SYAC_HUMAN
ID SYAC_HUMAN Reviewed; 968 AA.
AC P49588; A6NF14; B4DR45; Q53GV7; Q96FA0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Alanine--tRNA ligase, cytoplasmic {ECO:0000255|HAMAP-Rule:MF_03133};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:25817015, ECO:0000269|PubMed:27622773, ECO:0000269|PubMed:27911835, ECO:0000269|PubMed:28493438};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03133};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133};
DE AltName: Full=Renal carcinoma antigen NY-REN-42;
GN Name=AARS1; Synonyms=AARS {ECO:0000255|HAMAP-Rule:MF_03133};
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).
RX PubMed=7654687; DOI=10.1021/bi00033a004;
RA Shiba K., Ripmaster T.L., Suzuki N., Nichols R., Plotz P., Noda T.,
RA Schimmel P.;
RT "Human alanyl-tRNA synthetase: conservation in evolution of catalytic core
RT and microhelix recognition.";
RL Biochemistry 34:10340-10349(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [7]
RP PROTEIN SEQUENCE OF 1-11; 304-320 AND 684-695, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [9]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [12]
RP DOMAIN EXCHANGE EXPERIMENTS.
RX PubMed=19661429; DOI=10.1126/science.1174343;
RA Guo M., Chong Y.E., Beebe K., Shapiro R., Yang X.-L., Schimmel P.;
RT "The C-Ala domain brings together editing and aminoacylation functions on
RT one tRNA.";
RL Science 325:744-747(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-876, AND
RP IDENTIFICATION BY MASS 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND IDENTIFICATION BY
RP 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 [15]
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-8 AND SER-555, AND
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 [19]
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 [20]
RP BIOPHYSICOCHEMICAL PROPERTIES, INVOLVEMENT IN DEE29, VARIANTS DEE29 THR-81
RP AND GLY-751, CHARACTERIZATION OF VARIANTS DEE29 THR-81 AND GLY-751, AND
RP CATALYTIC ACTIVITY.
RX PubMed=25817015; DOI=10.1016/j.ajhg.2015.02.012;
RA Simons C., Griffin L.B., Helman G., Golas G., Pizzino A., Bloom M.,
RA Murphy J.L., Crawford J., Evans S.H., Topper S., Whitehead M.T.,
RA Schreiber J.M., Chapman K.A., Tifft C., Lu K.B., Gamper H., Shigematsu M.,
RA Taft R.J., Antonellis A., Hou Y.M., Vanderver A.;
RT "Loss-of-function alanyl-tRNA synthetase mutations cause an autosomal-
RT recessive early-onset epileptic encephalopathy with persistent myelination
RT defect.";
RL Am. J. Hum. Genet. 96:675-681(2015).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22] {ECO:0007744|PDB:4XEM}
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 1-455 IN COMPLEX WITH
RP L-ALANINYL-ADENYLATE ANALOG.
RA Zhou H., Yang X.L.;
RT "Crystal structure of wild type human AlaRS catalytic domain.";
RL Submitted (DEC-2014) to the PDB data bank.
RN [23] {ECO:0007744|PDB:5KNN}
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 4-453 IN COMPLEX WITH
RP L-ALANINYL-ADENYLATE ANALOG, CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS
RP OF ALA-448.
RX PubMed=27622773; DOI=10.1021/jacs.6b07121;
RA Sun L., Gomes A.C., He W., Zhou H., Wang X., Pan D.W., Schimmel P., Pan T.,
RA Yang X.L.;
RT "Evolutionary Gain of Alanine Mischarging to Noncognate tRNAs with a G4:U69
RT Base Pair.";
RL J. Am. Chem. Soc. 138:12948-12955(2016).
