SYQ_HUMAN
ID SYQ_HUMAN Reviewed; 775 AA.
AC P47897; B4DWJ2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Glutamine--tRNA ligase;
DE EC=6.1.1.18 {ECO:0000269|PubMed:24656866, ECO:0000269|PubMed:26869582};
DE AltName: Full=Glutaminyl-tRNA synthetase;
DE Short=GlnRS {ECO:0000303|PubMed:25288775, ECO:0000303|PubMed:26869582};
GN Name=QARS1 {ECO:0000312|HGNC:HGNC:9751}; Synonyms=QARS;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Liver;
RX PubMed=8078941; DOI=10.1073/pnas.91.18.8670;
RA Lamour V., Quevillon S., Diriong S., N'Guyen V.C., Lipinski M., Mirande M.;
RT "Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a
RT case of horizontal gene transfer.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8670-8674(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Ovary, and Placenta;
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 PROTEIN SEQUENCE OF 2-19; 206-225; 377-391 AND 602-616, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10791971; DOI=10.1083/jcb.149.3.567;
RA Ko Y.G., Kang Y.S., Kim E.K., Park S.G., Kim S.;
RT "Nucleolar localization of human methionyl-tRNA synthetase and its role in
RT ribosomal RNA synthesis.";
RL J. Cell Biol. 149:567-574(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19131329; DOI=10.1074/jbc.m809636200;
RA Kaminska M., Havrylenko S., Decottignies P., Gillet S., Le Marechal P.,
RA Negrutskii B., Mirande M.;
RT "Dissection of the structural organization of the aminoacyl-tRNA synthetase
RT complex.";
RL J. Biol. Chem. 284:6053-6060(2009).
RN [11]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=19289464; DOI=10.1074/jbc.m900480200;
RA Kaminska M., Havrylenko S., Decottignies P., Le Marechal P., Negrutskii B.,
RA Mirande M.;
RT "Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the
RT Cytoplasm of Human Cells.";
RL J. Biol. Chem. 284:13746-13754(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-309, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH RARS1,
RP VARIANTS MSCCA VAL-45; HIS-57; TRP-403 AND TRP-515, AND CHARACTERIZATION OF
RP VARIANTS MSCCA VAL-45; HIS-57; TRP-403 AND TRP-515.
RX PubMed=24656866; DOI=10.1016/j.ajhg.2014.03.003;
RA Zhang X., Ling J., Barcia G., Jing L., Wu J., Barry B.J., Mochida G.H.,
RA Hill R.S., Weimer J.M., Stein Q., Poduri A., Partlow J.N., Ville D.,
RA Dulac O., Yu T.W., Lam A.T., Servattalab S., Rodriguez J., Boddaert N.,
RA Munnich A., Colleaux L., Zon L.I., Soll D., Walsh C.A., Nabbout R.;
RT "Mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive
RT microcephaly, cerebral-cerebellar atrophy, and intractable seizures.";
RL Am. J. Hum. Genet. 94:547-558(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19] {ECO:0007744|PDB:4R3Z}
RP X-RAY CRYSTALLOGRAPHY (4.03 ANGSTROMS) IN COMPLEX WITH RARS1 AND AIMP1.
RX PubMed=25288775; DOI=10.1073/pnas.1408836111;
RA Fu Y., Kim Y., Jin K.S., Kim H.S., Kim J.H., Wang D., Park M., Jo C.H.,
RA Kwon N.H., Kim D., Kim M.H., Jeon Y.H., Hwang K.Y., Kim S., Cho Y.;
RT "Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for
RT mammalian translation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:15084-15089(2014).
RN [20] {ECO:0007744|PDB:4YE6, ECO:0007744|PDB:4YE8, ECO:0007744|PDB:4YE9}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF WILD-TYPE AND VARIANTS MSCCA
RP VAL-45 AND HIS-57, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF
RP HIS-175, AND CHARACTERIZATION OF VARIANTS MSCCA VAL-45; HIS-57; TRP-403 AND
RP TRP-515.
