GARS_MOUSE
ID GARS_MOUSE Reviewed; 729 AA.
AC Q9CZD3; Q3TMM4; Q3UK01; Q8VC67;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Glycine--tRNA ligase;
DE EC=6.1.1.14 {ECO:0000250|UniProtKB:P41250};
DE AltName: Full=Diadenosine tetraphosphate synthetase;
DE Short=Ap4A synthetase;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P41250};
DE AltName: Full=Glycyl-tRNA synthetase 1 {ECO:0000250|UniProtKB:P41250};
DE Short=GlyRS;
DE Flags: Precursor;
GN Name=Gars1; Synonyms=Gars;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Embryo, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 309-321; 554-573 AND 593-605, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-443, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=18614015; DOI=10.1016/j.cell.2008.06.016;
RA Pagliarini D.J., Calvo S.E., Chang B., Sheth S.A., Vafai S.B., Ong S.E.,
RA Walford G.A., Sugiana C., Boneh A., Chen W.K., Hill D.E., Vidal M.,
RA Evans J.G., Thorburn D.R., Carr S.A., Mootha V.K.;
RT "A mitochondrial protein compendium elucidates complex I disease biology.";
RL Cell 134:112-123(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-690, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP VARIANT PRO-278 DELINS TYR-LYS.
RX PubMed=16982418; DOI=10.1016/j.neuron.2006.08.027;
RA Seburn K.L., Nangle L.A., Cox G.A., Schimmel P., Burgess R.W.;
RT "An active dominant mutation of glycyl-tRNA synthetase causes neuropathy in
RT a Charcot-Marie-Tooth 2D mouse model.";
RL Neuron 51:715-726(2006).
RN [9]
RP CHARACTERIZATION OF VARIANT PRO-278 DELINS TYR-LYS, AND SUBCELLULAR
RP LOCATION.
RX PubMed=26503042; DOI=10.1038/nature15510;
RA He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y.,
RA Dumitru C.D., Lettieri K., Shubayev V., Jordanova A., Guergueltcheva V.,
RA Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
RT "CMT2D neuropathy is linked to the neomorphic binding activity of glycyl-
RT tRNA synthetase.";
RL Nature 526:710-714(2015).
RN [10]
RP ERRATUM OF PUBMED:26503042.
RX PubMed=26789244; DOI=10.1038/nature16499;
RA He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y.,
RA Dan Dumitru C., Lettieri K., Shubayev V., Jordanova A., Guergueltcheva V.,
RA Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
RT "Corrigendum: CMT2D neuropathy is linked to the neomorphic binding activity
RT of glycyl-tRNA synthetase.";
RL Nature 532:402-402(2016).
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.
CC {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 -!- 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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P41250}.
CC -!- INTERACTION:
CC Q9CZD3; P41250: GARS1; Xeno; NbExp=2; IntAct=EBI-8321941, EBI-724143;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41250}.
CC Mitochondrion {ECO:0000269|PubMed:18614015}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P41250}. Secreted {ECO:0000269|PubMed:26503042}.
CC Secreted, extracellular exosome {ECO:0000305|PubMed:26503042}.
CC Note=Associated with granules in cultured neuron cells (By similarity).
CC Secreted by motor neuron and differentiated myotube cell lines, but not
CC by undifferentiated myoblasts, possibly through the exosome pathway
CC (PubMed:26503042). {ECO:0000250|UniProtKB:P41250,
CC ECO:0000269|PubMed:26503042}.
CC -!- DISEASE: Note=Mice (Nmf249) heterozygous for the P278YK variant are
CC used a model for human Charcot-Marie-Tooth 2D (CMT2D), which is caused
CC by dominant GARS mutations. They exhibit reduced amplitudes of muscle
CC compound action potentials and a large reduction in sciatic nerve
CC conduction velocity in the absence of demyelination or remyelination,
CC resulting from an age-related decrease in the number of large
CC myelinated motor and sensory axons. The loss of myelinated axons is
CC length-dependent, and there is a length- and time-dependent decrease in
CC motor innervation of distal versus proximal muscles. Most of the axonal
CC loss occurs by 1 month of age and mice that survive this period can be
CC long-lived. At the molecular level, the P278YK mutation creates a
CC neomorphic binding activity leading to the interaction of the variant
CC with NRP1. This interaction competes out VEGFA binding and inhibits
CC VEGFA-NRP1 signling which is essential for motor neuron survival.
CC VEGFA, but not GDNF treatment significantly ameliorates the loss of
CC motor function in mutant mice. {ECO:0000269|PubMed:16982418}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AK146238; BAE27003.1; -; mRNA.
DR EMBL; AK165857; BAE38417.1; -; mRNA.
DR EMBL; BC021747; AAH21747.1; -; mRNA.
DR CCDS; CCDS39492.1; -.
DR RefSeq; NP_851009.2; NM_180678.3.
DR AlphaFoldDB; Q9CZD3; -.
DR SMR; Q9CZD3; -.
DR BioGRID; 237263; 26.
DR DIP; DIP-60956N; -.
DR IntAct; Q9CZD3; 2.
