SYRM_HUMAN
ID SYRM_HUMAN Reviewed; 578 AA.
AC Q5T160; B2RDT7; Q96FU5; Q9H8K8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable arginine--tRNA ligase, mitochondrial;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase;
DE Short=ArgRS;
DE Flags: Precursor;
GN Name=RARS2; Synonyms=RARSL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-331.
RC TISSUE=Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-291.
RC TISSUE=Uterus;
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 [5]
RP IDENTIFICATION.
RX PubMed=15779907; DOI=10.1021/bi047527z;
RA Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C.,
RA Sissler M.;
RT "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases:
RT characterization of AspRS and TyrRS.";
RL Biochemistry 44:4805-4816(2005).
RN [6]
RP INVOLVEMENT IN PCH6.
RX PubMed=17847012; DOI=10.1086/521227;
RA Edvardson S., Shaag A., Kolesnikova O., Gomori J.M., Tarassov I.,
RA Einbinder T., Saada A., Elpeleg O.;
RT "Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase
RT gene is associated with pontocerebellar hypoplasia.";
RL Am. J. Hum. Genet. 81:857-862(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP VARIANTS TYR-436 AND PHE-441.
RX PubMed=26741492; DOI=10.1371/journal.pgen.1005679;
RA Kohda M., Tokuzawa Y., Kishita Y., Nyuzuki H., Moriyama Y., Mizuno Y.,
RA Hirata T., Yatsuka Y., Yamashita-Sugahara Y., Nakachi Y., Kato H.,
RA Okuda A., Tamaru S., Borna N.N., Banshoya K., Aigaki T., Sato-Miyata Y.,
RA Ohnuma K., Suzuki T., Nagao A., Maehata H., Matsuda F., Higasa K.,
RA Nagasaki M., Yasuda J., Yamamoto M., Fushimi T., Shimura M.,
RA Kaiho-Ichimoto K., Harashima H., Yamazaki T., Mori M., Murayama K.,
RA Ohtake A., Okazaki Y.;
RT "A comprehensive genomic analysis reveals the genetic landscape of
RT mitochondrial respiratory chain complex deficiencies.";
RL PLoS Genet. 12:E1005679-E1005679(2016).
RN [10]
RP VARIANTS ALA-142; 315-ARG--MET-578 DEL AND ILE-342.
RX PubMed=33798445; DOI=10.1016/j.ajhg.2021.03.013;
RA Courage C., Oliver K.L., Park E.J., Cameron J.M., Grabinska K.A., Muona M.,
RA Canafoglia L., Gambardella A., Said E., Afawi Z., Baykan B., Brandt C.,
RA di Bonaventura C., Chew H.B., Criscuolo C., Dibbens L.M., Castellotti B.,
RA Riguzzi P., Labate A., Filla A., Giallonardo A.T., Berecki G.,
RA Jackson C.B., Joensuu T., Damiano J.A., Kivity S., Korczyn A., Palotie A.,
RA Striano P., Uccellini D., Giuliano L., Andermann E., Scheffer I.E.,
RA Michelucci R., Bahlo M., Franceschetti S., Sessa W.C., Berkovic S.F.,
RA Lehesjoki A.E.;
RT "Progressive myoclonus epilepsies-Residual unsolved cases have marked
RT genetic heterogeneity including dolichol-dependent protein glycosylation
RT pathway genes.";
RL Am. J. Hum. Genet. 108:722-738(2021).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC EC=6.1.1.19;
CC -!- INTERACTION:
CC Q5T160; P21964-2: COMT; NbExp=3; IntAct=EBI-1050546, EBI-10200977;
CC Q5T160; P21980-2: TGM2; NbExp=3; IntAct=EBI-1050546, EBI-25842075;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- DISEASE: Pontocerebellar hypoplasia 6 (PCH6) [MIM:611523]: A disorder
CC characterized by an abnormally small cerebellum and brainstem,
CC infantile encephalopathy, generalized hypotonia, lethargy and poor
CC feeding. Recurrent apnea, intractable seizures occur early in the
CC course of this condition. {ECO:0000269|PubMed:17847012}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AK023550; BAB14608.1; -; mRNA.
DR EMBL; AK315669; BAG38034.1; -; mRNA.
DR EMBL; AL451126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48584.1; -; Genomic_DNA.
DR EMBL; BC010420; AAH10420.1; -; mRNA.
DR CCDS; CCDS5011.1; -.
DR RefSeq; NP_064716.2; NM_020320.4.
DR AlphaFoldDB; Q5T160; -.
DR SMR; Q5T160; -.
DR BioGRID; 121334; 121.
DR IntAct; Q5T160; 27.
DR MINT; Q5T160; -.
DR STRING; 9606.ENSP00000358549; -.
DR GlyGen; Q5T160; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5T160; -.
DR PhosphoSitePlus; Q5T160; -.
DR BioMuta; RARS2; -.
DR DMDM; 74744409; -.
DR EPD; Q5T160; -.
DR jPOST; Q5T160; -.
DR MassIVE; Q5T160; -.
DR MaxQB; Q5T160; -.
DR PaxDb; Q5T160; -.
DR PeptideAtlas; Q5T160; -.
DR PRIDE; Q5T160; -.
DR ProteomicsDB; 64235; -.
DR Antibodypedia; 31811; 79 antibodies from 19 providers.
DR DNASU; 57038; -.
DR Ensembl; ENST00000369536.10; ENSP00000358549.5; ENSG00000146282.19.
DR GeneID; 57038; -.
DR KEGG; hsa:57038; -.
