ID SYEP_CRIGR Reviewed; 1511 AA. AC Q7SIA2; Q7SIG9; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 23-MAY-2018, sequence version 3. DT 27-MAR-2024, entry version 90. DE RecName: Full=Bifunctional glutamate/proline--tRNA ligase {ECO:0000305}; DE AltName: Full=Bifunctional aminoacyl-tRNA synthetase; DE AltName: Full=Glutamyl-prolyl-tRNA synthetase {ECO:0000303|PubMed:10654942}; DE Includes: DE RecName: Full=Glutamate--tRNA ligase {ECO:0000250|UniProtKB:P07814}; DE EC=6.1.1.17 {ECO:0000250|UniProtKB:P07814}; DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000250|UniProtKB:P07814}; DE Short=GluRS {ECO:0000250|UniProtKB:P07814}; DE Includes: DE RecName: Full=Proline--tRNA ligase {ECO:0000250|UniProtKB:P07814}; DE EC=6.1.1.15 {ECO:0000250|UniProtKB:P07814}; DE AltName: Full=Prolyl-tRNA synthetase; DE Short=ProRS; GN Name=EPRS1 {ECO:0000250|UniProtKB:P07814}; GN Synonyms=EPRS {ECO:0000303|PubMed:10654942}, QPRS; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; OC Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M., RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W., RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R., RA Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line."; RL Nat. Biotechnol. 29:735-741(2011). RN [2] RP STRUCTURE BY NMR OF 826-874, AND DOMAIN. RX PubMed=10654942; DOI=10.1093/emboj/19.3.445; RA Cahuzac B., Berthonneau E., Birlirakis N., Guittet E., Mirande M.; RT "A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA RT synthetases."; RL EMBO J. 19:445-452(2000). CC -!- FUNCTION: Multifunctional protein which primarily functions within the CC aminoacyl-tRNA synthetase multienzyme complex, also known as CC multisynthetase complex. Within the complex it catalyzes the attachment CC of both L-glutamate and L-proline to their cognate tRNAs in a two-step CC reaction where the amino acid is first activated by ATP to form a CC covalent intermediate with AMP. Subsequently, the activated amino acid CC is transferred to the acceptor end of the cognate tRNA to form L- CC glutamyl-tRNA(Glu) and L-prolyl-tRNA(Pro). Upon interferon-gamma CC stimulation, EPRS1 undergoes phosphorylation, causing its dissociation CC from the aminoacyl-tRNA synthetase multienzyme complex. It is recruited CC to form the GAIT complex, which binds to stem loop-containing GAIT CC elements found in the 3'-UTR of various inflammatory mRNAs, such as CC ceruloplasmin. The GAIT complex inhibits the translation of these CC mRNAs, allowing interferon-gamma to redirect the function of EPRS1 from CC protein synthesis to translation inhibition in specific cell contexts. CC Furthermore, it can function as a downstream effector in the mTORC1 CC signaling pathway, by promoting the translocation of SLC27A1 from the CC cytoplasm to the plasma membrane where it mediates the uptake of long- CC chain fatty acid by adipocytes. Thereby, EPRS1 also plays a role in fat CC metabolism and more indirectly influences lifespan. CC {ECO:0000250|UniProtKB:P07814}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L- CC glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, CC Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, CC ChEBI:CHEBI:456215; EC=6.1.1.17; CC Evidence={ECO:0000250|UniProtKB:P07814}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23541; CC Evidence={ECO:0000250|UniProtKB:P07814}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl- CC tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA- CC COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215; CC EC=6.1.1.15; Evidence={ECO:0000250|UniProtKB:P07814}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14306; CC Evidence={ECO:0000250|UniProtKB:P07814}; CC -!- SUBUNIT: Homodimer. Part of the aminoacyl-tRNA synthetase multienzyme CC complex, also know as multisynthetase complex, that is composed of the CC tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), CC Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu CC and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and CC EEF1E1/p18. Forms a linear complex that contains MARS1, EEF1E1, EPRS1 CC and AIMP2 that is at the core of the multisubunit complex. Interacts CC with TARS3. Interacts with DUS2L. Component of the GAIT complex which CC is composed of EPRS1, RPL13A and GAPDH. Interacts (phosphorylated at CC Ser-998) with SLC27A1; mediates the translocation of SLC27A1 from the CC cytoplasm to the plasma membrane thereby increasing the uptake of long- CC chain fatty acids. {ECO:0000250|UniProtKB:P07814}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P07814}. Membrane CC {ECO:0000250|UniProtKB:P07814}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P07814}. Note=Translocates from cytosol to CC membranes upon phosphorylation at Ser-998. CC {ECO:0000250|UniProtKB:P07814}. CC -!- DOMAIN: The WHEP-TRS domains are involved in RNA binding. CC {ECO:0000269|PubMed:10654942}. CC -!