ID SYWC_HUMAN Reviewed; 471 AA.
AC P23381; A6NGN1; A6NID3; P78535; Q502Y0; Q53XB6; Q9UDI5; Q9UDL3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 27-MAR-2024, entry version 223.
DE RecName: Full=Tryptophan--tRNA ligase, cytoplasmic {ECO:0000305};
DE EC=6.1.1.2 {ECO:0000269|PubMed:1761529, ECO:0000269|PubMed:28369220};
DE AltName: Full=Interferon-induced protein 53;
DE Short=IFP53;
DE AltName: Full=Tryptophanyl-tRNA synthetase;
DE Short=TrpRS;
DE Short=hWRS;
DE Contains:
DE RecName: Full=T1-TrpRS;
DE Contains:
DE RecName: Full=T2-TrpRS;
GN Name=WARS1 {ECO:0000312|HGNC:HGNC:12729}; Synonyms=IFI53, WARS, WRS;
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), FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1761529; DOI=10.1016/s0021-9258(18)54219-8;
RA Rubin B.Y., Anderson S.L., Xing L., Powell R.J., Tate W.P.;
RT "Interferon induces tryptophanyl-tRNA synthetase expression in human
RT fibroblasts.";
RL J. Biol. Chem. 266:24245-24248(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1763065; DOI=10.1073/pnas.88.24.11520;
RA Fleckner J., Rasmussen H.H., Justesen J.;
RT "Human interferon gamma potently induces the synthesis of a 55-kDa protein
RT (gamma 2) highly homologous to rabbit peptide chain release factor and
RT bovine tryptophanyl-tRNA synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11520-11524(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1765274; DOI=10.1016/0378-1119(91)90624-k;
RA Frolova L.Y., Sudomoina M.A., Grigorieva A.Y., Zinovieva O.L.,
RA Kisselev L.L.;
RT "Cloning and nucleotide sequence of the structural gene encoding for human
RT tryptophanyl-tRNA synthetase.";
RL Gene 109:291-296(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1537332; DOI=10.1002/j.1460-2075.1992.tb05079.x;
RA Buwitt U., Flohr T., Boettger E.C.;
RT "Molecular cloning and characterization of an interferon induced human cDNA
RT with sequence homology to a mammalian peptide chain release factor.";
RL EMBO J. 11:489-496(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood, and Lymph;
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RX PubMed=8724762;
RA Sokolova I.V., Narovlianskii A.N., Amchenkova A.M., Turpaev K.T.;
RT "Alternative splicing of 5'-terminal exons of the human tryptophanyl-tRNA
RT synthetase gene.";
RL Mol. Biol. (Mosk.) 30:319-329(1996).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-141 AND 182-471.
RC TISSUE=Sperm;
RX PubMed=7685728; DOI=10.1016/0378-1119(93)90568-n;
RA Frolova L.Y., Grigorieva A.Y., Sudomoina M.A., Kisselev L.L.;
RT "The human gene encoding tryptophanyl-tRNA synthetase: interferon-response
RT elements and exon-intron organization.";
RL Gene 128:237-245(1993).
RN [12]
RP PROTEIN SEQUENCE OF 2-19; 142-162; 205-220; 278-298; 350-366 AND 433-448,
RP AND INDUCTION.
RC TISSUE=Keratinocyte;
RX PubMed=8496617; DOI=10.1111/1523-1747.ep12476463;
RA Reano A., Richard M.H., Denoroy L., Viac J., Benedetto J.P., Schmitt D.;
RT "Gamma interferon potently induces tryptophanyl-tRNA synthetase expression
RT in human keratinocytes.";
RL J. Invest. Dermatol. 100:775-779(1993).
RN [13]
RP PROTEIN SEQUENCE OF 2-24; 97-106; 433-448 AND 465-471, CLEAVAGE OF
RP INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Gottlieb E.;
RL Submitted (MAR-2008) to UniProtKB.
RN [14]
RP PROTEIN SEQUENCE OF 71-75 AND 91-98, PROTEOLYTIC CLEAVAGE, AND FUNCTION
RP (ISOFORMS 1 AND 2).
RX PubMed=11773626; DOI=10.1073/pnas.012602099;
RA Wakasugi K., Slike B.M., Hood J., Otani A., Ewalt K.L., Friedlander M.,
RA Cheresh D.A., Schimmel P.;
RT "A human aminoacyl-tRNA synthetase as a regulator of angiogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:173-177(2002).
