SYMC_HUMAN
ID SYMC_HUMAN Reviewed; 900 AA.
AC P56192; B3KVK7; Q14895; Q53H14; Q96A15; Q96BZ0; Q9NSE0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Methionine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.10 {ECO:0000269|PubMed:11714285};
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=MARS1 {ECO:0000312|HGNC:HGNC:6898}; Synonyms=MARS;
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=Gastric carcinoma;
RX PubMed=8921912; DOI=10.1016/0378-1119(96)00313-7;
RA Lage H., Dietel M.;
RT "Cloning of a human cDNA encoding a protein with high homology to yeast
RT methionyl-tRNA synthetase.";
RL Gene 178:187-189(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Motegi H., Noda T., Shiba K.;
RT "Cloning and sequence determination of a human cytoplasmic methionyl-tRNA
RT synthetase gene.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Colon, and Muscle;
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 [8]
RP FUNCTION, AND 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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS
RP OF ARG-857; LYS-860; LYS-863; LYS-866 AND LYS-880.
RX PubMed=11714285; DOI=10.1021/bi015670b;
RA Kaminska M., Shalak V., Mirande M.;
RT "The appended C-domain of human methionyl-tRNA synthetase has a tRNA-
RT sequestering function.";
RL Biochemistry 40:14309-14316(2001).
RN [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP IDENTIFICATION BY 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [14]
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 [15]
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP INVOLVEMENT IN CMT2U, VARIANT CMT2U CYS-618, AND CHARACTERIZATION OF
RP VARIANT CMT2U CYS-618.
RX PubMed=23729695; DOI=10.1136/jnnp-2013-305049;
RG Inherited Neuropathy Consortium;
RA Gonzalez M., McLaughlin H., Houlden H., Guo M., Yo-Tsen L.,
RA Hadjivassilious M., Speziani F., Yang X.L., Antonellis A., Reilly M.M.,
RA Zuchner S.;
RT "Exome sequencing identifies a significant variant in methionyl-tRNA
RT synthetase (MARS) in a family with late-onset CMT2.";
RL J. Neurol. Neurosurg. Psych. 84:1247-1249(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [21]
RP INVOLVEMENT IN CMT2U, AND VARIANT CMT2U THR-800.
RX PubMed=24354524; DOI=10.1111/cge.12327;
RA Hyun Y.S., Park H.J., Heo S.H., Yoon B.R., Nam S.H., Kim S.B., Park C.I.,
RA Choi B.O., Chung K.W.;
RT "Rare variants in methionyl- and tyrosyl-tRNA synthetase genes in late-
RT onset autosomal dominant Charcot-Marie-Tooth neuropathy.";
RL Clin. Genet. 86:592-594(2014).
RN [22]
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 [23]
RP STRUCTURE BY NMR OF 835-900.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the WHEP-TRS domain of human methionyl-tRNA
RT synthetase.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [24] {ECO:0007744|PDB:4BL7}
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 1-224 IN COMPLEX WITH EEF1E1.
RA Cho H.Y., Seo W.W., Cho H.J., Kang B.S.;
RT "Crystal Structure of the Aimp3-Mrs N-Terminal Domain Complex in Different
RT Space Group.";
RL Submitted (MAY-2013) to the PDB data bank.
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-207 IN COMPLEX WITH EEF1E1,
RP INTERACTION WITH EEF1E1, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ALA-64 AND GLU-86.
RX PubMed=26472928; DOI=10.1074/jbc.m115.690867;
RA Cho H.Y., Maeng S.J., Cho H.J., Choi Y.S., Chung J.M., Lee S., Kim H.K.,
RA Kim J.H., Eom C.Y., Kim Y.G., Guo M., Jung H.S., Kang B.S., Kim S.;
RT "Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione
RT Transferase-homology Domains.";
RL J. Biol. Chem. 290:29313-29328(2015).
RN [26]
RP INVOLVEMENT IN ILLD, AND VARIANTS ILLD LEU-370 AND THR-523.