RX PubMed=26869582; DOI=10.1093/nar/gkw082;
RA Ognjenovic J., Wu J., Matthies D., Baxa U., Subramaniam S., Ling J.,
RA Simonovic M.;
RT "The crystal structure of human GlnRS provides basis for the development of
RT neurological disorders.";
RL Nucleic Acids Res. 44:3420-3431(2016).
CC -!- FUNCTION: Glutamine--tRNA ligase (PubMed:26869582). Plays a critical
CC role in brain development (PubMed:24656866).
CC {ECO:0000269|PubMed:24656866, ECO:0000269|PubMed:26869582}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC ChEBI:CHEBI:456215; EC=6.1.1.18;
CC Evidence={ECO:0000269|PubMed:24656866};
CC -!- SUBUNIT: Monomer (PubMed:26869582). Part of a multisubunit complex that
CC groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile
CC (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase
CC for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38
CC and EEF1E1/p18 (PubMed:19131329, PubMed:19289464). Interacts with RARS1
CC (PubMed:24656866). Part of a complex composed of RARS1, QARS1 and AIMP1
CC (PubMed:25288775). {ECO:0000269|PubMed:19131329,
CC ECO:0000269|PubMed:19289464, ECO:0000269|PubMed:24656866,
CC ECO:0000269|PubMed:25288775, ECO:0000269|PubMed:26869582}.
CC -!- INTERACTION:
CC P47897; P35609: ACTN2; NbExp=3; IntAct=EBI-347462, EBI-77797;
CC P47897; Q9BPU9: B9D2; NbExp=3; IntAct=EBI-347462, EBI-6958971;
CC P47897; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-347462, EBI-517623;
CC P47897; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-347462, EBI-739580;
CC P47897; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-347462, EBI-3866319;
CC P47897; P56545-3: CTBP2; NbExp=3; IntAct=EBI-347462, EBI-10171902;
CC P47897; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-347462, EBI-11988027;
CC P47897; P50570: DNM2; NbExp=3; IntAct=EBI-347462, EBI-346547;
CC P47897; Q96F86: EDC3; NbExp=3; IntAct=EBI-347462, EBI-997311;
CC P47897; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-347462, EBI-2349927;
CC P47897; Q96DF8: ESS2; NbExp=3; IntAct=EBI-347462, EBI-3928124;
CC P47897; Q3B820: FAM161A; NbExp=3; IntAct=EBI-347462, EBI-719941;
CC P47897; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-347462, EBI-1384254;
CC P47897; Q86WP2: GPBP1; NbExp=3; IntAct=EBI-347462, EBI-2349758;
CC P47897; P28799: GRN; NbExp=3; IntAct=EBI-347462, EBI-747754;
CC P47897; O43708: GSTZ1; NbExp=3; IntAct=EBI-347462, EBI-748043;
CC P47897; Q9BYE0: HES7; NbExp=3; IntAct=EBI-347462, EBI-12163087;
CC P47897; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-347462, EBI-740641;
CC P47897; P49639: HOXA1; NbExp=3; IntAct=EBI-347462, EBI-740785;
CC P47897; P04792: HSPB1; NbExp=3; IntAct=EBI-347462, EBI-352682;
CC P47897; P42858: HTT; NbExp=6; IntAct=EBI-347462, EBI-466029;
CC P47897; Q13123: IK; NbExp=3; IntAct=EBI-347462, EBI-713456;
CC P47897; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-347462, EBI-11522367;
CC P47897; O60333-2: KIF1B; NbExp=3; IntAct=EBI-347462, EBI-10975473;
CC P47897; Q6P597: KLC3; NbExp=3; IntAct=EBI-347462, EBI-1643885;
CC P47897; O76013-2: KRT36; NbExp=3; IntAct=EBI-347462, EBI-11958506;
CC P47897; Q3B8N2: LGALS9B; NbExp=3; IntAct=EBI-347462, EBI-10240775;
CC P47897; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-347462, EBI-9088829;
CC P47897; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-347462, EBI-739832;
CC P47897; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-347462, EBI-1216080;