RN [15]
RP PROTEIN SEQUENCE OF 265-276; 278-296; 299-317 AND 350-365.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [16]
RP FUNCTION.
RX PubMed=1373391; DOI=10.1016/0014-5793(92)80187-l;
RA Bange F.-C., Flohr T., Buwitt U., Boettger E.C.;
RT "An interferon-induced protein with release factor activity is a
RT tryptophanyl-tRNA synthetase.";
RL FEBS Lett. 300:162-166(1992).
RN [17]
RP ALTERNATIVE SPLICING.
RX PubMed=7814400; DOI=10.1074/jbc.270.1.397;
RA Tolstrup A.B., Bejder A., Fleckner J., Justesen J.;
RT "Transcriptional regulation of the interferon-gamma-inducible tryptophanyl-
RT tRNA synthetase includes alternative splicing.";
RL J. Biol. Chem. 270:397-403(1995).
RN [18]
RP FUNCTION (T2-TRPRS).
RX PubMed=11773625; DOI=10.1073/pnas.012601899;
RA Otani A., Slike B.M., Dorrell M.I., Hood J., Kinder K., Ewalt K.L.,
RA Cheresh D., Schimmel P., Friedlander M.;
RT "A fragment of human TrpRS as a potent antagonist of ocular angiogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:178-183(2002).
RN [19]
RP FUNCTION (T2-TRPRS).
RX PubMed=14630953; DOI=10.1073/pnas.2436330100;
RA Tzima E., Reader J.S., Irani-Tehrani M., Ewalt K.L., Schwartz M.A.,
RA Schimmel P.;
RT "Biologically active fragment of a human tRNA synthetase inhibits fluid
RT shear stress-activated responses of endothelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:14903-14907(2003).
RN [20]
RP INTERACTION WITH GAPDH.
RX PubMed=15628863; DOI=10.1021/bi048313k;
RA Wakasugi K., Nakano T., Morishima I.;
RT "Oxidative stress-responsive intracellular regulation specific for the
RT angiostatic form of human tryptophanyl-tRNA synthetase.";
RL Biochemistry 44:225-232(2005).
RN [21]
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 [22]
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 [23]
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 [24]
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 [25]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS 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 [26]
RP IDENTIFICATION BY MASS 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, 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 [28]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INVOLVEMENT IN HMND9, VARIANT HMND9
RP ARG-257, VARIANT SER-443, AND CHARACTERIZATION OF VARIANT HMND9 ARG-257.
RX PubMed=28369220; DOI=10.1093/brain/awx058;
RA Tsai P.C., Soong B.W., Mademan I., Huang Y.H., Liu C.R., Hsiao C.T.,
RA Wu H.T., Liu T.T., Liu Y.T., Tseng Y.T., Lin K.P., Yang U.C., Chung K.W.,
RA Choi B.O., Nicholson G.A., Kennerson M.L., Chan C.C., De Jonghe P.,
RA Cheng T.H., Liao Y.C., Zuechner S., Baets J., Lee Y.C.;
RT "A recurrent WARS mutation is a novel cause of autosomal dominant distal
RT hereditary motor neuropathy.";
RL Brain 140:1252-1266(2017).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-466.
RX PubMed=14671330; DOI=10.1073/pnas.2136794100;
RA Yang X.-L., Otero F.J., Skene R.J., McRee D.E., Schimmel P.,
RA Ribas de Pouplana L.;
RT "Crystal structures that suggest late development of genetic code
RT components for differentiating aromatic side chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15376-15380(2003).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 94-471.
RX PubMed=14660560; DOI=10.1074/jbc.m311284200;
RA Yu Y., Liu Y., Shen N., Xu X., Xu F., Jia J., Jin Y., Arnold E., Ding J.;
RT "Crystal structure of human tryptophanyl-tRNA synthetase catalytic
RT fragment: insights into substrate recognition, tRNA binding, and
RT angiogenesis activity.";
RL J. Biol. Chem. 279:8378-8388(2004).
RN [31]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-455.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [32]
RP INVOLVEMENT IN NEDMSBA, AND VARIANTS NEDMSBA THR-333 AND TRP-448.