RX PubMed=24103465; DOI=10.1186/1471-2350-14-106;
RA van Meel E., Wegner D.J., Cliften P., Willing M.C., White F.V.,
RA Kornfeld S., Cole F.S.;
RT "Rare recessive loss-of-function methionyl-tRNA synthetase mutations
RT presenting as a multi-organ phenotype.";
RL BMC Med. Genet. 14:106-106(2013).
RN [27]
RP VARIANTS MET-5 AND TRP-702.
RX PubMed=24482476; DOI=10.1126/science.1247363;
RA Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
RA Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L., Masri A.,
RA Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A., Kara M.,
RA Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F., Mahmoud I.G.,
RA Bouslam N., Bouhouche A., Benomar A., Hanein S., Raymond L., Forlani S.,
RA Mascaro M., Selim L., Shehata N., Al-Allawi N., Bindu P.S., Azam M.,
RA Gunel M., Caglayan A., Bilguvar K., Tolun A., Issa M.Y., Schroth J.,
RA Spencer E.G., Rosti R.O., Akizu N., Vaux K.K., Johansen A., Koh A.A.,
RA Megahed H., Durr A., Brice A., Stevanin G., Gabriel S.B., Ideker T.,
RA Gleeson J.G.;
RT "Exome sequencing links corticospinal motor neuron disease to common
RT neurodegenerative disorders.";
RL Science 343:506-511(2014).
RN [28]
RP VARIANTS ILLD CYS-344; THR-393; LEU-567 AND VAL-605, AND VARIANTS LEU-206
RP AND GLN-727.
RX PubMed=25913036; DOI=10.1016/j.ajhg.2015.03.010;
RA Hadchouel A., Wieland T., Griese M., Baruffini E., Lorenz-Depiereux B.,
RA Enaud L., Graf E., Dubus J.C., Halioui-Louhaichi S., Coulomb A.,
RA Delacourt C., Eckstein G., Zarbock R., Schwarzmayr T., Cartault F.,
RA Meitinger T., Lodi T., de Blic J., Strom T.M.;
RT "Biallelic mutations of methionyl-tRNA synthetase cause a specific type of
RT pulmonary alveolar proteinosis prevalent on Reunion island.";
RL Am. J. Hum. Genet. 96:826-831(2015).
CC -!- FUNCTION: Catalyzes the specific attachment of an amino acid to its
CC cognate tRNA in a 2 step reaction: the amino acid (AA) is first
CC activated by ATP to form AA-AMP and then transferred to the acceptor
CC end of the tRNA (PubMed:11714285). Plays a role in the synthesis of
CC ribosomal RNA in the nucleolus (PubMed:10791971).
CC {ECO:0000269|PubMed:10791971, ECO:0000269|PubMed:11714285}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10;
CC Evidence={ECO:0000269|PubMed:11714285};
CC -!- ACTIVITY REGULATION: Enzyme activity is increased by spermidine,
CC EEF1A1, and when the Mg(2+) concentration is increased from 5 mM to 13
CC mM (in vitro), possibly by promoting the dissociation of the complex
CC between the enzyme and its product. {ECO:0000269|PubMed:11714285}.
CC -!- SUBUNIT: Monomer (PubMed:11714285). 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, Ref.24,
CC PubMed:26472928). Forms a linear complex that contains MARS1, EEF1E1,
CC EPRS1 and AIMP2 that is at the core of the multisubunit complex
CC (PubMed:26472928). {ECO:0000269|PubMed:11714285,
CC ECO:0000269|PubMed:19131329, ECO:0000269|PubMed:19289464,
CC ECO:0000269|PubMed:26472928, ECO:0000269|Ref.24}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10791971,
CC ECO:0000269|PubMed:19289464, ECO:0000305|PubMed:26472928}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:10791971}. Note=Localizes to the
CC nucleolus in proliferative cells but disappears in quiescent cells.