CC P47897; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-347462, EBI-741037;
CC P47897; P59942: MCCD1; NbExp=3; IntAct=EBI-347462, EBI-11987923;
CC P47897; Q14696: MESD; NbExp=3; IntAct=EBI-347462, EBI-6165891;
CC P47897; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-347462, EBI-10172526;
CC P47897; Q15742: NAB2; NbExp=3; IntAct=EBI-347462, EBI-8641936;
CC P47897; O76041: NEBL; NbExp=3; IntAct=EBI-347462, EBI-2880203;
CC P47897; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-347462, EBI-10271199;
CC P47897; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-347462, EBI-12025760;
CC P47897; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-347462, EBI-79165;
CC P47897; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-347462, EBI-12000762;
CC P47897; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-347462, EBI-11320284;
CC P47897; Q16825: PTPN21; NbExp=3; IntAct=EBI-347462, EBI-2860264;
CC P47897; Q04864-2: REL; NbExp=3; IntAct=EBI-347462, EBI-10829018;
CC P47897; Q9Y3C5: RNF11; NbExp=10; IntAct=EBI-347462, EBI-396669;
CC P47897; Q15427: SF3B4; NbExp=3; IntAct=EBI-347462, EBI-348469;
CC P47897; Q8IYI0: SHLD1; NbExp=3; IntAct=EBI-347462, EBI-2560428;
CC P47897; Q13239-3: SLA; NbExp=3; IntAct=EBI-347462, EBI-17630587;
CC P47897; O60504: SORBS3; NbExp=3; IntAct=EBI-347462, EBI-741237;
CC P47897; Q8TDD2: SP7; NbExp=5; IntAct=EBI-347462, EBI-10713842;
CC P47897; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-347462, EBI-11995806;
CC P47897; A6NLX3: SPDYE4; NbExp=3; IntAct=EBI-347462, EBI-12047907;
CC P47897; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-347462, EBI-7082156;
CC P47897; O75478: TADA2A; NbExp=3; IntAct=EBI-347462, EBI-742268;
CC P47897; Q99081: TCF12; NbExp=4; IntAct=EBI-347462, EBI-722877;
CC P47897; Q96PF1: TGM7; NbExp=3; IntAct=EBI-347462, EBI-12029034;
CC P47897; Q08117: TLE5; NbExp=3; IntAct=EBI-347462, EBI-717810;
CC P47897; Q12933: TRAF2; NbExp=3; IntAct=EBI-347462, EBI-355744;
CC P47897; Q9BUZ4: TRAF4; NbExp=6; IntAct=EBI-347462, EBI-3650647;
CC P47897; P14373: TRIM27; NbExp=3; IntAct=EBI-347462, EBI-719493;
CC P47897; Q9UPQ4-2: TRIM35; NbExp=4; IntAct=EBI-347462, EBI-17716262;
CC P47897; Q15645: TRIP13; NbExp=6; IntAct=EBI-347462, EBI-358993;
CC P47897; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-347462, EBI-739895;
CC P47897; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-347462, EBI-4400866;
CC P47897; O76024: WFS1; NbExp=3; IntAct=EBI-347462, EBI-720609;
CC P47897; P98170: XIAP; NbExp=3; IntAct=EBI-347462, EBI-517127;
CC P47897; Q9H0C1: ZMYND12; NbExp=5; IntAct=EBI-347462, EBI-12030590;
CC P47897; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-347462, EBI-527853;
CC P47897-2; Q86UW9: DTX2; NbExp=3; IntAct=EBI-10209725, EBI-740376;
CC P47897-2; Q6P597: KLC3; NbExp=3; IntAct=EBI-10209725, EBI-1643885;
CC P47897-2; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-10209725, EBI-741037;
CC P47897-2; Q99081: TCF12; NbExp=3; IntAct=EBI-10209725, EBI-722877;
CC P47897-2; Q08117: TLE5; NbExp=3; IntAct=EBI-10209725, EBI-717810;
CC P47897-2; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-10209725, EBI-3650647;
CC P47897-2; Q15645: TRIP13; NbExp=3; IntAct=EBI-10209725, EBI-358993;
CC P47897-2; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-10209725, EBI-4400866;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}.
