THTM_MOUSE
ID THTM_MOUSE Reviewed; 297 AA.
AC Q99J99; Q3UW66; Q505N7;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=3-mercaptopyruvate sulfurtransferase;
DE Short=MST;
DE EC=2.8.1.2 {ECO:0000269|PubMed:18855522, ECO:0000269|PubMed:28079151};
GN Name=Mpst;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23053.1};
RC TISSUE=Cecum {ECO:0000312|EMBL:BAE23053.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 53-64; 119-133; 147-164 AND 198-224, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP DEVELOPMENTAL STAGE, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, ACTIVE SITE, AND MUTAGENESIS OF ARG-188; ARG-197 AND
RP CYS-248.
RX PubMed=18855522; DOI=10.1089/ars.2008.2253;
RA Shibuya N., Tanaka M., Yoshida M., Ogasawara Y., Togawa T., Ishii K.,
RA Kimura H.;
RT "3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound
RT sulfane sulfur in the brain.";
RL Antioxid. Redox Signal. 11:703-714(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP THIOREDOXIN AND DIHYDROLIPOIC ACID AS REDUCING AGENTS.
RX PubMed=21732914; DOI=10.1042/bj20110841;
RA Mikami Y., Shibuya N., Kimura Y., Nagahara N., Ogasawara Y., Kimura H.;
RT "Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate
RT sulfurtransferase to produce hydrogen sulfide.";
RL Biochem. J. 439:479-485(2011).
RN [9]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=21937432; DOI=10.1074/jbc.m111.298208;
RA Mikami Y., Shibuya N., Kimura Y., Nagahara N., Yamada M., Kimura H.;
RT "Hydrogen sulfide protects the retina from light-induced degeneration by
RT the modulation of Ca2+ influx.";
RL J. Biol. Chem. 286:39379-39386(2011).
RN [10]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=22808324; DOI=10.4161/cib.18679;
RA Mikami Y., Kimura H.;
RT "A mechanism of retinal protection from light-induced degeneration by
RT hydrogen sulfide.";
RL Commun. Integr. Biol. 5:169-171(2012).
RN [11]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-146 AND LYS-164, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [13] {ECO:0007744|PDB:5WQJ, ECO:0007744|PDB:5WQK}
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR,
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=28079151; DOI=10.1038/srep40227;
RA Hanaoka K., Sasakura K., Suwanai Y., Toma-Fukai S., Shimamoto K.,
RA Takano Y., Shibuya N., Terai T., Komatsu T., Ueno T., Ogasawara Y.,
RA Tsuchiya Y., Watanabe Y., Kimura H., Wang C., Uchiyama M., Kojima H.,
RA Okabe T., Urano Y., Shimizu T., Nagano T.;
RT "Discovery and Mechanistic Characterization of Selective Inhibitors of H2S-
RT producing Enzyme: 3-Mercaptopyruvate Sulfurtransferase (3MST) Targeting
RT Active-site Cysteine Persulfide.";
RL Sci. Rep. 7:40227-40227(2017).
CC -!- FUNCTION: Transfer of a sulfur ion to cyanide or to other thiol
CC compounds. Also has weak rhodanese activity. Detoxifies cyanide and is
CC required for thiosulfate biosynthesis. Acts as an antioxidant. In
CC combination with cysteine aminotransferase (CAT), contributes to the
CC catabolism of cysteine and is an important producer of hydrogen sulfide
CC in the brain, retina and vascular endothelial cells. Hydrogen sulfide
CC H(2)S is an important synaptic modulator, signaling molecule, smooth
CC muscle contractor and neuroprotectant. Its production by the 3MST/CAT
CC pathway is regulated by calcium ions. {ECO:0000269|PubMed:18855522,
CC ECO:0000269|PubMed:21937432, ECO:0000269|PubMed:22808324,
CC ECO:0000269|PubMed:28079151}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol =
CC [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate;
CC Xref=Rhea:RHEA:21740, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57678; EC=2.8.1.2;
CC Evidence={ECO:0000269|PubMed:18855522, ECO:0000269|PubMed:28079151};
CC -!- ACTIVITY REGULATION: By oxidative stress, and thioredoxin. Under
CC oxidative stress conditions, the catalytic cysteine site is converted
CC to a sulfenate which inhibits the MPST enzyme activity. Reduced
CC thioredoxin cleaves an intersubunit disulfide bond to turn on the redox
CC switch and reactivate the enzyme. Inhibited by different oxidants,
CC hydrogen peroxide and tetrathionate. {ECO:0000250|UniProtKB:P97532}.