CC {ECO:0000269|PubMed:10791971}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P56192-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P56192-2; Sequence=VSP_056563, VSP_056564;
CC -!- DISEASE: Interstitial lung and liver disease (ILLD) [MIM:615486]: An
CC autosomal recessive, life-threatening disorder characterized by
CC respiratory insufficiency and progressive liver disease with onset in
CC infancy or early childhood. Clinical features include failure to
CC thrive, hypotonia, intermittent lactic acidosis, aminoaciduria,
CC hypothyroidism, interstitial lung disease, pulmonary alveolar
CC proteinosis, anemia, and liver canalicular cholestasis, steatosis, and
CC iron deposition. {ECO:0000269|PubMed:24103465,
CC ECO:0000269|PubMed:25913036}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Charcot-Marie-Tooth disease 2U (CMT2U) [MIM:616280]: An axonal
CC form of Charcot-Marie-Tooth disease, a disorder of the peripheral
CC nervous system, characterized by progressive weakness and atrophy,
CC initially of the peroneal muscles and later of the distal muscles of
CC the arms. Charcot-Marie-Tooth disease is classified in two main groups
CC on the basis of electrophysiologic properties and histopathology:
CC primary peripheral demyelinating neuropathies (designated CMT1 when
CC they are dominantly inherited) and primary peripheral axonal
CC neuropathies (CMT2). Neuropathies of the CMT2 group are characterized
CC by signs of axonal degeneration in the absence of obvious myelin
CC alterations, normal or slightly reduced nerve conduction velocities,
CC and progressive distal muscle weakness and atrophy. CMT2U is a slowly
CC progressive, autosomal dominant form characterized by late-adult onset.
CC {ECO:0000269|PubMed:23729695, ECO:0000269|PubMed:24354524}. 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; X94754; CAA64381.1; -; mRNA.
DR EMBL; Z49216; CAA89153.1; -; mRNA.
DR EMBL; D84224; BAA95668.1; -; mRNA.
DR EMBL; BT007338; AAP36002.1; -; mRNA.
DR EMBL; AK122956; BAG53819.1; -; mRNA.
DR EMBL; AK222767; BAD96487.1; -; mRNA.
DR EMBL; AC022506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002384; AAH02384.1; -; mRNA.
DR EMBL; BC006328; AAH06328.1; -; mRNA.
DR EMBL; BC011639; AAH11639.1; -; mRNA.
DR EMBL; BC011849; AAH11849.1; -; mRNA.
DR EMBL; BC015011; AAH15011.1; -; mRNA.
DR CCDS; CCDS8942.1; -. [P56192-1]
DR PIR; JC5224; JC5224.
DR RefSeq; NP_004981.2; NM_004990.3. [P56192-1]
DR PDB; 2DJV; NMR; -; A=835-900.
DR PDB; 4BL7; X-ray; 1.89 A; A=1-224.
DR PDB; 4BVX; X-ray; 1.60 A; A=1-207.
DR PDB; 4BVY; X-ray; 1.99 A; A=1-225.
DR PDB; 5GL7; X-ray; 2.01 A; A=221-834.
DR PDB; 5GOY; X-ray; 2.28 A; A=221-834.
DR PDB; 5Y6L; X-ray; 2.90 A; A=1-224.
DR PDBsum; 2DJV; -.
DR PDBsum; 4BL7; -.
DR PDBsum; 4BVX; -.
DR PDBsum; 4BVY; -.
DR PDBsum; 5GL7; -.
DR PDBsum; 5GOY; -.
DR PDBsum; 5Y6L; -.
DR AlphaFoldDB; P56192; -.
DR BMRB; P56192; -.
DR SMR; P56192; -.
DR BioGRID; 110311; 239.
DR CORUM; P56192; -.
DR DIP; DIP-38164N; -.
DR IntAct; P56192; 54.
DR MINT; P56192; -.
DR STRING; 9606.ENSP00000262027; -.
DR BindingDB; P56192; -.
DR ChEMBL; CHEMBL2870; -.
DR DrugBank; DB00134; Methionine.
DR MoonProt; P56192; -.
DR CarbonylDB; P56192; -.
DR GlyGen; P56192; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P56192; -.
DR MetOSite; P56192; -.
DR PhosphoSitePlus; P56192; -.
DR SwissPalm; P56192; -.
DR BioMuta; MARS; -.
DR DMDM; 20178332; -.
DR CPTAC; CPTAC-538; -.
DR CPTAC; CPTAC-539; -.