RN [24] {ECO:0007744|PDB:5T5S, ECO:0007744|PDB:5T76}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 757-965, CATALYTIC ACTIVITY,
RP FUNCTION, DOMAIN, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=27911835; DOI=10.1073/pnas.1617316113;
RA Sun L., Song Y., Blocquel D., Yang X.L., Schimmel P.;
RT "Two crystal structures reveal design for repurposing the C-Ala domain of
RT human AlaRS.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:14300-14305(2016).
RN [25]
RP VARIANT CMT2N HIS-329.
RX PubMed=20045102; DOI=10.1016/j.ajhg.2009.12.005;
RA Latour P., Thauvin-Robinet C., Baudelet-Mery C., Soichot P., Cusin V.,
RA Faivre L., Locatelli M.C., Mayencon M., Sarcey A., Broussolle E., Camu W.,
RA David A., Rousson R.;
RT "A major determinant for binding and aminoacylation of tRNA(Ala) in
RT cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-
RT Marie-Tooth disease.";
RL Am. J. Hum. Genet. 86:77-82(2010).
RN [26]
RP VARIANT CMT2N TYR-71.
RX PubMed=22206013; DOI=10.1371/journal.pone.0029393;
RA Lin K.P., Soong B.W., Yang C.C., Huang L.W., Chang M.H., Lee I.H.,
RA Antonellis A., Lee Y.C.;
RT "The mutational spectrum in a cohort of Charcot-Marie-Tooth disease type 2
RT among the Han Chinese in Taiwan.";
RL PLoS ONE 6:E29393-E29393(2011).
RN [27]
RP VARIANT CMT2N HIS-329, AND CHARACTERIZATION OF VARIANT CMT2N HIS-329.
RX PubMed=22009580; DOI=10.1002/humu.21635;
RA McLaughlin H.M., Sakaguchi R., Giblin W., Wilson T.E., Biesecker L.,
RA Lupski J.R., Talbot K., Vance J.M., Zuchner S., Lee Y.C., Kennerson M.,
RA Hou Y.M., Nicholson G., Antonellis A.;
RT "A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation in
RT patients with Charcot-Marie-Tooth disease type 2N (CMT2N).";
RL Hum. Mutat. 33:244-253(2012).
RN [28]
RP VARIANT MET-608.
RX PubMed=24627108; DOI=10.1007/s00415-014-7289-8;
RA Schabhuettl M., Wieland T., Senderek J., Baets J., Timmerman V.,
RA De Jonghe P., Reilly M.M., Stieglbauer K., Laich E., Windhager R., Erwa W.,
RA Trajanoski S., Strom T.M., Auer-Grumbach M.;
RT "Whole-exome sequencing in patients with inherited neuropathies: outcome
RT and challenges.";
RL J. Neurol. 261:970-982(2014).
RN [29]
RP VARIANT DEE29 ASP-913, CHARACTERIZATION OF VARIANT DEE29 ASP-913, FUNCTION,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-723.
RX PubMed=28493438; DOI=10.1002/humu.23250;
RA Nakayama T., Wu J., Galvin-Parton P., Weiss J., Andriola M.R., Hill R.S.,
RA Vaughan D.J., El-Quessny M., Barry B.J., Partlow J.N., Barkovich A.J.,
RA Ling J., Mochida G.H.;
RT "Deficient activity of alanyl-tRNA synthetase underlies an autosomal
RT recessive syndrome of progressive microcephaly, hypomyelination, and
RT epileptic encephalopathy.";
RL Hum. Mutat. 38:1348-1354(2017).