- PTM: Phosphorylated at Ser-998 by RPS6KB1; triggers EPRS1 release from CC the aminoacyl-tRNA synthetase multienzyme complex. In monocytes, the CC IFN-gamma-induced phosphorylation at Ser-998 releases EPRS1 from the CC aminoacyl-tRNA synthetase multienzyme complex, allowing its association CC with the GAIT complex. Phosphorylation at Ser-998 is specifically CC required for the RPL13A-mediated interaction of the GAIT complex with CC eIF4G. Phosphorylation at Ser-998 by RPS6KB1, is also induced by CC insulin through activation of the mTORC1 signaling pathway and promotes CC the interaction of EPRS1 with SLC27A1. {ECO:0000250|UniProtKB:P07814}. CC -!- SIMILARITY: In the N-terminal section; belongs to the class-I CC aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the class-II CC aminoacyl-tRNA synthetase family. {ECO:0000305}. 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; AMDS01047676; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMDS01047677; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMDS01047678; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMDS01047679; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMDS01047680; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PDB; 1D2D; NMR; -; A=826-874. DR PDB; 1R1B; NMR; -; A=826-874. DR PDBsum; 1D2D; -. DR PDBsum; 1R1B; -. DR AlphaFoldDB; Q7SIA2; -. DR SMR; Q7SIA2; -. DR PaxDb; 10029-XP_007636777-1; -. DR Ensembl; ENSCGRT00001011517.1; ENSCGRP00001007475.1; ENSCGRG00001009885.1. DR Ensembl; ENSCGRT00015052903; ENSCGRP00015044688; ENSCGRG00015008514. DR eggNOG; KOG1147; Eukaryota. DR eggNOG; KOG4163; Eukaryota. DR GeneTree; ENSGT00550000074815; -. DR OrthoDB; 2733051at2759; -. DR EvolutionaryTrace; Q7SIA2; -. DR Proteomes; UP000694386; Unplaced. DR Proteomes; UP001108280; Genome assembly. DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0097452; C:GAIT complex; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004818; F:glutamate-tRNA ligase activity; ISS:UniProtKB. DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl. DR GO; GO:0004827; F:proline-tRNA ligase activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl. DR GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB. DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; ISS:UniProtKB. DR GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl. DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; ISS:UniProtKB. DR GO; GO:0140212; P:regulation of long-chain fatty acid import into cell; ISS:UniProtKB. DR CDD; cd00807; GlnRS_core; 1. DR CDD; cd10309; GST_C_GluProRS_N; 1. DR CDD; cd00862; ProRS_anticodon_zinc; 1. DR CDD; cd00778; ProRS_core_arch_euk; 1. DR CDD; cd00936; WEPRS_RNA; 3. DR Gene3D; 1.20.1050.130; -; 1. DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1. DR Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 3. DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1. DR HAMAP; MF_01571; Pro_tRNA_synth_type3; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. 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; IPR004526; Glu-tRNA-synth_arc/euk. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR004046; GST_C. DR InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type. DR InterPro; IPR016061; Pro-tRNA_ligase_II_C. DR InterPro; IPR017449; Pro-tRNA_synth_II. DR InterPro; IPR033721; ProRS_core_arch_euk. DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N. DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR049437; tRNA-synt_1c_C2. DR InterPro; IPR009068; uS15_NS1_RNA-bd_sf. DR InterPro; IPR000738; WHEP-TRS_dom. DR NCBIfam; TIGR00463; gltX_arch; 1. DR NCBIfam; TIGR00408; proS_fam_I; 1. DR PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1. DR PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF09180; ProRS-C_1; 1. DR Pfam; PF00749; tRNA-synt_1c; 1. DR Pfam; PF03950; tRNA-synt_1c_C; 1. DR Pfam; PF20974; tRNA-synt_1c_C2; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF00458; WHEP-TRS; 3. DR PRINTS; PR00987; TRNASYNTHGLU. DR SMART; SM00946; ProRS-C_1; 1. DR SMART; SM00991; WHEP-TRS; 3. DR SUPFAM; SSF64586; C-terminal domain of ProRS; 1. DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1. DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 3. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. DR PROSITE; PS00762; WHEP_TRS_1; 2. DR PROSITE; PS51185; WHEP_TRS_2; 3. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; KW Cytoplasm; Ligase; Magnesium; Membrane; Metal-binding; Methylation; KW Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; KW Protein biosynthesis; RNA-binding; Translation regulation; Zinc. FT CHAIN 1..1511 FT /note="Bifunctional glutamate/proline--tRNA ligase" FT /id="PRO_0000119742" FT DOMAIN 748..804 FT /note="WHEP-TRS 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531" FT DOMAIN 821..877 FT /note="WHEP-TRS 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531" FT DOMAIN 899..955 FT /note="WHEP-TRS 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531" FT REGION 164..758 FT /note="Glutamate--tRNA ligase" FT /evidence="ECO:0000250|UniProtKB:P28668" FT REGION 296..315 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 708..741 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 759..955 FT /note="3 X 57 AA approximate repeats" FT /evidence="ECO:0000250|UniProtKB:P07814" FT REGION 794..823 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 868..903 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 952..1015 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1006..1511 FT /note="Proline--tRNA ligase" FT /evidence="ECO:0000250|UniProtKB:P28668" FT MOTIF 204..214 FT /note="'HIGH' region" FT /evidence="ECO:0000250|UniProtKB:P28668" FT MOTIF 432..436 FT /note="'KMSKS' region" FT /evidence="ECO:0000250|UniProtKB:P28668" FT COMPBIAS 710..729 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 803..819 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 954..980 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 981..1005 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1120..1122 FT /ligand="L-proline" FT /ligand_id="ChEBI:CHEBI:60039" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1151 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1151 FT /ligand="L-proline" FT /ligand_id="ChEBI:CHEBI:60039" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1153 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1162 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1163 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1236 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1236 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1239 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1241 FT /ligand="L-proline" FT /ligand_id="ChEBI:CHEBI:60039" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1275 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1277 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1447 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1452 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1494 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P07814" FT BINDING 1496 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 300 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 300 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 355 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 417 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 434 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 498 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 535 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 542 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 637 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 746 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 787 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 860 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8CGC7" FT MOD_RES 871 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 885 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 897 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 997 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 998 FT /note="Phosphoserine; by RPS6KB1" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 999 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 1151 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 1349 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT MOD_RES 1502 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P07814" FT HELIX 827..841 FT /evidence="ECO:0007829|PDB:1D2D" FT HELIX 846..863 FT /evidence="ECO:0007829|PDB:1D2D" FT STRAND 865..870 FT /evidence="ECO:0007829|PDB:1D2D" SQ SEQUENCE 1511 AA; 169781 MW; 58CC131EAD375785 CRC64; MAALCLTVNA GDPPLDALLA VEHVKGDVSV SVEEGKENLL RVSEDVVFTD INSILRYLAR VATTSGLYGT NLMEHTEIDH WLEFSATKLS SCAALTSALT ELNHCLSLRT YLVGNSLTLA DLCVWATLKG NAAWQEQLEQ NKTLVHVKRW FGFLEAQQAF RSVGTKWDVS ENKARVVPDK KQDVGKFVEL PGAEMGKVTV RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN PEKEKEDFEK VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK AEREQRAESK HRQNSVEKNL QMWEEMKKGS PFGQSCCLRA KIDMSSNNGC MRDPTLYRCK IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH DRDEQFYWII EALGIRKPYI WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS SRSVVNMEWD KIWAFNKKVI DPVAPRYVAL LKKEVVPVNV PEAQEEMKEV ARHPKNPDVG LKPVWYSPKV FIEGADAETF SEGEMVTFIN WGNINITKIH KNADGKITSL DAKLNLENKD YKKTTKITWL AETTHALPIP AICVTYEHLI TKPVLGKDED FKQYVNKDSK HEELMLGDPC LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCKEAPCILI YIPDGHTKEM PTSGSKEKTK AEPLKKETSS APKEGPVPAV SPCAASEESS VLYNRVAAQG DVVRELKAKK AAKEDVDAAV KQLLALKAEY KQKTGQEYKP GNPPSAAAQS ASTKSLPSAG EDRSLYDKIA AQGEVVRKLK AEKAPKAKVT EAVECLLSLK AEYKEKTGKE YVPGQPPASQ KSQPSPASKA EPAGPETTEA KALFDRVACQ GEVVRKLKAE KASKDQVDPA VQELLQLKAQ YKSLTGIEYK PVSATGSEDK DKKKKEKENK SEKQNKPQKQ NDGPGKDSSK SQGGGLSSSG AGEGQGPKKQ TRLGLEAKKE ENLAEWYSQV ITKSEMIEYY DVSGCYILRP WSYSIWESIK DFFDTEIKKL GVENCYFPIF VSQAALEKEK SHIEDFAPEV AWVTRSGKTE LAEPIAIRPT SETVMYPAYA KWVQSHRDLP IRLNQWCNVV RWEFKHPQPF LRTREFLWQE GHSAFATFEE AADEVMQILE LYARVYEELL AIPVVRGRKT EKEKFAGGDY TTTVEAFISA SGRAIQGATS HHLGQNFSKM CEIVFEDPKT PGEKQFAFQC SWGLTTRTIG VMIMVHGDNM GLVLPPRVAC VQVVVIPCGI TNALSEEDRE ALMAKCNEYR KRLLGVNIRV RVDLRDNYSP GWKFNHWELK GVPVRLEVGP RDMKSCQFVA VRRDTGEKLT IAEKEAESKL QEILEDIQLN LFTRASEDLK THMVVSNTLE DFQKVLDSGK IAQIPFCGEI DCEDWIKKTT ARDQDVEPGA PSMGAKSLCI PFTPLCELQP GAMCVCGKNP AKFYTLFGRS Y //