CC -!- SUBUNIT: Monomer (active form). Homodimer; disulfide-linked (inactive
CC form). {ECO:0000250|UniProtKB:P97532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P97532}.
CC Mitochondrion {ECO:0000269|PubMed:18855522}. Synapse, synaptosome
CC {ECO:0000269|PubMed:18855522}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain and retina. In the retina,
CC localized to the inner and outer plexiform layer, the inner and outer
CC nuclear layer and the outer segments of photoreceptors. In the brain,
CC localized to neurons of mitral cell layers, glomerular, and external
CC plexiform layers in the olfactory bulb. Also found in Purkinje cell
CC stomata and proximal dendrites. In the spinal cord, localized to large
CC neurons. In the cerebral cortex, localized to pyramidial neurons in
CC layers II/III and V, and in layers I-VI of neocortical areas. In the
CC hippocampus, found in CA1 and CA3 pyramidal cells.
CC {ECO:0000269|PubMed:18855522, ECO:0000269|PubMed:21937432,
CC ECO:0000269|PubMed:22808324}.
CC -!- DEVELOPMENTAL STAGE: In the developing brain, maintained expression
CC from 16 dpc to postnatal day 14. Levels decrease between postnatal day
CC 28 and postnatal day 52 and increase again with further aging up to 156
CC days old. {ECO:0000269|PubMed:18855522}.
CC -!- DOMAIN: Contains two rhodanese domains with different primary
CC structures but with near identical secondary structure conformations
CC suggesting a common evolutionary origin. Only the C-terminal rhodanese
CC domain contains the catalytic cysteine residue (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Thioredoxin (Trx) or dihydrolipoic acid (DHLA) are
CC required to release hydrogen sulfide from the persulfide intermediate.
CC {ECO:0000305|PubMed:21732914}.
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DR EMBL; AK136571; BAE23053.1; -; mRNA.
DR EMBL; AL583893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466545; EDL29674.1; -; Genomic_DNA.
DR EMBL; BC004079; AAH04079.1; -; mRNA.
DR EMBL; BC094469; AAH94469.1; -; mRNA.
DR CCDS; CCDS27615.1; -.
DR RefSeq; NP_001155964.1; NM_001162492.1.
DR RefSeq; NP_001155965.1; NM_001162493.1.
DR RefSeq; NP_619611.3; NM_138670.3.
DR RefSeq; XP_006521057.1; XM_006520994.3.
DR RefSeq; XP_006521058.1; XM_006520995.2.
DR RefSeq; XP_006521059.1; XM_006520996.3.
DR PDB; 5WQJ; X-ray; 1.20 A; A/B=1-297.
DR PDB; 5WQK; X-ray; 1.70 A; A/B=5-297.
DR PDBsum; 5WQJ; -.
DR PDBsum; 5WQK; -.
DR AlphaFoldDB; Q99J99; -.
DR SMR; Q99J99; -.
DR IntAct; Q99J99; 1.
DR MINT; Q99J99; -.
DR STRING; 10090.ENSMUSP00000043061; -.
DR iPTMnet; Q99J99; -.
DR PhosphoSitePlus; Q99J99; -.
DR SwissPalm; Q99J99; -.
DR REPRODUCTION-2DPAGE; IPI00114957; -.
DR REPRODUCTION-2DPAGE; Q99J99; -.
DR EPD; Q99J99; -.
DR jPOST; Q99J99; -.
DR MaxQB; Q99J99; -.
DR PaxDb; Q99J99; -.
DR PRIDE; Q99J99; -.
DR ProteomicsDB; 262820; -.
DR ProteomicsDB; 342690; -.
DR Antibodypedia; 223; 155 antibodies from 24 providers.
DR DNASU; 246221; -.
DR Ensembl; ENSMUST00000043865; ENSMUSP00000043061; ENSMUSG00000071711.
DR Ensembl; ENSMUST00000167140; ENSMUSP00000130493; ENSMUSG00000071711.