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala) (PubMed:27622773,
CC PubMed:27911835, PubMed:28493438). Also edits incorrectly charged
CC tRNA(Ala) via its editing domain (PubMed:27622773, PubMed:27911835,
CC PubMed:28493438). {ECO:0000255|HAMAP-Rule:MF_03133,
CC ECO:0000269|PubMed:27622773, ECO:0000269|PubMed:27911835,
CC ECO:0000269|PubMed:28493438}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03133,
CC ECO:0000269|PubMed:25817015, ECO:0000269|PubMed:27622773,
CC ECO:0000269|PubMed:27911835, ECO:0000269|PubMed:28493438};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03133};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03133};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 uM for tRNA(Ala) (at 37 Celsius)
CC {ECO:0000269|PubMed:25817015};
CC Note=kcat is 0.4 sec(-1). {ECO:0000269|PubMed:25817015};
CC -!- SUBUNIT: Monomer (PubMed:27911835). Interacts with ANKRD16; the
CC interaction is direct (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_03133, ECO:0000269|PubMed:27911835}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133,
CC ECO:0000269|PubMed:27911835}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49588-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49588-2; Sequence=VSP_057201, VSP_057202;
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- DOMAIN: The C-terminal C-Ala domain (residues 756 to 968) is not
CC required for catalytic activity and can bind DNA (in vitro)
CC (PubMed:27911835). The C-terminal C-Ala domain (residues 756 to 968),
CC along with tRNA(Ala), serves as a bridge to cooperatively bring
CC together the editing and aminoacylation centers thus stimulating
CC deacylation of misacylated tRNAs. The human domain can be used in vitro
CC to replace the corresponding domain in E.coli (PubMed:19661429).
CC {ECO:0000269|PubMed:19661429, ECO:0000269|PubMed:27911835}.
CC -!- PTM: ISGylated. {ECO:0000255|HAMAP-Rule:MF_03133,
CC ECO:0000269|PubMed:16139798}.
CC -!- DISEASE: Charcot-Marie-Tooth disease 2N (CMT2N) [MIM:613287]: 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.
CC {ECO:0000269|PubMed:20045102, ECO:0000269|PubMed:22009580,
CC ECO:0000269|PubMed:22206013}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Developmental and epileptic encephalopathy 29 (DEE29)
CC [MIM:616339]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE29 patients manifest severe infantile epileptic
CC encephalopathy, clubfoot, absent deep tendon reflexes, extrapyramidal
CC symptoms, and persistently deficient myelination.
CC {ECO:0000269|PubMed:25817015, ECO:0000269|PubMed:28493438}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
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DR EMBL; D32050; BAA06808.1; -; mRNA.
DR EMBL; AK299098; BAG61157.1; -; mRNA.
DR EMBL; AK222824; BAD96544.1; -; mRNA.
DR EMBL; AC012184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471241; EAW51839.1; -; Genomic_DNA.
DR EMBL; BC011451; AAH11451.1; -; mRNA.
DR CCDS; CCDS32474.1; -. [P49588-1]
DR PIR; I60107; I60107.
DR RefSeq; NP_001596.2; NM_001605.2. [P49588-1]
DR PDB; 4XEM; X-ray; 1.28 A; A=1-455.
DR PDB; 4XEO; X-ray; 1.38 A; A/B=1-455.
DR PDB; 5KNN; X-ray; 2.68 A; A/B/C/D/E/F/G/H=4-453.
DR PDB; 5T5S; X-ray; 2.20 A; A=757-965.
DR PDB; 5T76; X-ray; 2.00 A; A=757-965.
DR PDB; 5V59; X-ray; 2.03 A; A=1-455.
DR PDBsum; 4XEM; -.
DR PDBsum; 4XEO; -.
DR PDBsum; 5KNN; -.
DR PDBsum; 5T5S; -.
DR PDBsum; 5T76; -.
DR PDBsum; 5V59; -.
DR AlphaFoldDB; P49588; -.
DR SMR; P49588; -.
DR BioGRID; 106534; 124.
DR IntAct; P49588; 24.
DR MINT; P49588; -.
DR STRING; 9606.ENSP00000261772; -.
DR BindingDB; P49588; -.
DR ChEMBL; CHEMBL3574; -.
DR DrugBank; DB00160; Alanine.
DR GlyGen; P49588; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49588; -.
DR MetOSite; P49588; -.
DR PhosphoSitePlus; P49588; -.
DR SwissPalm; P49588; -.
