TRXR1_HUMAN
ID TRXR1_HUMAN Reviewed; 649 AA.
AC Q16881; B7Z1F4; B7Z3Y8; B7Z904; E9PMY9; F5H780; Q6FI31; Q6VB40; Q6VB41;
AC Q6VB42; Q6VBP2; Q6VBP3; Q6VBP4; Q6VBP5; Q6VBP9; Q6VBQ0; Q6YNQ1; Q76P53;
AC Q7LA96; Q8WVC8; Q99475; Q9UES8; Q9UH79;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Thioredoxin reductase 1, cytoplasmic {ECO:0000305};
DE Short=TR;
DE EC=1.8.1.9 {ECO:0000269|PubMed:8577704};
DE AltName: Full=Gene associated with retinoic and interferon-induced mortality 12 protein;
DE Short=GRIM-12;
DE Short=Gene associated with retinoic and IFN-induced mortality 12 protein;
DE AltName: Full=KM-102-derived reductase-like factor;
DE AltName: Full=Peroxidase TXNRD1 {ECO:0000305|PubMed:10849437};
DE EC=1.11.1.2 {ECO:0000269|PubMed:10849437};
DE AltName: Full=Thioredoxin reductase TR1;
GN Name=TXNRD1 {ECO:0000312|HGNC:HGNC:12437}; Synonyms=GRIM12, KDRF;
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 5), PROTEIN SEQUENCE OF 153-161;
RP 307-315 AND 585-607, AND VARIANT GLY-365.
RC TISSUE=Placenta;
RX PubMed=7589432; DOI=10.1016/0014-5793(95)01003-w;
RA Gasdaska P.Y., Gasdaska J.R., Cochran S., Powis G.;
RT "Cloning and sequencing of a human thioredoxin reductase.";
RL FEBS Lett. 373:5-9(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF 122-127 AND
RP 147-151, AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow stroma;
RX PubMed=8999974; DOI=10.1074/jbc.272.4.2570;
RA Koishi R., Kawashima I., Yoshimura C., Sugawara M., Serizawa N.;
RT "Cloning and characterization of a novel oxidoreductase KDRF from a human
RT bone marrow-derived stromal cell line KM-102.";
RL J. Biol. Chem. 272:2570-2577(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, AND INDUCTION.
RC TISSUE=Mammary carcinoma;
RX PubMed=9774665; DOI=10.1128/mcb.18.11.6493;
RA Hofman E.R., Boyanapalli M., Lindner D.J., Weihua X., Hassel B.A.,
RA Jagus R., Gutierrez P.L., Kalvakolanu D.V.;
RT "Thioredoxin reductase mediates cell death effects of the combination of
RT beta interferon and retinoic acid.";
RL Mol. Cell. Biol. 18:6493-6504(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [MRNA]
RP (ISOFORMS 2; 3; 4 AND 5), AND VARIANT GLY-365.
RC TISSUE=Mammary gland, Ovary, Testis, and Thymus;
RX PubMed=14980707; DOI=10.1016/j.freeradbiomed.2003.12.004;
RA Rundloef A.-K., Janard M., Miranda-Vizuete A., Arner E.S.;
RT "Evidence for intriguingly complex transcription of human thioredoxin
RT reductase 1.";
RL Free Radic. Biol. Med. 36:641-656(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Schuetze N., Bachthaler M., Lechner A., Koehrle J., Jakob F.;
RT "Identification by ddPCR of thioredoxin reductase as a vitamin D regulated
RT gene in human osteoblasts.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RA Xu L., Dai R., Xu J.Y.;
RT "Cloning and sequencing of thioredoxin reductase gene from human brain.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Astrocyte, Thalamus, and Trachea;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC TISSUE=Trachea;
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 [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Lung;
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 [14]
RP PROTEIN SEQUENCE OF 307-316; 449-456; 466-476 AND 638-649, BLOCKAGE OF
RP N-TERMINUS, SELENOCYSTEINE AT SEC-648, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=8650234; DOI=10.1073/pnas.93.12.6146;
RA Gladyshev V.N., Jeang K.-T., Stadtman T.C.;
RT "Selenocysteine, identified as the penultimate C-terminal residue in human
RT T-cell thioredoxin reductase, corresponds to TGA in the human placental
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6146-6151(1996).