RX PubMed=34585293; DOI=10.1007/s10072-021-05626-z;
RA Okamoto N., Miya F., Tsunoda T., Kanemura Y., Saitoh S., Kato M.,
RA Yanagi K., Kaname T., Kosaki K.;
RT "Four pedigrees with aminoacyl-tRNA synthetase abnormalities.";
RL Neurol. Sci. 43:2765-2774(2022).
RN [33]
RP VARIANT HMND9 TYR-138.
RX PubMed=31321409; DOI=10.1093/brain/awz218;
RA Li J.Q., Dong H.L., Chen C.X., Wu Z.Y.;
RT "A novel WARS mutation causes distal hereditary motor neuropathy in a
RT Chinese family.";
RL Brain 142:e49-e49(2019).
RN [34]
RP VARIANT HMND9 GLY-314.
RX PubMed=31069783; DOI=10.1111/cge.13563;
RA Wang B., Li X., Huang S., Zhao H., Liu J., Hu Z., Lin Z., Liu L., Xie Y.,
RA Jin Q., Zhao H., Tang B., Niu Q., Zhang R.;
RT "A novel WARS mutation (p.Asp314Gly) identified in a Chinese distal
RT hereditary motor neuropathy family.";
RL Clin. Genet. 96:176-182(2019).
RN [35]
RP VARIANT NEDMSBA CYS-133, AND CHARACTERIZATION OF VARIANT NEDMSBA CYS-133.
RX PubMed=35790048; DOI=10.1002/humu.24430;
RA Boegershausen N., Krawczyk H.E., Jamra R.A., Lin S.J., Yigit G.,
RA Huening I., Polo A.M., Vona B., Huang K., Schmidt J., Altmueller J.,
RA Luppe J., Platzer K., Doergeloh B.B., Busche A., Biskup S., Mendes M.I.,
RA Smith D.E.C., Salomons G.S., Zibat A., Bueltmann E., Nuernberg P.,
RA Spielmann M., Lemke J.R., Li Y., Zenker M., Varshney G.K., Hillen H.S.,
RA Kratz C.P., Wollnik B.;
RT "WARS1 and SARS1: Two tRNA synthetases implicated in autosomal recessive
RT microcephaly.";
RL Hum. Mutat. 43:1454-1471(2022).
RN [36]
RP VARIANT NEDMSBA ASN-419, AND CHARACTERIZATION OF VARIANTS NEDMSBA THR-333
RP AND TRP-448.
RX PubMed=35815345; DOI=10.1002/humu.24435;
RA Lin S.J., Vona B., Porter H.M., Izadi M., Huang K., Lacassie Y.,
RA Rosenfeld J.A., Khan S., Petree C., Ali T.A., Muhammad N., Khan S.A.,
RA Muhammad N., Liu P., Haymon M.L., Rueschendorf F., Kong I.K., Schnapp L.,
RA Shur N., Chorich L., Layman L., Haaf T., Pourkarimi E., Kim H.G.,
RA Varshney G.K.;
RT "Biallelic variants in WARS1 cause a highly variable neurodevelopmental
RT syndrome and implicate a critical exon for normal auditory function.";
RL Hum. Mutat. 43:1472-1489(2022).
CC -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp) in a two-
CC step reaction: tryptophan is first activated by ATP to form Trp-AMP and
CC then transferred to the acceptor end of the tRNA(Trp).
CC {ECO:0000269|PubMed:1373391, ECO:0000269|PubMed:1761529,
CC ECO:0000269|PubMed:28369220}.
CC -!- FUNCTION: [Isoform 1]: Has no angiostatic activity.
CC {ECO:0000269|PubMed:11773625, ECO:0000269|PubMed:11773626}.
CC -!- FUNCTION: [T2-TrpRS]: Possesses an angiostatic activity but has no
CC aminoacylation activity (PubMed:11773626, PubMed:11773625,
CC PubMed:14630953). Inhibits fluid shear stress-activated responses of
CC endothelial cells (PubMed:14630953). Regulates ERK, Akt, and eNOS
CC activation pathways that are associated with angiogenesis, cytoskeletal
CC reorganization and shear stress-responsive gene expression
CC (PubMed:14630953). {ECO:0000269|PubMed:11773625,
CC ECO:0000269|PubMed:11773626, ECO:0000269|PubMed:14630953}.
CC -!- FUNCTION: [Isoform 2]: Has an angiostatic activity.