DR BioMuta; AARS; -.
DR DMDM; 115502460; -.
DR CPTAC; CPTAC-1; -.
DR CPTAC; CPTAC-2; -.
DR EPD; P49588; -.
DR jPOST; P49588; -.
DR MassIVE; P49588; -.
DR MaxQB; P49588; -.
DR PaxDb; P49588; -.
DR PeptideAtlas; P49588; -.
DR PRIDE; P49588; -.
DR ProteomicsDB; 56022; -. [P49588-1]
DR ABCD; P49588; 3 sequenced antibodies.
DR Antibodypedia; 29958; 227 antibodies from 28 providers.
DR DNASU; 16; -.
DR Ensembl; ENST00000261772.13; ENSP00000261772.8; ENSG00000090861.17. [P49588-1]
DR Ensembl; ENST00000674691.1; ENSP00000502247.1; ENSG00000090861.17. [P49588-1]
DR Ensembl; ENST00000674963.1; ENSP00000501924.1; ENSG00000090861.17. [P49588-1]
DR Ensembl; ENST00000675643.1; ENSP00000502797.1; ENSG00000090861.17. [P49588-1]
DR GeneID; 16; -.
DR KEGG; hsa:16; -.
DR MANE-Select; ENST00000261772.13; ENSP00000261772.8; NM_001605.3; NP_001596.2.
DR UCSC; uc002eyn.2; human. [P49588-1]
DR CTD; 16; -.
DR DisGeNET; 16; -.
DR GeneCards; AARS1; -.
DR GeneReviews; AARS1; -.
DR HGNC; HGNC:20; AARS1.
DR HPA; ENSG00000090861; Low tissue specificity.
DR MalaCards; AARS1; -.
DR MIM; 601065; gene.
DR MIM; 613287; phenotype.
DR MIM; 616339; phenotype.
DR neXtProt; NX_P49588; -.
DR OpenTargets; ENSG00000090861; -.
DR Orphanet; 228174; Autosomal dominant Charcot-Marie-Tooth disease type 2N.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA24367; -.
DR VEuPathDB; HostDB:ENSG00000090861; -.
DR eggNOG; KOG0188; Eukaryota.
DR GeneTree; ENSGT00940000157335; -.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; P49588; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 129373at2759; -.
DR PhylomeDB; P49588; -.
DR TreeFam; TF300737; -.
DR PathwayCommons; P49588; -.
DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
DR SignaLink; P49588; -.
DR BioGRID-ORCS; 16; 782 hits in 1058 CRISPR screens.
DR ChiTaRS; AARS; human.
DR GenomeRNAi; 16; -.
DR Pharos; P49588; Tbio.
DR PRO; PR:P49588; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P49588; protein.
DR Bgee; ENSG00000090861; Expressed in endometrium epithelium and 211 other tissues.
DR ExpressionAtlas; P49588; baseline and differential.
DR Genevisible; P49588; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0002196; F:Ser-tRNA(Ala) hydrolase activity; ISS:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IEA:Ensembl.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IDA:UniProtKB.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0140018; P:regulation of cytoplasmic translational fidelity; IEA:Ensembl.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; TAS:ProtInc.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF101353; SSF101353; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase;
KW ATP-binding; Charcot-Marie-Tooth disease; Cytoplasm;
KW Direct protein sequencing; Disease variant; Epilepsy; Ligase;
KW Metal-binding; Neurodegeneration; Neuropathy; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Ubl conjugation; Zinc.
