TRXR1_MOUSE
ID TRXR1_MOUSE Reviewed; 613 AA.
AC Q9JMH6; Q3UEB7; Q3UK84; Q8CI31; Q99P49; Q9CSV5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Thioredoxin reductase 1, cytoplasmic {ECO:0000305};
DE Short=TR;
DE EC=1.8.1.9 {ECO:0000250|UniProtKB:Q16881};
DE AltName: Full=Peroxidase TXNRD1 {ECO:0000250|UniProtKB:Q16881};
DE EC=1.11.1.2 {ECO:0000250|UniProtKB:Q16881};
DE AltName: Full=Thioredoxin reductase TR1;
GN Name=Txnrd1 {ECO:0000312|MGI:MGI:1354175}; Synonyms=Trxr1;
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 [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RC TISSUE=Thymus;
RX PubMed=10721726; DOI=10.1016/s0378-1119(99)00498-9;
RA Kawai H., Ota T., Suzuki F., Tatsuka M.;
RT "Molecular cloning of mouse thioredoxin reductases.";
RL Gene 242:321-330(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11060283; DOI=10.1074/jbc.m004750200;
RA Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L.,
RA Gladyshev V.N.;
RT "Heterogeneity within animal thioredoxin reductases: evidence for
RT alternative first exon splicing.";
RL J. Biol. Chem. 276:3106-3114(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N-3; 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 ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RX PubMed=11737861; DOI=10.1186/1471-2164-2-10;
RA Osborne S.A., Tonissen K.F.;
RT "Genomic organisation and alternative splicing of mouse and human
RT thioredoxin reductase 1 genes.";
RL BMC Genomics 2:10-10(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
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 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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).
CC -!- FUNCTION: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-
CC containing form. Homodimeric flavoprotein involved in the regulation of
CC cellular redox reactions, growth and differentiation. Contains a
CC selenocysteine residue at the C-terminal active site that is essential
CC for catalysis. Also has reductase activity on hydrogen peroxide (H2O2).
CC {ECO:0000250|UniProtKB:Q16881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q16881};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347;
CC Evidence={ECO:0000250|UniProtKB:Q16881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O2 + NADPH = 2 H2O + NADP(+); Xref=Rhea:RHEA:15173,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.11.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q16881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15174;
CC Evidence={ECO:0000250|UniProtKB:Q16881};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q16881};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q16881};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q16881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10721726}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JMH6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JMH6-2; Sequence=VSP_031566;
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:Q16881}.
CC -!- MISCELLANEOUS: The thioredoxin reductase active site is a redox-active
CC disulfide bond. The selenocysteine residue is also essential for
CC catalytic activity. {ECO:0000250|UniProtKB:O89049}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37643.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE26918.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE40292.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB027565; BAA86985.2; -; mRNA.
DR EMBL; AF333036; AAK01140.1; -; mRNA.
DR EMBL; AK011902; BAB27905.1; -; mRNA.
DR EMBL; AK146125; BAE26918.1; ALT_SEQ; mRNA.
DR EMBL; AK149625; BAE28994.1; -; mRNA.
DR EMBL; AK168356; BAE40292.1; ALT_SEQ; mRNA.
DR EMBL; BC037643; AAH37643.1; ALT_SEQ; mRNA.
DR CCDS; CCDS24072.1; -. [Q9JMH6-2]
DR CCDS; CCDS88064.1; -. [Q9JMH6-1]
DR RefSeq; NP_001035978.1; NM_001042513.1. [Q9JMH6-2]
DR RefSeq; NP_001035979.1; NM_001042514.1. [Q9JMH6-2]
DR RefSeq; NP_001035988.1; NM_001042523.1. [Q9JMH6-1]
DR RefSeq; NP_056577.2; NM_015762.2. [Q9JMH6-2]
DR BioGRID; 206041; 10.
DR IntAct; Q9JMH6; 1.
DR MINT; Q9JMH6; -.
DR STRING; 10090.ENSMUSP00000020484; -.
DR iPTMnet; Q9JMH6; -.
DR PhosphoSitePlus; Q9JMH6; -.
DR SwissPalm; Q9JMH6; -.
DR REPRODUCTION-2DPAGE; Q9JMH6; -.
DR EPD; Q9JMH6; -.
DR jPOST; Q9JMH6; -.
DR MaxQB; Q9JMH6; -.
DR PaxDb; Q9JMH6; -.
DR PeptideAtlas; Q9JMH6; -.
DR PRIDE; Q9JMH6; -.
DR ProteomicsDB; 297528; -. [Q9JMH6-1]
DR ProteomicsDB; 297529; -. [Q9JMH6-2]
DR Antibodypedia; 3897; 466 antibodies from 43 providers.
DR DNASU; 50493; -.