DR Ensembl; ENSMUST00000169133; ENSMUSP00000128075; ENSMUSG00000071711.
DR Ensembl; ENSMUST00000229739; ENSMUSP00000155371; ENSMUSG00000071711.
DR GeneID; 246221; -.
DR KEGG; mmu:246221; -.
DR UCSC; uc007wpe.2; mouse.
DR CTD; 4357; -.
DR MGI; MGI:2179733; Mpst.
DR VEuPathDB; HostDB:ENSMUSG00000071711; -.
DR eggNOG; KOG1529; Eukaryota.
DR GeneTree; ENSGT00510000046773; -.
DR InParanoid; Q99J99; -.
DR OMA; QRPGHVP; -.
DR OrthoDB; 1553525at2759; -.
DR PhylomeDB; Q99J99; -.
DR TreeFam; TF315133; -.
DR BRENDA; 2.8.1.2; 3474.
DR Reactome; R-MMU-1614558; Degradation of cysteine and homocysteine.
DR BioGRID-ORCS; 246221; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Mpst; mouse.
DR PRO; PR:Q99J99; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q99J99; protein.
DR Bgee; ENSMUSG00000071711; Expressed in hindlimb stylopod muscle and 163 other tissues.
DR ExpressionAtlas; Q99J99; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0016784; F:3-mercaptopyruvate sulfurtransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; ISO:MGI.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISO:MGI.
DR GO; GO:0001889; P:liver development; ISO:MGI.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0019346; P:transsulfuration; ISO:MGI.
DR Gene3D; 3.40.250.10; -; 2.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR InterPro; IPR045078; TST/MPST-like.
DR PANTHER; PTHR11364; PTHR11364; 1.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; SSF52821; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Mitochondrion; Phosphoprotein; Redox-active center;
KW Reference proteome; Repeat; Synapse; Synaptosome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P25325"
FT CHAIN 2..297
FT /note="3-mercaptopyruvate sulfurtransferase"
FT /id="PRO_0000139399"
FT DOMAIN 25..144
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 174..288
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 145..160
FT /note="Hinge"
FT ACT_SITE 248
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173,
FT ECO:0000269|PubMed:18855522, ECO:0000269|PubMed:28079151"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P25325"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25325"
FT MOD_RES 40
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 40
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 146
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 164
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT DISULFID 264
FT /note="Interchain (with C-264); redox-active"
FT /evidence="ECO:0000250"
FT MUTAGEN 188
FT /note="R->G: Abolishes hydrogen sulfide production.
FT Slightly increased basal levels of bound persulfide."
FT /evidence="ECO:0000269|PubMed:18855522"
FT MUTAGEN 197
FT /note="R->G: Reduces hydrogen sulfide production by 50%. No
FT change in basal levels of bound persulfide."
FT /evidence="ECO:0000269|PubMed:18855522"
FT MUTAGEN 248
FT /note="C->S: Loss of redox potential. Abolishes bound
FT persulfide and hydrogen sulfide production."
FT /evidence="ECO:0000269|PubMed:18855522"
FT CONFLICT 102
FT /note="D -> G (in Ref. 3; EDL29674 and 4; AAH04079/
FT AAH94469)"
FT CONFLICT 107
FT /note="L -> P (in Ref. 4; AAH04079)"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:5WQJ"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5WQJ"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:5WQJ"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:5WQJ"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:5WQJ"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:5WQJ"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:5WQJ"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:5WQJ"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:5WQJ"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5WQJ"
SQ SEQUENCE 297 AA; 33097 MW; 9D316B9AD9344D0A CRC64;
MAAPQLFRAL VSAQWVAEAL KAPRSSQPLK LLDASWYLPK LGRDARREFE ERHIPGAAFF
DIDRCSDHTS PYDHMLPNAT HFADYAGSLG VSAATHVVIY DDSDQGLYSA PRVWWMFRAF
GHHSVSLLDG GFRHWLNQNL PISSGKSHSE PAEFSAQLDP SFIKTHEDIL ENLDARRFQV
VDARAAGRFQ GTQPEPRDGI EPGHIPGSVN IPFTEFLTNE GLEKSPEEIK RLFKEKKVDL
SKPLVATCGS GVTACHVVLG AFLCGKSDVP VYDGSWVEWY MRAQPEHIIS EGRGKTQ
