SYEP_CRIGR
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 03-AUG-2022, entry version 84.
DE RecName: Full=Bifunctional glutamate/proline--tRNA ligase;
DE AltName: Full=Bifunctional aminoacyl-tRNA synthetase;
DE Includes:
DE RecName: Full=Glutamate--tRNA ligase;
DE EC=6.1.1.17;
DE AltName: Full=Glutamyl-tRNA synthetase;
DE Short=GluRS;
DE Includes:
DE RecName: Full=Proline--tRNA ligase;
DE EC=6.1.1.15 {ECO:0000250|UniProtKB:P07814};
DE AltName: Full=Prolyl-tRNA synthetase;
DE Short=ProRS;
GN Name=EPRS1; Synonyms=EPRS, 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 is primarily part of the
CC aminoacyl-tRNA synthetase multienzyme complex, also know as
CC multisynthetase complex, that catalyzes the attachment of the cognate
CC amino acid to the corresponding tRNA in a two-step reaction: the amino
CC acid is first activated by ATP to form a covalent intermediate with AMP
CC and is then transferred to the acceptor end of the cognate tRNA. The
CC phosphorylation of EPRS1, induced by interferon-gamma, dissociates the
CC protein from the aminoacyl-tRNA synthetase multienzyme complex and
CC recruits it to the GAIT complex that binds to stem loop-containing GAIT
CC elements in the 3'-UTR of diverse inflammatory mRNAs (such as
CC ceruplasmin), suppressing their translation. Interferon-gamma can
CC therefore redirect, in specific cells, the EPRS1 function from protein
CC synthesis to translation inhibition. Also functions as an effector of
CC the mTORC1 signaling pathway by promoting, through SLC27A1, the uptake
CC of long-chain fatty acid by adipocytes. Thereby, it also plays a role
CC in fat 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 -!- 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 -!- 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}.
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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 STRING; 10029.XP_007636777.1; -.
DR Ensembl; ENSCGRT00001011517; ENSCGRP00001007475; ENSCGRG00001009885.
DR eggNOG; KOG1147; Eukaryota.
DR eggNOG; KOG4163; Eukaryota.
DR GeneTree; ENSGT00550000074815; -.
DR EvolutionaryTrace; Q7SIA2; -.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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 interferon-gamma; IEA:Ensembl.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
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; cd00778; ProRS_core_arch_euk; 1.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.30.110.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
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_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR PANTHER; PTHR43382; PTHR43382; 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; 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; SSF47060; SSF47060; 3.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF50715; SSF50715; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF64586; SSF64586; 1.
DR TIGRFAMs; TIGR00463; gltX_arch; 1.
DR TIGRFAMs; TIGR00408; proS_fam_I; 1.
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; 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:P07814"
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 958..990
FT /note="Charged"
FT /evidence="ECO:0000250|UniProtKB:P07814"
FT REGION 1006..1511
FT /note="Proline--tRNA ligase"
FT /evidence="ECO:0000250|UniProtKB:P07814"
FT MOTIF 204..214
FT /note="'HIGH' region"
FT MOTIF 432..436
FT /note="'KMSKS' region"
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 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07814"
FT BINDING 398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07814"
FT BINDING 432..436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07814"
FT BINDING 1120..1122
FT /ligand="L-proline"
FT /ligand_id="ChEBI:CHEBI:60039"
FT /evidence="ECO:0000250|UniProtKB:P07814"
FT BINDING 1151..1153
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 1162..1163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07814"
FT BINDING 1236..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 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