CC {ECO:0000269|PubMed:11773625, ECO:0000269|PubMed:11773626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC Evidence={ECO:0000269|PubMed:1761529, ECO:0000269|PubMed:28369220};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24081;
CC Evidence={ECO:0000269|PubMed:28369220};
CC -!- SUBUNIT: Homodimer (PubMed:28369220). Interacts with an oxidized form
CC of GAPDH. GAPDH stimulates the aminoacylation activity of isoform 2
CC (PubMed:15628863). {ECO:0000269|PubMed:15628863,
CC ECO:0000269|PubMed:28369220}.
CC -!- INTERACTION:
CC P23381; P33151: CDH5; NbExp=4; IntAct=EBI-721244, EBI-2903122;
CC P23381; P54274: TERF1; NbExp=2; IntAct=EBI-721244, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P23381-1; Sequence=Displayed;
CC Name=2; Synonyms=mini TrpRS;
CC IsoId=P23381-2; Sequence=VSP_038221;
CC -!- INDUCTION: By IFNG/IFN-gamma. {ECO:0000269|PubMed:8496617}.
CC -!- PTM: Proteolytic cleavage generates 2 forms; T1-TrpRS and T2-TrpRS.
CC {ECO:0000269|PubMed:11773626}.
CC -!- DISEASE: Neuronopathy, distal hereditary motor, autosomal dominant 9
CC (HMND9) [MIM:617721]: A form of distal hereditary motor neuronopathy, a
CC heterogeneous group of neuromuscular disorders caused by selective
CC degeneration of motor neurons in the anterior horn of the spinal cord,
CC without sensory deficit in the posterior horn. The overall clinical
CC picture consists of a classical distal muscular atrophy syndrome in the
CC legs without clinical sensory loss. The disease starts with weakness
CC and wasting of distal muscles of the anterior tibial and peroneal
CC compartments of the legs. Later on, weakness and atrophy may expand to
CC the proximal muscles of the lower limbs and/or to the distal upper
CC limbs. HMND9 is characterized by juvenile onset of slowly progressive
CC distal muscle weakness and atrophy affecting both the lower and upper
CC limbs. {ECO:0000269|PubMed:28369220, ECO:0000269|PubMed:31069783,
CC ECO:0000269|PubMed:31321409}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Neurodevelopmental disorder with microcephaly and speech
CC delay, with or without brain abnormalities (NEDMSBA) [MIM:620317]: An
CC autosomal recessive disorder apparent from early infancy and
CC characterized by global developmental delay, delayed or absent walking,
CC impaired intellectual development, poor or absent speech, and postnatal
CC progressive microcephaly. Additional variable features include cortical
CC visual impairment, seizures, hypotonia, spasticity, and sensorineural
CC deafness. Brain anomalies including myelination defects, cortical
CC atrophy, or thin corpus callosum are present in most patients.
CC {ECO:0000269|PubMed:34585293, ECO:0000269|PubMed:35790048,
CC ECO:0000269|PubMed:35815345}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; M77804; AAA67324.1; -; mRNA.
DR EMBL; X59892; CAA42545.1; -; mRNA.
DR EMBL; M61715; AAA61298.1; -; mRNA.
DR EMBL; X62570; CAA44450.1; -; mRNA.
DR EMBL; BX248006; CAD62335.1; -; mRNA.
DR EMBL; AK056100; BAG51626.1; -; mRNA.
DR EMBL; AK291141; BAF83830.1; -; mRNA.
DR EMBL; AL157871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81700.1; -; Genomic_DNA.
DR EMBL; BC017489; AAH17489.1; -; mRNA.
DR EMBL; BC095453; AAH95453.1; -; mRNA.
DR EMBL; S82905; AAB39381.1; -; Genomic_DNA.
DR EMBL; X67920; CAB94198.1; -; Genomic_DNA.
DR EMBL; X67921; CAB94198.1; JOINED; Genomic_DNA.
DR EMBL; X67922; CAB94198.1; JOINED; Genomic_DNA.
DR EMBL; X67923; CAB94199.1; -; Genomic_DNA.
DR EMBL; X67924; CAB94199.1; JOINED; Genomic_DNA.
DR EMBL; X67925; CAB94199.1; JOINED; Genomic_DNA.
DR EMBL; X67926; CAB94199.1; JOINED; Genomic_DNA.
DR EMBL; X67927; CAB94199.1; JOINED; Genomic_DNA.
DR EMBL; X67928; CAB94199.1; JOINED; Genomic_DNA.