DR Ensembl; ENSMUST00000020484; ENSMUSP00000020484; ENSMUSG00000020250. [Q9JMH6-2]
DR Ensembl; ENSMUST00000219368; ENSMUSP00000151629; ENSMUSG00000020250. [Q9JMH6-1]
DR Ensembl; ENSMUST00000219442; ENSMUSP00000152046; ENSMUSG00000020250. [Q9JMH6-2]
DR Ensembl; ENSMUST00000219962; ENSMUSP00000151825; ENSMUSG00000020250. [Q9JMH6-2]
DR GeneID; 50493; -.
DR KEGG; mmu:50493; -.
DR UCSC; uc007gjy.1; mouse. [Q9JMH6-1]
DR CTD; 7296; -.
DR MGI; MGI:1354175; Txnrd1.
DR VEuPathDB; HostDB:ENSMUSG00000020250; -.
DR eggNOG; KOG4716; Eukaryota.
DR GeneTree; ENSGT00940000160180; -.
DR HOGENOM; CLU_016755_2_4_1; -.
DR InParanoid; Q9JMH6; -.
DR OMA; SGHAAWH; -.
DR OrthoDB; 581771at2759; -.
DR PhylomeDB; Q9JMH6; -.
DR TreeFam; TF314782; -.
DR BRENDA; 1.8.1.9; 3474.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-MMU-5263617; Metabolism of ingested MeSeO2H into MeSeH.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR SABIO-RK; Q9JMH6; -.
DR BioGRID-ORCS; 50493; 23 hits in 73 CRISPR screens.
DR ChiTaRS; Txnrd1; mouse.
DR PRO; PR:Q9JMH6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9JMH6; protein.
DR Bgee; ENSMUSG00000020250; Expressed in somite and 284 other tissues.
DR ExpressionAtlas; Q9JMH6; baseline and differential.
DR Genevisible; Q9JMH6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0045340; F:mercury ion binding; ISO:MGI.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; ISO:MGI.
DR GO; GO:0050137; F:NADPH peroxidase activity; ISS:UniProtKB.
DR GO; GO:0033797; F:selenate reductase activity; ISO:MGI.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:MGI.
DR GO; GO:0042537; P:benzene-containing compound metabolic process; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:MGI.
DR GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR GO; GO:0070995; P:NADPH oxidation; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0016259; P:selenocysteine metabolic process; ISO:MGI.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01438; TGR; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Phosphoprotein; Redox-active center; Reference proteome;
KW Selenocysteine; Ubl conjugation.
FT CHAIN 1..613
FT /note="Thioredoxin reductase 1, cytoplasmic"
FT /id="PRO_0000067982"
FT REGION 57..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 586
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 136..137
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 156..157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 172..173
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 177..181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 245..246
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 280
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 312..318
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 335..336
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 340..342
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 340
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O89049"
FT BINDING 406..407
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 429
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 448
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 455..457
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 455
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 586
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT NON_STD 612
FT /note="Selenocysteine"
FT /evidence="ECO:0000250"
FT MOD_RES 182
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 245
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT DISULFID 173..178
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CROSSLNK 611..612
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10721726,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_031566"
FT CONFLICT 238
FT /note="K -> E (in Ref. 3; BAE28994)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="Q -> R (in Ref. 3; BAE26918)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="L -> V (in Ref. 3; BAE26918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 67084 MW; C9FD2E2E8C55118C CRC64;
MPVDDCWLYF PASRGRTFVQ TVWVAPTCPN CCWFPGFLPP VPRPPHVPRV LLRGPRGAVL
PASRPSKTLP SSSQTPCPTD PCICPPPSTP DSRQEKNTQS ELPNKKGQLQ KLPTMNGSKD
PPGSYDFDLI IIGGGSGGLA AAKEAAKFDK KVLVLDFVTP TPLGTRWGLG GTCVNVGCIP
KKLMHQAALL GQALKDSRNY GWKVEDTVKH DWEKMTESVQ SHIGSLNWGY RVALREKKVV
YENAYGRFIG PHRIVATNNK GKEKIYSAER FLIATGERPR YLGIPGDKEY CISSDDLFSL
PYCPGKTLVV GASYVALECA GFLAGIGLDV TVMVRSILLR GFDQDMANKI GEHMEEHGIK
FIRQFVPTKI EQIEAGTPGR LRVTAQSTNS EETIEGEFNT VLLAVGRDSC TRTIGLETVG
VKINEKTGKI PVTDEEQTNV PYIYAIGDIL EGKLELTPVA IQAGRLLAQR LYGGSNVKCD
YDNVPTTVFT PLEYGCCGLS EEKAVEKFGE ENIEVYHSFF WPLEWTVPSR DNNKCYAKII
CNLKDDERVV GFHVLGPNAG EVTQGFAAAL KCGLTKQQLD STIGIHPVCA EIFTTLSVTK
RSGGDILQSG CUG