DR EPD; P56192; -.
DR jPOST; P56192; -.
DR MassIVE; P56192; -.
DR MaxQB; P56192; -.
DR PaxDb; P56192; -.
DR PeptideAtlas; P56192; -.
DR PRIDE; P56192; -.
DR ProteomicsDB; 3760; -.
DR ProteomicsDB; 56902; -. [P56192-1]
DR ABCD; P56192; 1 sequenced antibody.
DR Antibodypedia; 1110; 177 antibodies from 29 providers.
DR DNASU; 4141; -.
DR Ensembl; ENST00000262027.10; ENSP00000262027.5; ENSG00000166986.15. [P56192-1]
DR Ensembl; ENST00000537638.6; ENSP00000446168.2; ENSG00000166986.15. [P56192-2]
DR GeneID; 4141; -.
DR KEGG; hsa:4141; -.
DR MANE-Select; ENST00000262027.10; ENSP00000262027.5; NM_004990.4; NP_004981.2.
DR UCSC; uc001sof.2; human. [P56192-1]
DR CTD; 4141; -.
DR DisGeNET; 4141; -.
DR GeneCards; MARS1; -.
DR GeneReviews; MARS1; -.
DR HGNC; HGNC:6898; MARS1.
DR HPA; ENSG00000166986; Low tissue specificity.
DR MalaCards; MARS1; -.
DR MIM; 156560; gene.
DR MIM; 615486; phenotype.
DR MIM; 616280; phenotype.
DR neXtProt; NX_P56192; -.
DR OpenTargets; ENSG00000166986; -.
DR Orphanet; 397735; Autosomal dominant Charcot-Marie-Tooth disease type 2U.
DR Orphanet; 401835; Autosomal recessive spastic paraplegia type 70.
DR Orphanet; 440427; Severe early-onset pulmonary alveolar proteinosis due to MARS deficiency.
DR PharmGKB; PA30642; -.
DR VEuPathDB; HostDB:ENSG00000166986; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1247; Eukaryota.
DR GeneTree; ENSGT00550000075017; -.
DR HOGENOM; CLU_009710_3_2_1; -.
DR InParanoid; P56192; -.
DR OMA; HGNGYMQ; -.
DR OrthoDB; 333013at2759; -.
DR PhylomeDB; P56192; -.
DR TreeFam; TF300526; -.
DR BRENDA; 6.1.1.10; 2681.
DR PathwayCommons; P56192; -.
DR Reactome; R-HSA-2408522; Selenoamino acid metabolism.
DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
DR SignaLink; P56192; -.
DR SIGNOR; P56192; -.
DR BioGRID-ORCS; 4141; 787 hits in 1084 CRISPR screens.
DR ChiTaRS; MARS; human.
DR EvolutionaryTrace; P56192; -.
DR GeneWiki; MARS_(gene); -.
DR GenomeRNAi; 4141; -.
DR Pharos; P56192; Tchem.
DR PRO; PR:P56192; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P56192; protein.
DR Bgee; ENSG00000166986; Expressed in right hemisphere of cerebellum and 204 other tissues.
DR ExpressionAtlas; P56192; baseline and differential.
DR Genevisible; P56192; HS.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:CAFA.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:CAFA.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IDA:UniProtKB.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:CAFA.