DR CCDS; CCDS9960.1; -. [P23381-1]
DR CCDS; CCDS9961.1; -. [P23381-2]
DR PIR; A41633; A41706.
DR RefSeq; NP_004175.2; NM_004184.3. [P23381-1]
DR RefSeq; NP_776049.1; NM_173701.1. [P23381-1]
DR RefSeq; NP_998810.1; NM_213645.1. [P23381-2]
DR RefSeq; NP_998811.1; NM_213646.1. [P23381-2]
DR RefSeq; XP_005268101.1; XM_005268044.3.
DR RefSeq; XP_006720312.1; XM_006720249.3.
DR RefSeq; XP_011535435.1; XM_011537133.2.
DR RefSeq; XP_011535437.1; XM_011537135.2.
DR RefSeq; XP_011535438.1; XM_011537136.2. [P23381-2]
DR RefSeq; XP_016877116.1; XM_017021627.1. [P23381-1]
DR RefSeq; XP_016877117.1; XM_017021628.1.
DR RefSeq; XP_016877118.1; XM_017021629.1.
DR PDB; 1O5T; X-ray; 2.50 A; A=94-471.
DR PDB; 1R6T; X-ray; 2.10 A; A/B=1-466.
DR PDB; 1R6U; X-ray; 2.00 A; A/B=48-471.
DR PDB; 1ULH; X-ray; 2.31 A; A/B=82-471.
DR PDB; 2AKE; X-ray; 3.10 A; A=94-471.
DR PDB; 2AZX; X-ray; 2.80 A; A/B=1-471.
DR PDB; 2DR2; X-ray; 3.00 A; A=94-471.
DR PDB; 2QUH; X-ray; 2.40 A; A/B=1-471.
DR PDB; 2QUI; X-ray; 2.40 A; A/B=1-471.
DR PDB; 2QUJ; X-ray; 2.42 A; A/B=1-471.
DR PDB; 2QUK; X-ray; 2.80 A; A=1-471.
DR PDB; 5UJI; X-ray; 2.79 A; A/B=97-471.
DR PDB; 5UJJ; X-ray; 2.10 A; A/B=1-471.
DR PDBsum; 1O5T; -.
DR PDBsum; 1R6T; -.
DR PDBsum; 1R6U; -.
DR PDBsum; 1ULH; -.
DR PDBsum; 2AKE; -.
DR PDBsum; 2AZX; -.
DR PDBsum; 2DR2; -.
DR PDBsum; 2QUH; -.
DR PDBsum; 2QUI; -.
DR PDBsum; 2QUJ; -.
DR PDBsum; 2QUK; -.
DR PDBsum; 5UJI; -.
DR PDBsum; 5UJJ; -.
DR AlphaFoldDB; P23381; -.
DR SMR; P23381; -.
DR BioGRID; 113292; 173.
DR DIP; DIP-29493N; -.
DR IntAct; P23381; 24.
DR MINT; P23381; -.
DR STRING; 9606.ENSP00000347495; -.
DR DrugBank; DB00150; Tryptophan.
DR DrugBank; DB04537; Tryptophanamide.
DR DrugBank; DB01831; Tryptophanyl-5'amp.
DR MoonProt; P23381; -.
DR GlyGen; P23381; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P23381; -.
DR MetOSite; P23381; -.
DR PhosphoSitePlus; P23381; -.
DR SwissPalm; P23381; -.
DR BioMuta; WARS; -.
DR DMDM; 135191; -.
DR OGP; P23381; -.
DR EPD; P23381; -.
DR jPOST; P23381; -.
DR MassIVE; P23381; -.
DR MaxQB; P23381; -.
DR PaxDb; 9606-ENSP00000347495; -.
DR PeptideAtlas; P23381; -.
DR ProteomicsDB; 54085; -. [P23381-1]
DR ProteomicsDB; 54086; -. [P23381-2]
DR Pumba; P23381; -.
DR ABCD; P23381; 4 sequenced antibodies.
DR Antibodypedia; 27522; 307 antibodies from 30 providers.
DR DNASU; 7453; -.