CC Cytoplasm {ECO:0000269|PubMed:10791971, ECO:0000269|PubMed:24656866}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P47897-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P47897-2; Sequence=VSP_055107;
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal cerebral cortex,
CC particularly in the ventricular zone, inner subventricular zone, outer
CC subventricular zone, and cortical plate. {ECO:0000269|PubMed:24656866}.
CC -!- DISEASE: Microcephaly, progressive, with seizures and cerebral and
CC cerebellar atrophy (MSCCA) [MIM:615760]: A severe, autosomal recessive,
CC neurodevelopmental and neurodegenerative disorder characterized by
CC progressive microcephaly, severe seizures in infancy, atrophy of the
CC cerebral cortex and cerebellar vermis, and mild atrophy of the
CC cerebellar hemispheres, resulting in profoundly delayed development and
CC hypotonia. {ECO:0000269|PubMed:24656866, ECO:0000269|PubMed:26869582}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; X76013; CAA53600.1; -; mRNA.
DR EMBL; AK301559; BAG63054.1; -; mRNA.
DR EMBL; AC135506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000394; AAH00394.1; -; mRNA.
DR EMBL; BC001567; AAH01567.1; -; mRNA.
DR EMBL; BC029739; AAH29739.1; -; mRNA.
DR CCDS; CCDS2788.1; -. [P47897-1]
DR CCDS; CCDS63633.1; -. [P47897-2]
DR PIR; I37422; I37422.
DR RefSeq; NP_001259002.1; NM_001272073.1. [P47897-2]
DR RefSeq; NP_005042.1; NM_005051.2. [P47897-1]
DR PDB; 4R3Z; X-ray; 4.03 A; C=1-775.
DR PDB; 4YE6; X-ray; 2.40 A; A=1-775.
DR PDB; 4YE8; X-ray; 3.30 A; A=1-775.
DR PDB; 4YE9; X-ray; 2.70 A; A=1-775.
DR PDBsum; 4R3Z; -.
DR PDBsum; 4YE6; -.
DR PDBsum; 4YE8; -.
DR PDBsum; 4YE9; -.
DR AlphaFoldDB; P47897; -.
DR SMR; P47897; -.
DR BioGRID; 111797; 332.
DR CORUM; P47897; -.
DR IntAct; P47897; 141.
DR MINT; P47897; -.
DR STRING; 9606.ENSP00000307567; -.
DR BindingDB; P47897; -.
DR ChEMBL; CHEMBL3054; -.
DR DrugBank; DB00130; L-Glutamine.
DR MoonProt; P47897; -.
DR GlyGen; P47897; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P47897; -.
DR MetOSite; P47897; -.
DR PhosphoSitePlus; P47897; -.
DR SwissPalm; P47897; -.
DR BioMuta; QARS; -.
DR DMDM; 1351170; -.
DR CPTAC; CPTAC-123; -.
DR CPTAC; CPTAC-124; -.
DR EPD; P47897; -.
DR jPOST; P47897; -.
DR MassIVE; P47897; -.
DR MaxQB; P47897; -.
DR PaxDb; P47897; -.
DR PeptideAtlas; P47897; -.
DR PRIDE; P47897; -.
DR ProteomicsDB; 5345; -.
DR ProteomicsDB; 55816; -. [P47897-1]
DR ABCD; P47897; 1 sequenced antibody.
DR Antibodypedia; 30393; 148 antibodies from 26 providers.
DR DNASU; 5859; -.
DR Ensembl; ENST00000306125.12; ENSP00000307567.6; ENSG00000172053.18. [P47897-1]
DR Ensembl; ENST00000414533.5; ENSP00000390015.1; ENSG00000172053.18. [P47897-2]
DR GeneID; 5859; -.
DR KEGG; hsa:5859; -.