RN [15]
RP FUNCTION, HOMODIMERIZATION, CHARACTERIZATION, PRESENCE OF SELENOCYSTEINE,
RP COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=8577704; DOI=10.1073/pnas.93.3.1006;
RA Tamura T., Stadtman T.C.;
RT "A new selenoprotein from human lung adenocarcinoma cells: purification,
RT properties, and thioredoxin reductase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1006-1011(1996).
RN [16]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=10849437; DOI=10.1074/jbc.m000690200;
RA Zhong L., Holmgren A.;
RT "Essential role of selenium in the catalytic activities of mammalian
RT thioredoxin reductase revealed by characterization of recombinant enzymes
RT with selenocysteine mutations.";
RL J. Biol. Chem. 275:18121-18128(2000).
RN [17]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5 AND 6), AND DOMAIN.
RX PubMed=15379556; DOI=10.1021/bi048478t;
RA Su D., Gladyshev V.N.;
RT "Alternative splicing involving the thioredoxin reductase module in
RT mammals: a glutaredoxin-containing thioredoxin reductase 1.";
RL Biochemistry 43:12177-12188(2004).
RN [18]
RP FUNCTION, INTERACTION WITH ESR1 AND ESR2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY (ISOFORM 4).
RX PubMed=15199063; DOI=10.1074/jbc.m402753200;
RA Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A.,
RA Spyrou G.;
RT "An alternative splicing variant of the selenoprotein thioredoxin reductase
RT is a modulator of estrogen signaling.";
RL J. Biol. Chem. 279:38721-38729(2004).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-281, 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 [20]
RP INTERACTION WITH HERC5, AND ISGYLATION.
RX PubMed=16815975; DOI=10.1073/pnas.0600397103;
RA Wong J.J., Pung Y.F., Sze N.S., Chin K.C.;
RT "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I
RT IFN-induced ISGylation of protein targets.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006).
RN [21]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION (ISOFORM 1).
RX PubMed=18042542; DOI=10.1074/jbc.m708939200;
RA Dammeyer P., Damdimopoulos A.E., Nordman T., Jimenez A.,
RA Miranda-Vizuete A., Arner E.S.J.;
RT "Induction of cell membrane protrusions by the N-terminal glutaredoxin
RT domain of a rare splice variant of human thioredoxin reductase 1.";
RL J. Biol. Chem. 283:2814-2821(2008).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 5), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 5), 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] {ECO:0007744|PDB:2J3N}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) (ISOFORM 5) IN COMPLEX WITH FAD AND
RP NADPH, COFACTOR, AND SUBUNIT.
RX PubMed=17512005; DOI=10.1016/j.jmb.2007.04.044;
RA Fritz-Wolf K., Urig S., Becker K.;
RT "The structure of human thioredoxin reductase 1 provides insights into C-
RT terminal rearrangements during catalysis.";
RL J. Mol. Biol. 370:116-127(2007).
CC -!- FUNCTION: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-
CC containing form (PubMed:8577704). Homodimeric flavoprotein involved in
CC the regulation of cellular redox reactions, growth and differentiation.
CC Contains a selenocysteine residue at the C-terminal active site that is
CC essential for catalysis (Probable). Also has reductase activity on
CC hydrogen peroxide (H2O2) (PubMed:10849437).
CC {ECO:0000269|PubMed:10849437, ECO:0000269|PubMed:8577704,
CC ECO:0000305|PubMed:17512005}.
CC -!- FUNCTION: [Isoform 1]: Induces actin and tubulin polymerization,
CC leading to formation of cell membrane protrusions.
CC {ECO:0000269|PubMed:18042542, ECO:0000269|PubMed:8577704}.
CC -!- FUNCTION: [Isoform 4]: Enhances the transcriptional activity of
CC estrogen receptors ESR1 and ESR2. {ECO:0000269|PubMed:15199063}.
CC -!- FUNCTION: [Isoform 5]: Enhances the transcriptional activity of the
CC estrogen receptor ESR2 only (PubMed:15199063). Mediates cell death
CC induced by a combination of interferon-beta and retinoic acid
CC (PubMed:9774665). {ECO:0000269|PubMed:15199063,
CC ECO:0000269|PubMed:9774665}.