DR MINT; Q9CZD3; -.
DR STRING; 10090.ENSMUSP00000003572; -.
DR MoonProt; Q9CZD3; -.
DR iPTMnet; Q9CZD3; -.
DR PhosphoSitePlus; Q9CZD3; -.
DR SwissPalm; Q9CZD3; -.
DR REPRODUCTION-2DPAGE; Q9CZD3; -.
DR EPD; Q9CZD3; -.
DR jPOST; Q9CZD3; -.
DR MaxQB; Q9CZD3; -.
DR PaxDb; Q9CZD3; -.
DR PeptideAtlas; Q9CZD3; -.
DR PRIDE; Q9CZD3; -.
DR ProteomicsDB; 267560; -.
DR Antibodypedia; 6744; 377 antibodies from 32 providers.
DR DNASU; 353172; -.
DR Ensembl; ENSMUST00000003572; ENSMUSP00000003572; ENSMUSG00000029777.
DR GeneID; 353172; -.
DR KEGG; mmu:353172; -.
DR UCSC; uc009cai.1; mouse.
DR CTD; 353172; -.
DR MGI; MGI:2449057; Gars.
DR VEuPathDB; HostDB:ENSMUSG00000029777; -.
DR eggNOG; KOG2298; Eukaryota.
DR GeneTree; ENSGT00940000153759; -.
DR HOGENOM; CLU_015515_1_0_1; -.
DR InParanoid; Q9CZD3; -.
DR OMA; EPSYGID; -.
DR OrthoDB; 1183820at2759; -.
DR PhylomeDB; Q9CZD3; -.
DR TreeFam; TF343504; -.
DR BioGRID-ORCS; 353172; 26 hits in 79 CRISPR screens.
DR ChiTaRS; Gars; mouse.
DR PRO; PR:Q9CZD3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CZD3; protein.
DR Bgee; ENSMUSG00000029777; Expressed in floor plate of midbrain and 272 other tissues.
DR Genevisible; Q9CZD3; MM.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; ISS:UniProtKB.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IMP:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IMP:MGI.
DR GO; GO:0070150; P:mitochondrial glycyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; ISS:UniProtKB.
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 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cell projection;
KW Cytoplasm; Direct protein sequencing; Disease variant; Hydrolase; Ligase;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Secreted; Transferase; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..729
FT /note="Glycine--tRNA ligase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000072999"
FT DOMAIN 53..109
FT /note="WHEP-TRS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT BINDING 289
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 321..323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 332..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 340
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 447..448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 566..568
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 573
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT MOD_RES 194
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT MOD_RES 443
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 491
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 726
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT VARIANT 278
FT /note="P -> YK (found in Nmf249 mice, a Charcot-Marie-Tooth
FT 2D model; involved in neuromuscular dysfunction; contrary
FT to the wild-type protein, strongly interacts with NRP1 and
FT competes with VEGFA for NRP1-binding; no effect on
FT subcellular location)"
FT /evidence="ECO:0000269|PubMed:16982418,
FT ECO:0000269|PubMed:26503042"
FT CONFLICT 5
FT /note="L -> V (in Ref. 1; BAE38417)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="H -> N (in Ref. 1; BAE27003)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="F -> L (in Ref. 1; BAE27003)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="N -> S (in Ref. 2; AAH21747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 81878 MW; 596613F746B9C7D0 CRC64;
MPCLLPSLLR ATRAALPLLS PPRVVAASAS QRLLSAPAQP AASRSSMDSA EELLAPLRLA
VRQQGDFVRK LKEDKAPQVD VDRAVAELKA RKRVLEAKEL ALQPKDDIVD RAKMEDTLKR
RFFYDQAFAI YGGVSGLYDF GPVGCALKNN IIQAWRQHFI QEEQILEIDC TMLTPEPVLK
TSGHVDKFAD FMVKDVKNGE CFRADHLLKA HLQKLMSDKK CSAEKKSEME SVLAQLDNYG
QQELADLFVN YNVKSPTTGN DLSPPVPFNL MFQTFIGPGG NMPGYLRPET AQGIFLNFKR
LLEFNQGKLP FAAAQIGNSF RNEISPRSGL IRVREFTMAE IEHFVDPTEK DHPKFQSVAD
LCLYLYSAKA QVTGQSARKM RLGDAVEQGV INNSVLGYFI GRIYLYLTKV GISPDKLRFR
QHMENEMAHY ACDCWDAESK TSYGWIEIVG CADRSCYDLS CHARATKVPL VAEKPLKEPK
TVNVVQFEPN KGAVGKAYKK DAKLVLEYLS ACDECYISEM ELLLSEKGEF TIETEGKTFQ
LTKDMVSVKR FQKTLHVEEV VPSVIEPSFG LGRIMYTILE HTFHVREGDE QRTFFSFPAV
VAPFKCSVLP LSQNQEFMPF VKELSEALTR NGVSHKVDDS SGSIGRRYAR TDEIGVAFGI
TIDFDTVNKT PHTATLRDRD SMRQIRAEVS ELPNVVRDLA NGNITWADVE ARYPLFEGQE
TGKKETVEE