DR MANE-Select; ENST00000306125.12; ENSP00000307567.6; NM_005051.3; NP_005042.1.
DR UCSC; uc003cvx.5; human. [P47897-1]
DR CTD; 5859; -.
DR DisGeNET; 5859; -.
DR GeneCards; QARS1; -.
DR HGNC; HGNC:9751; QARS1.
DR HPA; ENSG00000172053; Low tissue specificity.
DR MalaCards; QARS1; -.
DR MIM; 603727; gene.
DR MIM; 615760; phenotype.
DR neXtProt; NX_P47897; -.
DR OpenTargets; ENSG00000172053; -.
DR Orphanet; 404437; Diffuse cerebral and cerebellar atrophy-intractable seizures-progressive microcephaly syndrome.
DR Orphanet; 423306; Microcephaly-short stature-intellectual disability-facial dysmorphism syndrome.
DR PharmGKB; PA34093; -.
DR VEuPathDB; HostDB:ENSG00000172053; -.
DR eggNOG; KOG1148; Eukaryota.
DR GeneTree; ENSGT00550000074972; -.
DR HOGENOM; CLU_001882_2_3_1; -.
DR InParanoid; P47897; -.
DR OMA; INNFCAQ; -.
DR PhylomeDB; P47897; -.
DR TreeFam; TF105683; -.
DR BRENDA; 6.1.1.18; 2681.
DR PathwayCommons; P47897; -.
DR Reactome; R-HSA-2408522; Selenoamino acid metabolism.
DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
DR SignaLink; P47897; -.
DR BioGRID-ORCS; 5859; 805 hits in 1088 CRISPR screens.
DR ChiTaRS; QARS; human.
DR GeneWiki; QARS; -.
DR GenomeRNAi; 5859; -.
DR Pharos; P47897; Tchem.
DR PRO; PR:P47897; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P47897; protein.
DR Bgee; ENSG00000172053; Expressed in mammalian vulva and 210 other tissues.
DR ExpressionAtlas; P47897; baseline and differential.
DR Genevisible; P47897; HS.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:CAFA.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IMP:CAFA.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IDA:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IDA:CAFA.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:CAFA.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IDA:CAFA.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:CAFA.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR Gene3D; 1.10.10.2420; -; 1.
DR Gene3D; 1.10.8.1290; -; 1.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004514; Gln-tRNA-synth.
DR InterPro; IPR007638; Gln-tRNA-synth_Ib_RNA-bd_2.
DR InterPro; IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
DR InterPro; IPR042558; Gln-tRNA-synth_Ib_RNA-bd_N_1.
DR InterPro; IPR042559; Gln-tRNA-synth_Ib_RNA-bd_N_2.
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; 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 Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF04558; tRNA_synt_1c_R1; 1.
DR Pfam; PF04557; tRNA_synt_1c_R2; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00440; glnS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Disease variant;
KW Epilepsy; Ligase; Nucleotide-binding; Phosphoprotein; Primary microcephaly;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..775
FT /note="Glutamine--tRNA ligase"
FT /id="PRO_0000195860"
FT MOTIF 270..280
FT /note="'HIGH' region"
FT /evidence="ECO:0000305|PubMed:26869582"
FT MOTIF 493..497
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305|PubMed:26869582"
FT BINDING 271..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 277..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 303
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 438
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 486..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 494..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 309
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 78..89
FT /note="SKKIHTEPQLSA -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055107"
FT VARIANT 45
FT /note="G -> V (in MSCCA; results in reduced glutaminyl-tRNA
FT aminoacylation activity; does not affect interaction with
FT RARS1; dbSNP:rs587777331)"
FT /evidence="ECO:0000269|PubMed:24656866,
FT ECO:0000269|PubMed:26869582"
FT /id="VAR_071189"
FT VARIANT 57
FT /note="Y -> H (in MSCCA; results in reduced glutaminyl-tRNA
FT aminoacylation activity; does not affect interaction with
FT RARS1; dbSNP:rs587777333)"
FT /evidence="ECO:0000269|PubMed:24656866,
FT ECO:0000269|PubMed:26869582"
FT /id="VAR_071190"
FT VARIANT 403
FT /note="R -> W (in MSCCA; results in loss of glutaminyl-tRNA
FT aminoacylation activity; impairs protein folding; does not
FT interact with RARS1; results in reduced protein solubility;
FT dbSNP:rs587777332)"
FT /evidence="ECO:0000269|PubMed:24656866,
FT ECO:0000269|PubMed:26869582"
FT /id="VAR_071191"
FT VARIANT 515
FT /note="R -> W (in MSCCA; results in loss of glutaminyl-tRNA
FT aminoacylation activity; impairs protein folding; results
FT in reduced protein solubility; dbSNP:rs587777334)"
FT /evidence="ECO:0000269|PubMed:24656866,
FT ECO:0000269|PubMed:26869582"
FT /id="VAR_071192"
FT MUTAGEN 175
FT /note="H->A: Decreases catalytic efficiency about 60-fold."