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:0000269|PubMed:8577704};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347;
CC Evidence={ECO:0000305|PubMed:8577704};
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:0000269|PubMed:10849437};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15174;
CC Evidence={ECO:0000305|PubMed:10849437};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:17512005,
CC ECO:0000269|PubMed:8577704};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 mM for H202 {ECO:0000269|PubMed:10849437};
CC Note=kcat is 100 min(-1) with H2O2 as substrate.
CC {ECO:0000269|PubMed:10849437};
CC -!- SUBUNIT: Homodimer (PubMed:17512005, PubMed:8577704). Interacts with
CC HERC5. {ECO:0000269|PubMed:16815975, ECO:0000269|PubMed:17512005,
CC ECO:0000269|PubMed:8577704}.
CC -!- SUBUNIT: [Isoform 4]: Interacts with ESR1 and ESR2.
CC {ECO:0000269|PubMed:16815975}.
CC -!- INTERACTION:
CC Q16881; Q03135: CAV1; NbExp=4; IntAct=EBI-716617, EBI-603614;
CC Q16881-4; P03372: ESR1; NbExp=4; IntAct=EBI-9080335, EBI-78473;
CC Q16881-4; Q92731: ESR2; NbExp=3; IntAct=EBI-9080335, EBI-78505;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:18042542}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm
CC {ECO:0000269|PubMed:15199063}. Nucleus {ECO:0000269|PubMed:15199063}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm
CC {ECO:0000269|PubMed:15199063}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=V, TXNRD1_v3 {ECO:0000303|PubMed:18042542};
CC IsoId=Q16881-1; Sequence=Displayed;
CC Name=2; Synonyms=II, TXNRD1_v4;
CC IsoId=Q16881-2; Sequence=VSP_031560, VSP_031565;
CC Name=3; Synonyms=III, TXNRD1_v5;
CC IsoId=Q16881-3; Sequence=VSP_031562, VSP_031563;
CC Name=4; Synonyms=IV, TXNRD1_v2, TrxR1b {ECO:0000303|PubMed:15199063};
CC IsoId=Q16881-4; Sequence=VSP_031561, VSP_031564;
CC Name=5; Synonyms=I, TXNRD1_v1, TrxR1a {ECO:0000303|PubMed:15199063};
CC IsoId=Q16881-5; Sequence=VSP_031558;
CC Name=6; Synonyms=VI;
CC IsoId=Q16881-6; Sequence=VSP_031559;
CC Name=7;
CC IsoId=Q16881-7; Sequence=VSP_053819;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed predominantly in Leydig
CC cells (at protein level). Also expressed in ovary, spleen, heart,
CC liver, kidney and pancreas and in a number of cancer cell lines.
CC {ECO:0000269|PubMed:18042542}.
CC -!- TISSUE SPECIFICITY: [Isoform 4]: Widely expressed with highest levels
CC in kidney, testis, uterus, ovary, prostate, placenta and fetal liver.
CC {ECO:0000269|PubMed:8999974}.
CC -!- INDUCTION: [Isoform 1]: Induced by estradiol or testosterone in HeLa
CC cells. {ECO:0000269|PubMed:18042542}.
CC -!- INDUCTION: [Isoform 5]: Induced by a combination of interferon-beta and
CC retinoic acid (at protein level). {ECO:0000269|PubMed:9774665}.
CC -!- DOMAIN: [Isoform 1]: The N-terminal glutaredoxin domain does not
CC contain the C-P-Y-C redox-active motif normally found in glutaredoxins
CC and has been found to be inactive in classical glutaredoxin assays.
CC {ECO:0000269|PubMed:15379556}.
CC -!- PTM: [Isoform 5]: The N-terminus is blocked.
CC -!- PTM: ISGylated. {ECO:0000305|PubMed:16815975}.
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 -!- MISCELLANEOUS: [Isoform 1]: Minor isoform.
CC {ECO:0000269|PubMed:18042542}.