FT CHAIN 1..968
FT /note="Alanine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000075281"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27622773, ECO:0000269|Ref.22,
FT ECO:0007744|PDB:4XEM, ECO:0007744|PDB:4XEO,
FT ECO:0007744|PDB:5KNN"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27622773, ECO:0000269|Ref.22,
FT ECO:0007744|PDB:4XEM, ECO:0007744|PDB:4XEO,
FT ECO:0007744|PDB:5KNN"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27622773, ECO:0000269|Ref.22,
FT ECO:0007744|PDB:4XEM, ECO:0007744|PDB:4XEO,
FT ECO:0007744|PDB:5KNN"
FT BINDING 214..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27622773, ECO:0000269|Ref.22,
FT ECO:0007744|PDB:4XEM, ECO:0007744|PDB:4XEO,
FT ECO:0007744|PDB:5KNN"
FT BINDING 216
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000269|PubMed:27622773, ECO:0000269|Ref.22,
FT ECO:0007744|PDB:4XEM, ECO:0007744|PDB:4XEO,
FT ECO:0007744|PDB:5KNN"
FT BINDING 239
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000269|PubMed:27622773, ECO:0000269|Ref.22,
FT ECO:0007744|PDB:4XEM, ECO:0007744|PDB:4XEO,
FT ECO:0007744|PDB:5KNN"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27622773, ECO:0000269|Ref.22,
FT ECO:0007744|PDB:4XEM, ECO:0007744|PDB:4XEO,
FT ECO:0007744|PDB:5KNN"
FT BINDING 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 609
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 723
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 727
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133,
FT ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 876
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 160
FT /note="G -> GTYLYSFVR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057201"
FT VAR_SEQ 869
FT /note="K -> KATQGPGSPPLGLISSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057202"
FT VARIANT 71
FT /note="N -> Y (in CMT2N; dbSNP:rs387906792)"
FT /evidence="ECO:0000269|PubMed:22206013"
FT /id="VAR_067084"
FT VARIANT 81
FT /note="K -> T (in DEE29; hypomorphic allele; results in
FT only 2-fold reduction in aminoacylation efficiency;
FT dbSNP:rs786205157)"
FT /evidence="ECO:0000269|PubMed:25817015"
FT /id="VAR_073719"
FT VARIANT 275
FT /note="G -> D (in dbSNP:rs11537667)"
FT /id="VAR_028204"
FT VARIANT 329
FT /note="R -> H (in CMT2N; severely reduces enzyme activity;
FT dbSNP:rs267606621)"
FT /evidence="ECO:0000269|PubMed:20045102,
FT ECO:0000269|PubMed:22009580"
FT /id="VAR_063527"
FT VARIANT 608
FT /note="T -> M (found in a patient with distal hereditary
FT motor neuropathy; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:24627108"
FT /id="VAR_073293"
FT VARIANT 751
FT /note="R -> G (in DEE29; results in 10-fold reduction in
FT aminoacylation efficiency; dbSNP:rs143370729)"
FT /evidence="ECO:0000269|PubMed:25817015"
FT /id="VAR_073720"
FT VARIANT 913
FT /note="G -> D (in DEE29; decreases protein abundance;
FT decreases aminoacylation activity; no effect on the editing
FT activity; dbSNP:rs369774476)"
FT /evidence="ECO:0000269|PubMed:28493438"
FT /id="VAR_079703"
FT MUTAGEN 448
FT /note="A->Q: Decreases misincorporation of Cys instead of
FT Ala."
FT /evidence="ECO:0000269|PubMed:27622773"
FT MUTAGEN 723
FT /note="C->A: Decreases editing activity."