DR Ensembl; ENST00000344102.9; ENSP00000339485.5; ENSG00000140105.18. [P23381-2]
DR Ensembl; ENST00000355338.6; ENSP00000347495.2; ENSG00000140105.18. [P23381-1]
DR Ensembl; ENST00000358655.8; ENSP00000351481.4; ENSG00000140105.18. [P23381-2]
DR Ensembl; ENST00000392882.7; ENSP00000376620.2; ENSG00000140105.18. [P23381-1]
DR Ensembl; ENST00000556645.5; ENSP00000451887.1; ENSG00000140105.18. [P23381-2]
DR Ensembl; ENST00000557135.5; ENSP00000451460.1; ENSG00000140105.18. [P23381-1]
DR GeneID; 7453; -.
DR KEGG; hsa:7453; -.
DR MANE-Select; ENST00000392882.7; ENSP00000376620.2; NM_004184.4; NP_004175.2.
DR UCSC; uc001yhg.3; human. [P23381-1]
DR AGR; HGNC:12729; -.
DR CTD; 7453; -.
DR DisGeNET; 7453; -.
DR GeneCards; WARS1; -.
DR GeneReviews; WARS1; -.
DR HGNC; HGNC:12729; WARS1.
DR HPA; ENSG00000140105; Tissue enhanced (placenta).
DR MalaCards; WARS1; -.
DR MIM; 191050; gene.
DR MIM; 617721; phenotype.
DR MIM; 620317; phenotype.
DR neXtProt; NX_P23381; -.
DR OpenTargets; ENSG00000140105; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA37340; -.
DR VEuPathDB; HostDB:ENSG00000140105; -.
DR eggNOG; KOG2145; Eukaryota.
DR GeneTree; ENSGT00940000153724; -.
DR HOGENOM; CLU_032621_0_1_1; -.
DR InParanoid; P23381; -.
DR OMA; SIYHRFM; -.
DR OrthoDB; 540846at2759; -.
DR PhylomeDB; P23381; -.
DR TreeFam; TF105669; -.
DR BRENDA; 6.1.1.2; 2681.
DR PathwayCommons; P23381; -.
DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
DR SignaLink; P23381; -.
DR SIGNOR; P23381; -.
DR BioGRID-ORCS; 7453; 781 hits in 1175 CRISPR screens.
DR ChiTaRS; WARS; human.
DR EvolutionaryTrace; P23381; -.
DR GeneWiki; WARS_(gene); -.
DR GenomeRNAi; 7453; -.
DR Pharos; P23381; Tbio.
DR PRO; PR:P23381; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P23381; Protein.
DR Bgee; ENSG00000140105; Expressed in monocyte and 204 other cell types or tissues.
DR ExpressionAtlas; P23381; baseline and differential.
DR Genevisible; P23381; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019210; F:kinase inhibitor activity; IDA:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:CAFA.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:CAFA.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:CAFA.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:CAFA.
DR GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00806; TrpRS_core; 1.
DR CDD; cd00936; WEPRS_RNA; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR NCBIfam; TIGR00233; trpS; 1.
DR PANTHER; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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;
KW Angiogenesis; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Disease variant; Intellectual disability; Ligase; Neurodegeneration;
KW Neuropathy; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8496617, ECO:0000269|Ref.13,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..471
FT /note="Tryptophan--tRNA ligase, cytoplasmic"
FT /id="PRO_0000136738"
FT CHAIN 71..471
FT /note="T1-TrpRS"
FT /evidence="ECO:0000269|PubMed:11773626"
FT /id="PRO_0000386461"
FT CHAIN 94..471
FT /note="T2-TrpRS"
FT /evidence="ECO:0000269|PubMed:11773626"
FT /id="PRO_0000386462"
FT DOMAIN 8..64
FT /note="WHEP-TRS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT REGION 59..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..173
FT /note="'HIGH' region"
FT /evidence="ECO:0000269|PubMed:1373391"
FT MOTIF 349..353
FT /note="'KMSKS' region"
FT /evidence="ECO:0000269|PubMed:1373391"
FT MOD_RES 154
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32921"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038221"
FT VARIANT 54
FT /note="A -> S (in dbSNP:rs2234521)"
FT /id="VAR_052406"
FT VARIANT 83
FT /note="D -> A"
FT /evidence="ECO:0000269|PubMed:35815345"
FT /id="VAR_088482"
FT VARIANT 133
FT /note="R -> C (in NEDMSBA; loss of function; failed to