DR GO; GO:0009303; P:rRNA transcription; IMP:CAFA.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.20.28.20; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR041598; MARS_N.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR029038; MetRS_Zn.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR PANTHER; PTHR45765; PTHR45765; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF18485; GST_N_5; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF57770; SSF57770; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding;
KW Charcot-Marie-Tooth disease; Cytoplasm; Disease variant; Ligase;
KW Neurodegeneration; Neuropathy; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..900
FT /note="Methionine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000139262"
FT DOMAIN 74..198
FT /note="GST C-terminal"
FT DOMAIN 841..897
FT /note="WHEP-TRS"
FT MOTIF 273..283
FT /note="'HIGH' region"
FT MOTIF 593..597
FT /note="'KMSKS' region"
FT BINDING 596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FL6"
FT MOD_RES 835
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68FL6"
FT VAR_SEQ 546
FT /note="V -> P (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056563"
FT VAR_SEQ 547..900
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056564"
FT VARIANT 5
FT /note="V -> M (found in a patient with spastic paraplegia;
FT unknown pathological significance; dbSNP:rs587777227)"
FT /evidence="ECO:0000269|PubMed:24482476"
FT /id="VAR_077848"
FT VARIANT 206
FT /note="P -> L (in dbSNP:rs138776588)"
FT /evidence="ECO:0000269|PubMed:25913036"
FT /id="VAR_075360"
FT VARIANT 344
FT /note="Y -> C (in ILLD; when assayed in yeast, induces a
FT slight growth retardation and reduction in methionine
FT incorporation; may interfere with efficient substrate
FT binding; dbSNP:rs766466297)"
FT /evidence="ECO:0000269|PubMed:25913036"
FT /id="VAR_075361"
FT VARIANT 370
FT /note="F -> L (in ILLD; dbSNP:rs140467171)"
FT /evidence="ECO:0000269|PubMed:24103465"
FT /id="VAR_070872"
FT VARIANT 393
FT /note="A -> T (in ILLD; may act as a disease modifier
FT aggravating the phenotype; found in patients that carried
FT additional mutations C-344 and/or L-567; when assayed in
FT yeast, does not exhibit any phenotype; when assayed in
FT yeast in association with L-567, increases L-567-induced
FT growth retardation and reduction in methionine
FT incorporation; dbSNP:rs141340466)"
FT /evidence="ECO:0000269|PubMed:25913036"
FT /id="VAR_075362"
FT VARIANT 523
FT /note="I -> T (in ILLD; dbSNP:rs201555303)"
FT /evidence="ECO:0000269|PubMed:24103465"
FT /id="VAR_070873"
FT VARIANT 567
FT /note="S -> L (in ILLD; when assayed in yeast, reduces
FT methionine incorporation; when assayed in yeast in
FT association with T-393, induces growth retardation and
FT strong reduction in methionine incorporation; may interfere
FT with efficient substrate binding; dbSNP:rs143592405)"
FT /evidence="ECO:0000269|PubMed:25913036"
FT /id="VAR_075363"
FT VARIANT 605
FT /note="D -> V (in ILLD; when assayed in yeast, induces a
FT slight growth retardation and reduction in methionine
FT incorporation; may interfere with efficient substrate
FT binding; dbSNP:rs756021768)"
FT /evidence="ECO:0000269|PubMed:25913036"
FT /id="VAR_075364"
FT VARIANT 618
FT /note="R -> C (in CMT2U; loss of function mutation;
FT dbSNP:rs587777718)"
FT /evidence="ECO:0000269|PubMed:23729695"
FT /id="VAR_073377"
FT VARIANT 683
FT /note="A -> D (in dbSNP:rs1054403)"
FT /id="VAR_020459"
FT VARIANT 702
FT /note="R -> W (found in a patient with spastic paraplegia;
FT unknown pathological significance; dbSNP:rs587777228)"
FT /evidence="ECO:0000269|PubMed:24482476"
FT /id="VAR_077849"
FT VARIANT 727
FT /note="R -> Q (in dbSNP:rs113808165)"
FT /evidence="ECO:0000269|PubMed:25913036"
FT /id="VAR_075365"
FT VARIANT 800
FT /note="P -> T (in CMT2U; dbSNP:rs781249411)"
FT /evidence="ECO:0000269|PubMed:24354524"
FT /id="VAR_073378"
FT MUTAGEN 64
FT /note="A->R: Loss of interaction with EEF1E1."
FT /evidence="ECO:0000269|PubMed:26472928"
FT MUTAGEN 86
FT /note="E->R: Loss of interaction with EEF1E1."
FT /evidence="ECO:0000269|PubMed:26472928"
FT MUTAGEN 857
FT /note="R->A: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:11714285"
FT MUTAGEN 860
FT /note="K->A: Strongly decreased affinity for tRNA."
