q9VUK8-1]
DR AlphaFoldDB; Q9VUK8; -.
DR SMR; Q9VUK8; -.
DR IntAct; Q9VUK8; 8.
DR STRING; 7227.FBpp0075386; -.
DR PaxDb; Q9VUK8; -.
DR PRIDE; Q9VUK8; -.
DR DNASU; 39644; -.
DR EnsemblMetazoa; FBtr0075632; FBpp0075385; FBgn0027088. [Q9VUK8-2]
DR EnsemblMetazoa; FBtr0075633; FBpp0075386; FBgn0027088. [Q9VUK8-1]
DR EnsemblMetazoa; FBtr0333934; FBpp0306062; FBgn0027088. [Q9VUK8-1]
DR GeneID; 39644; -.
DR KEGG; dme:Dmel_CG6778; -.
DR UCSC; CG6778-RA; d. melanogaster.
DR UCSC; CG6778-RB; d. melanogaster. [Q9VUK8-1]
DR CTD; 39644; -.
DR FlyBase; FBgn0027088; GlyRS.
DR VEuPathDB; VectorBase:FBgn0027088; -.
DR eggNOG; KOG2298; Eukaryota.
DR GeneTree; ENSGT00940000153759; -.
DR HOGENOM; CLU_015515_1_0_1; -.
DR InParanoid; Q9VUK8; -.
DR OMA; EPSYGID; -.
DR OrthoDB; 1183820at2759; -.
DR PhylomeDB; Q9VUK8; -.
DR SignaLink; Q9VUK8; -.
DR BioGRID-ORCS; 39644; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39644; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0027088; Expressed in oviduct (Drosophila) and 40 other tissues.
DR ExpressionAtlas; Q9VUK8; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
DR GO; GO:0070150; P:mitochondrial glycyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00774; GlyRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR033731; GlyRS-like_core.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR InterPro; IPR002315; tRNA-synt_gly.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR PANTHER; PTHR10745; PTHR10745; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Cell projection; Cytoplasm; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..87
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 88..765
FT /note="Glycine--tRNA ligase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000452350"
FT DOMAIN 95..151
FT /note="WHEP-TRS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT REGION 41..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 331
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 363..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 374..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 382
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 489..490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 609..611
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT VAR_SEQ 1..86
FT /note="Missing (in isoform A)"
FT /id="VSP_060972"
FT MUTAGEN 87
FT /note="M->T: Results in increased localization to
FT mitochondria."
FT /evidence="ECO:0000269|PubMed:17529987"
FT MUTAGEN 97..163
FT /note="Missing: Suppresses accumulation at the synapse,
FT reduced fly viability and defective neuromuscular junction;
FT when associated with K-320."
FT /evidence="ECO:0000269|PubMed:25972375"
FT MUTAGEN 98
FT /note="P->L: Results in neuronal terminal arborization
FT defects and loss of neuroblasts."
FT /evidence="ECO:0000269|PubMed:17529987"
FT MUTAGEN 320
FT /note="P->K: When overexpressed in the whole body, leads to
FT motor deficits, progressive neuromuscular junction (NMJ)
FT denervation and pre-synaptic build-up of mutant GlyRS
FT ultimately causing lethality. Similar effects are shown
FT when overexpressed in the mesoderm or neurons. Accumulates
FT at the synapse. When overexpressed in neurons, impairs
FT progressively neuronal functionality and morphology.
FT Toxicity might be mediated by modulation of the plexin-
FT semaphorin signaling. Suppresses accumulation at the
FT synapse, reduced fly viability and defective neuromuscular
FT junction; when associated with 97-A--F-163 DEL."
FT /evidence="ECO:0000269|PubMed:24807208,
FT ECO:0000269|PubMed:25972375, ECO:0000269|PubMed:29520219"
FT MUTAGEN 326
FT /note="G->R: When overexpressed in the whole body or
FT mesoderm, impairs development and reduces longevity. When
FT overexpressed in neurons, impairs progressively neuronal
FT functionality and morphology."
FT /evidence="ECO:0000269|PubMed:24807208,
FT ECO:0000269|PubMed:25972375"
FT CONFLICT 550
FT /note="A -> G (in Ref. 4; ACX32978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 765 AA; 85192 MW; E72462D4A04B84FF CRC64;
MSLQLLKALP HLRSATTAVR TQIARTTWSE HIATKVFFST TTTKPTPSAP PPPPPTQPQQ
PAATTSWGTK KQNRKVKLRS AAAEFIMSNP EIEAQLAPLR ERVQEQGNLV RDLKAKGAPE
IDVKKAVAEL KARKKLLEDK ELALTPSVVS FDRAKMEDLL KRRFFYDQSF AIYGGITGQY
DFGPMGCALK SNILALWRQY FALEEQMLEV DCSILTPEPV LKASGHVERF ADLMVKDVKT
GECFRLDHLI KQALEKLSKA KDATPALQAE CEDIIIKLDG LNKQELAGVL AKYNIKSPLT
GNDLTEPIEF NLMFATQIGP TGLVKGFLRP ETAQGIFVNF KRLLEFNQGK LPFAVAQIGN
SFRNEISPRS GLIRVREFTM AEIEHFCDPV LKDHPKFGNI KSEKLTLYSA CNQMDGKSAA
QVQIGEAVAS KLVANETLGY YMARIQQFLL AIGIKPECLR FRQHMSNEMA HYACDCWDAE
ILTSYGWVEC VGCADRSAYD LGQHTAATGV RLVAEKRLPA PKTVEVSEIV PNKQALGKTF
KKEAKNITDA LAKLSLEEIT KVEEQLAGDG QYKLTTADGQ SHDLGKDTIS VKHSTKTVHV
EEFIPSVVEP SFGIGRIMYS LLEHSFQCRD GDEQRCYFTL PPLVAPIKCS ILPLSNNTDF
QPYTQKLSSA LTKAELSHKV DDSSGSIGRR YARTDEIAIP YGITVDFDTL KEPHTVTLRD
RNTMKQVRVG LEEVVGVVKD LSTARTTWES VTEQYPLFEQ QEASK