FT rescue both the eye and head size phenotypes in a zebrafish
FT wars1-knockout disease model)"
FT /evidence="ECO:0000269|PubMed:35790048"
FT /id="VAR_088483"
FT VARIANT 138
FT /note="F -> Y (in HMND9)"
FT /evidence="ECO:0000269|PubMed:31321409"
FT /id="VAR_088484"
FT VARIANT 257
FT /note="H -> R (in HMND9; decreased tryptophan-tRNA ligase
FT activity; dominant negative effect; decreased general
FT protein synthesis; decreased cell viability; no effect on
FT homodimerization)"
FT /evidence="ECO:0000269|PubMed:28369220"
FT /id="VAR_080407"
FT VARIANT 314
FT /note="D -> G (in HMND9)"
FT /evidence="ECO:0000269|PubMed:31069783"
FT /id="VAR_088485"
FT VARIANT 333
FT /note="A -> T (in NEDMSBA; uncertain significance; when
FT tested in a wars1-knockout zebrafish disease model it
FT partially rescues the ocular defects and is able to rescue
FT hearing deficits and head abnormalities)"
FT /evidence="ECO:0000269|PubMed:34585293,
FT ECO:0000269|PubMed:35815345"
FT /id="VAR_088486"
FT VARIANT 419
FT /note="D -> N (in NEDMSBA; uncertain significance; when
FT tested in a wars1-knockout zebrafish disease model is able
FT to rescue head and eye sizes partially while the hearing
FT phenotype was rescued completely)"
FT /evidence="ECO:0000269|PubMed:35815345"
FT /id="VAR_088487"
FT VARIANT 443
FT /note="A -> S (in dbSNP:rs139914390)"
FT /evidence="ECO:0000269|PubMed:28369220"
FT /id="VAR_080408"
FT VARIANT 448
FT /note="R -> W (in NEDMSBA; uncertain significance; when
FT tested in a zebrafish wars1-knockout disease model it fails
FT to rescue head abnormalities while it partially rescues the
FT ocular defects and is able to fully rescue hearing
FT deficits)"
FT /evidence="ECO:0000269|PubMed:34585293,
FT ECO:0000269|PubMed:35815345"
FT /id="VAR_088488"
FT VARIANT 455
FT /note="E -> D (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036466"
FT CONFLICT 213..214
FT /note="SY -> GD (in Ref. 3; AAA61298)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="A -> V (in Ref. 9; AAH95453)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="A -> R (in Ref. 4; CAA44450)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="Q -> L (in Ref. 9; AAH95453)"
FT /evidence="ECO:0000305"
FT HELIX 8..28
FT /evidence="ECO:0007829|PDB:1R6T"
FT HELIX 33..53
FT /evidence="ECO:0007829|PDB:1R6T"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1R6T"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1R6U"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:1R6U"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:5UJJ"
FT HELIX 171..187
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 208..223
FT /evidence="ECO:0007829|PDB:1R6U"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:1ULH"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:2AZX"
FT HELIX 365..374
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:5UJI"
FT HELIX 384..390
FT /evidence="ECO:0007829|PDB:1R6U"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 398..406
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 410..422
FT /evidence="ECO:0007829|PDB:1R6U"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 430..450
FT /evidence="ECO:0007829|PDB:1R6U"
FT HELIX 454..460
FT /evidence="ECO:0007829|PDB:1R6U"
SQ SEQUENCE 471 AA; 53165 MW; E96344449053A0D0 CRC64;
MPNSEPASLL ELFNSIATQG ELVRSLKAGN ASKDEIDSAV KMLVSLKMSY KAAAGEDYKA
DCPPGNPAPT SNHGPDATEA EEDFVDPWTV QTSSAKGIDY DKLIVRFGSS KIDKELINRI
ERATGQRPHH FLRRGIFFSH RDMNQVLDAY ENKKPFYLYT GRGPSSEAMH VGHLIPFIFT
KWLQDVFNVP LVIQMTDDEK YLWKDLTLDQ AYSYAVENAK DIIACGFDIN KTFIFSDLDY
MGMSSGFYKN VVKIQKHVTF NQVKGIFGFT DSDCIGKISF PAIQAAPSFS NSFPQIFRDR
TDIQCLIPCA IDQDPYFRMT RDVAPRIGYP KPALLHSTFF PALQGAQTKM SASDPNSSIF
LTDTAKQIKT KVNKHAFSGG RDTIEEHRQF GGNCDVDVSF MYLTFFLEDD DKLEQIRKDY
TSGAMLTGEL KKALIEVLQP LIAEHQARRK EVTDEIVKEF MTPRKLSFDF Q
//