FT /evidence="ECO:0000269|PubMed:11714285"
FT MUTAGEN 863
FT /note="K->A: Slightly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:11714285"
FT MUTAGEN 866
FT /note="K->A: Slightly decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:11714285"
FT MUTAGEN 880
FT /note="K->A: Strongly decreased affinity for tRNA."
FT /evidence="ECO:0000269|PubMed:11714285"
FT CONFLICT 53
FT /note="L -> V (in Ref. 1; CAA64381)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> P (in Ref. 1; CAA64381)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="L -> Q (in Ref. 1; CAA64381)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="W -> S (in Ref. 7; AAH15011)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="L -> P (in Ref. 5; BAD96487)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="A -> G (in Ref. 1; CAA64381/CAA89153)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 12..18
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:4BVX"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:4BVX"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4BVX"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:4BVX"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:4BVX"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 329..346
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 360..374
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 379..389
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 390..393
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 443..452
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 454..468
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 517..520
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 524..532
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 534..536
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 537..540
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 546..553
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 557..561
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 563..571
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 578..584
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 596..599
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 604..606
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 607..610
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 614..623
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 627..629
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 635..645
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 646..649
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 650..664
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 676..696
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 697..699
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 701..722
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 724..727
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 732..755
FT /evidence="ECO:0007829|PDB:5GL7"
FT TURN 756..759
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 761..771
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 775..778
FT /evidence="ECO:0007829|PDB:5GL7"
FT HELIX 807..816
FT /evidence="ECO:0007829|PDB:5GL7"
FT STRAND 817..819
FT /evidence="ECO:0007829|PDB:5GOY"
FT HELIX 838..861
FT /evidence="ECO:0007829|PDB:2DJV"
FT HELIX 866..887
FT /evidence="ECO:0007829|PDB:2DJV"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:2DJV"
FT STRAND 897..899
FT /evidence="ECO:0007829|PDB:2DJV"
SQ SEQUENCE 900 AA; 101116 MW; 3D687C77E17C5C96 CRC64;
MRLFVSDGVP GCLPVLAAAG RARGRAEVLI STVGPEDCVV PFLTRPKVPV LQLDSGNYLF
STSAICRYFF LLSGWEQDDL TNQWLEWEAT ELQPALSAAL YYLVVQGKKG EDVLGSVRRA
LTHIDHSLSR QNCPFLAGET ESLADIVLWG ALYPLLQDPA YLPEELSALH SWFQTLSTQE
PCQRAAETVL KQQGVLALRP YLQKQPQPSP AEGRAVTNEP EEEELATLSE EEIAMAVTAW
EKGLESLPPL RPQQNPVLPV AGERNVLITS ALPYVNNVPH LGNIIGCVLS ADVFARYSRL
RQWNTLYLCG TDEYGTATET KALEEGLTPQ EICDKYHIIH ADIYRWFNIS FDIFGRTTTP
QQTKITQDIF QQLLKRGFVL QDTVEQLRCE HCARFLADRF VEGVCPFCGY EEARGDQCDK
CGKLINAVEL KKPQCKVCRS CPVVQSSQHL FLDLPKLEKR LEEWLGRTLP GSDWTPNAQF
ITRSWLRDGL KPRCITRDLK WGTPVPLEGF EDKVFYVWFD ATIGYLSITA NYTDQWERWW
KNPEQVDLYQ FMAKDNVPFH SLVFPCSALG AEDNYTLVSH LIATEYLNYE DGKFSKSRGV
GVFGDMAQDT GIPADIWRFY LLYIRPEGQD SAFSWTDLLL KNNSELLNNL GNFINRAGMF
VSKFFGGYVP EMVLTPDDQR LLAHVTLELQ HYHQLLEKVR IRDALRSILT ISRHGNQYIQ
VNEPWKRIKG SEADRQRAGT VTGLAVNIAA LLSVMLQPYM PTVSATIQAQ LQLPPPACSI
LLTNFLCTLP AGHQIGTVSP LFQKLENDQI ESLRQRFGGG QAKTSPKPAV VETVTTAKPQ
QIQALMDEVT KQGNIVRELK AQKADKNEVA AEVAKLLDLK KQLAVAEGKP PEAPKGKKKK