FT /evidence="ECO:0000269|PubMed:28493438"
FT CONFLICT 82
FT /note="H -> Q (in Ref. 1; BAA06808)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="Y -> C (in Ref. 2; BAG61157)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="A -> T (in Ref. 2; BAG61157)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="S -> T (in Ref. 3; BAD96544)"
FT /evidence="ECO:0000305"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:4XEM"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5KNN"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:4XEM"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:4XEM"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4XEO"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4XEM"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:4XEM"
FT STRAND 96..109
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4XEM"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4XEM"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:4XEM"
FT STRAND 178..195
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4XEM"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:4XEM"
FT STRAND 211..224
FT /evidence="ECO:0007829|PDB:4XEM"
FT STRAND 230..243
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4XEM"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 291..310
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 319..339
FT /evidence="ECO:0007829|PDB:4XEM"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 350..357
FT /evidence="ECO:0007829|PDB:4XEM"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 368..383
FT /evidence="ECO:0007829|PDB:4XEM"
FT HELIX 386..399
FT /evidence="ECO:0007829|PDB:5KNN"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:5KNN"
FT HELIX 408..416
FT /evidence="ECO:0007829|PDB:5KNN"
FT HELIX 422..431
FT /evidence="ECO:0007829|PDB:5KNN"
FT HELIX 438..450
FT /evidence="ECO:0007829|PDB:5KNN"
FT HELIX 759..782
FT /evidence="ECO:0007829|PDB:5T76"
FT HELIX 789..804
FT /evidence="ECO:0007829|PDB:5T76"
FT HELIX 809..851
FT /evidence="ECO:0007829|PDB:5T76"
FT STRAND 856..861
FT /evidence="ECO:0007829|PDB:5T76"
FT HELIX 868..881
FT /evidence="ECO:0007829|PDB:5T76"
FT STRAND 886..893
FT /evidence="ECO:0007829|PDB:5T76"
FT TURN 894..897
FT /evidence="ECO:0007829|PDB:5T76"
FT STRAND 898..904
FT /evidence="ECO:0007829|PDB:5T76"
FT HELIX 907..912
FT /evidence="ECO:0007829|PDB:5T76"
FT HELIX 916..924
FT /evidence="ECO:0007829|PDB:5T76"
FT TURN 925..928
FT /evidence="ECO:0007829|PDB:5T76"
FT STRAND 929..933
FT /evidence="ECO:0007829|PDB:5T76"
FT STRAND 935..943
FT /evidence="ECO:0007829|PDB:5T76"
FT HELIX 945..947
FT /evidence="ECO:0007829|PDB:5T76"
FT HELIX 948..960
FT /evidence="ECO:0007829|PDB:5T76"
SQ SEQUENCE 968 AA; 106810 MW; 8683F111CEE42506 CRC64;
MDSTLTASEI RQRFIDFFKR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK PIFLNTIDPS
HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KELACKMALE
LLTQEFGIPI ERLYVTYFGG DEAAGLEADL ECKQIWQNLG LDDTKILPGN MKDNFWEMGD
TGPCGPCSEI HYDRIGGRDA AHLVNQDDPN VLEIWNLVFI QYNREADGIL KPLPKKSIDT
GMGLERLVSV LQNKMSNYDT DLFVPYFEAI QKGTGARPYT GKVGAEDADG IDMAYRVLAD
HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYAHEKLN ASRGFFATLV DVVVQSLGDA
FPELKKDPDM VKDIINEEEV QFLKTLSRGR RILDRKIQSL GDSKTIPGDT AWLLYDTYGF
PVDLTGLIAE EKGLVVDMDG FEEERKLAQL KSQGKGAGGE DLIMLDIYAI EELRARGLEV
TDDSPKYNYH LDSSGSYVFE NTVATVMALR REKMFVEEVS TGQECGVVLD KTCFYAEQGG
QIYDEGYLVK VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GDLKVGDQVW LFIDEPRRRP
IMSNHTATHI LNFALRSVLG EADQKGSLVA PDRLRFDFTA KGAMSTQQIK KAEEIANEMI
EAAKAVYTQD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG VPVSELLDDP SGPAGSLTSV
EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR RIVAVTGAEA QKALRKAESL KKCLSVMEAK
VKAQTAPNKD VQREIADLGE ALATAVIPQW QKDELRETLK SLKKVMDDLD RASKADVQKR
VLEKTKQFID SNPNQPLVIL EMESGASAKA LNEALKLFKM HSPQTSAMLF TVDNEAGKIT
CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDVSAQA TGKNVGCLQE ALQLATSFAQ
LRLGDVKN