FT /evidence="ECO:0000269|PubMed:26869582"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 27..42
FT /evidence="ECO:0007829|PDB:4YE6"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 119..140
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 278..293
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:4YE6"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 380..391
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:4YE6"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 438..448
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 452..457
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 464..473
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 496..504
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 519..524
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 529..539
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 551..564
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 570..576
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 592..594
FT /evidence="ECO:0007829|PDB:4YE6"
FT HELIX 599..601
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 603..606
FT /evidence="ECO:0007829|PDB:4YE9"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:4YE6"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 647..650
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 681..683
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 685..692
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 695..700
FT /evidence="ECO:0007829|PDB:4YE6"
FT TURN 702..705
FT /evidence="ECO:0007829|PDB:4YE6"
FT TURN 711..714
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 725..728
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 740..743
FT /evidence="ECO:0007829|PDB:4YE6"
FT TURN 744..746
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 747..751
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:4YE6"
FT STRAND 761..766
FT /evidence="ECO:0007829|PDB:4YE6"
SQ SEQUENCE 775 AA; 87799 MW; ADDE23E6C442FF73 CRC64;
MAALDSLSLF TSLGLSEQKA RETLKNSALS AQLREAATQA QQTLGSTIDK ATGILLYGLA
SRLRDTRRLS FLVSYIASKK IHTEPQLSAA LEYVRSHPLD PIDTVDFERE CGVGVIVTPE
QIEEAVEAAI NRHRPQLLVE RYHFNMGLLM GEARAVLKWA DGKMIKNEVD MQVLHLLGPK
LEADLEKKFK VAKARLEETD RRTAKDVVEN GETADQTLSL MEQLRGEALK FHKPGENYKT
PGYVVTPHTM NLLKQHLEIT GGQVRTRFPP EPNGILHIGH AKAINFNFGY AKANNGICFL
RFDDTNPEKE EAKFFTAICD MVAWLGYTPY KVTYASDYFD QLYAWAVELI RRGLAYVCHQ
RGEELKGHNT LPSPWRDRPM EESLLLFEAM RKGKFSEGEA TLRMKLVMED GKMDPVAYRV
KYTPHHRTGD KWCIYPTYDY THCLCDSIEH ITHSLCTKEF QARRSSYFWL CNALDVYCPV
QWEYGRLNLH YAVVSKRKIL QLVATGAVRD WDDPRLFTLT ALRRRGFPPE AINNFCARVG
VTVAQTTMEP HLLEACVRDV LNDTAPRAMA VLESLRVIIT NFPAAKSLDI QVPNFPADET
KGFHQVPFAP IVFIERTDFK EEPEPGFKRL AWGQPVGLRH TGYVIELQHV VKGPSGCVES
LEVTCRRADA GEKPKAFIHW VSQPLMCEVR LYERLFQHKN PEDPTEVPGG FLSDLNLASL
HVVDAALVDC SVALAKPFDK FQFERLGYFS VDPDSHQGKL VFNRTVTLKE DPGKV