DR MANE-Select; ENST00000369536.10; ENSP00000358549.5; NM_020320.5; NP_064716.2.
DR UCSC; uc003pme.4; human.
DR CTD; 57038; -.
DR DisGeNET; 57038; -.
DR GeneCards; RARS2; -.
DR HGNC; HGNC:21406; RARS2.
DR HPA; ENSG00000146282; Low tissue specificity.
DR MalaCards; RARS2; -.
DR MIM; 611523; phenotype.
DR MIM; 611524; gene.
DR neXtProt; NX_Q5T160; -.
DR OpenTargets; ENSG00000146282; -.
DR Orphanet; 166073; Pontocerebellar hypoplasia type 6.
DR PharmGKB; PA162400662; -.
DR VEuPathDB; HostDB:ENSG00000146282; -.
DR eggNOG; KOG1195; Eukaryota.
DR GeneTree; ENSGT00530000063407; -.
DR HOGENOM; CLU_006406_6_2_1; -.
DR InParanoid; Q5T160; -.
DR OMA; YEFKWER; -.
DR OrthoDB; 463402at2759; -.
DR PhylomeDB; Q5T160; -.
DR TreeFam; TF300888; -.
DR PathwayCommons; Q5T160; -.
DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
DR SignaLink; Q5T160; -.
DR BioGRID-ORCS; 57038; 426 hits in 1087 CRISPR screens.
DR ChiTaRS; RARS2; human.
DR GenomeRNAi; 57038; -.
DR Pharos; Q5T160; Tbio.
DR PRO; PR:Q5T160; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5T160; protein.
DR Bgee; ENSG00000146282; Expressed in ileal mucosa and 179 other tissues.
DR ExpressionAtlas; Q5T160; baseline and differential.
DR Genevisible; Q5T160; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR CDD; cd00671; ArgRS_core; 1.
DR Gene3D; 3.30.1360.70; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR11956; PTHR11956; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF55190; SSF55190; 1.
DR TIGRFAMs; TIGR00456; argS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Neurodegeneration; Nucleotide-binding; Pontocerebellar hypoplasia;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..578
FT /note="Probable arginine--tRNA ligase, mitochondrial"
FT /id="PRO_0000250731"
FT MOTIF 133..144
FT /note="'HIGH' region"
FT BINDING 133..135
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 144
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 322
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 326
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 350
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT MOD_RES 568
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3U186"
FT VARIANT 142
FT /note="V -> A (found in a patient with progressive
FT myoclonus epilepsy and dementia; unknown pathological
FT significance; dbSNP:rs761568260)"
FT /evidence="ECO:0000269|PubMed:33798445"
FT /id="VAR_085046"
FT VARIANT 291
FT /note="K -> R (in dbSNP:rs17850652)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037800"
FT VARIANT 315..578
FT /note="Missing (found in a patient with progressive
FT myoclonus epilepsy and dementia; unknown pathological
FT significance; dbSNP:rs199835443)"
FT /evidence="ECO:0000269|PubMed:33798445"
FT /id="VAR_085047"
FT VARIANT 331
FT /note="I -> V (in dbSNP:rs3757370)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_037801"
FT VARIANT 342
FT /note="M -> I (found in a patient with late onset
FT progressive myoclonus epilepsy; unknown pathological
FT significance; dbSNP:rs34647222)"
FT /evidence="ECO:0000269|PubMed:33798445"
FT /id="VAR_085048"
FT VARIANT 367
FT /note="D -> G (in dbSNP:rs1108758)"
FT /id="VAR_037802"
FT VARIANT 436
FT /note="D -> Y (found in a patient with complex IV
FT deficiency and non-lethal infantile mitochondrial disease;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:26741492"
FT /id="VAR_076278"
FT VARIANT 441
FT /note="L -> F (found in a patient with complex IV
FT deficiency and non-lethal infantile mitochondrial disease;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:26741492"
FT /id="VAR_076279"
FT CONFLICT 48
FT /note="S -> P (in Ref. 1; BAB14608)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="I -> V (in Ref. 1; BAB14608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 65505 MW; 682075D065D88F82 CRC64;
MACGFRRAIA CQLSRVLNLP PENLITSISA VPISQKEEVA DFQLSVDSLL EKDNDHSRPD
IQVQAKRLAE KLRCDTVVSE ISTGQRTVNF KINRELLTKT VLQQVIEDGS KYGLKSELFS
GLPQKKIVVE FSSPNVAKKF HVGHLRSTII GNFIANLKEA LGHQVIRINY LGDWGMQFGL
LGTGFQLFGY EEKLQSNPLQ HLFEVYVQVN KEAADDKSVA KAAQEFFQRL ELGDVQALSL
WQKFRDLSIE EYIRVYKRLG VYFDEYSGES FYREKSQEVL KLLESKGLLL KTIKGTAVVD
LSGNGDPSSI CTVMRSDGTS LYATRDLAAA IDRMDKYNFD TMIYVTDKGQ KKHFQQVFQM
LKIMGYDWAE RCQHVPFGVV QGMKTRRGDV TFLEDVLNEI QLRMLQNMAS IKTTKELKNP
QETAERVGLA ALIIQDFKGL LLSDYKFSWD RVFQSRGDTG VFLQYTHARL HSLEETFGCG
YLNDFNTACL QEPQSVSILQ HLLRFDEVLY KSSQDFQPRH IVSYLLTLSH LAAVAHKTLQ
IKDSPPEVAG ARLHLFKAVR SVLANGMKLL GITPVCRM