CC -!- MISCELLANEOUS: [Isoform 5]: Major isoform. The N-terminus of the
CC sequence is processed into a mature form that lacks residues Met-151
CC and Asn-152 at the N-terminus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB35418.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC69621.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF15900.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV38446.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAZ67916.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA13674.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH11490.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH12374.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH14140.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA04503.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA62629.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAG38744.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW97745.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/txnrd1/";
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DR EMBL; X91247; CAA62629.1; ALT_SEQ; mRNA.
DR EMBL; S79851; AAB35418.1; ALT_SEQ; mRNA.
DR EMBL; D88687; BAA13674.1; ALT_SEQ; mRNA.
DR EMBL; AF077367; AAC69621.1; ALT_SEQ; mRNA.
DR EMBL; AY057105; AAL15432.1; -; mRNA.
DR EMBL; AY344081; AAQ62461.1; -; mRNA.
DR EMBL; AY344083; AAQ62462.1; -; mRNA.
DR EMBL; AY344084; AAQ62463.1; -; mRNA.
DR EMBL; AY344086; AAQ62464.1; -; mRNA.
DR EMBL; AY344087; AAQ62465.1; -; mRNA.
DR EMBL; AY344089; AAQ62466.1; -; mRNA.
DR EMBL; AY344092; AAQ62467.1; -; mRNA.
DR EMBL; AY344093; AAQ62468.1; -; mRNA.
DR EMBL; AY344095; AAQ62469.1; -; mRNA.
DR EMBL; AY344096; AAQ62470.1; -; mRNA.
DR EMBL; AY344670; AAQ62471.1; -; mRNA.
DR EMBL; AY344673; AAQ62472.1; -; mRNA.
DR EMBL; AY344679; AAQ62473.1; -; mRNA.
DR EMBL; AJ001050; CAA04503.1; ALT_SEQ; mRNA.
DR EMBL; AF208018; AAF15900.1; ALT_SEQ; mRNA.
DR EMBL; AK293322; BAH11490.1; ALT_SEQ; mRNA.
DR EMBL; AK296495; BAH12374.1; ALT_SEQ; mRNA.
DR EMBL; AK304241; BAH14140.1; ALT_SEQ; mRNA.
DR EMBL; CR536506; CAG38744.1; ALT_SEQ; mRNA.
DR EMBL; BT019640; AAV38446.1; ALT_SEQ; mRNA.
DR EMBL; DQ157758; AAZ67916.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC089983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97745.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC018122; AAH18122.2; -; mRNA.
DR CCDS; CCDS53820.1; -. [Q16881-1]
DR CCDS; CCDS53821.1; -. [Q16881-4]
DR CCDS; CCDS53823.1; -. [Q16881-5]
DR CCDS; CCDS58274.1; -. [Q16881-7]
DR PIR; S66677; S66677.
DR RefSeq; NP_001087240.1; NM_001093771.2. [Q16881-1]
DR RefSeq; NP_001248374.1; NM_001261445.1.
DR RefSeq; NP_001248375.1; NM_001261446.1. [Q16881-7]
DR RefSeq; NP_003321.3; NM_003330.3. [Q16881-4]
DR RefSeq; NP_877393.1; NM_182729.2. [Q16881-5]
DR RefSeq; NP_877419.1; NM_182742.2. [Q16881-5]
DR RefSeq; NP_877420.1; NM_182743.2. [Q16881-5]
DR PDB; 2CFY; X-ray; 2.70 A; A/B/C/D/E/F=151-647.
DR PDB; 2J3N; X-ray; 2.80 A; A/B/C/D/E/F=151-647.
DR PDB; 2ZZ0; X-ray; 2.80 A; A/B/C/D=150-647.
DR PDB; 2ZZB; X-ray; 3.20 A; A/B/C/D=150-647.
DR PDB; 2ZZC; X-ray; 2.60 A; A/B/C/D=150-647.
DR PDB; 3QFA; X-ray; 2.20 A; A/B=151-649.
DR PDB; 3QFB; X-ray; 2.60 A; A/B=151-649.
DR PDBsum; 2CFY; -.
DR PDBsum; 2J3N; -.
DR PDBsum; 2ZZ0; -.
DR PDBsum; 2ZZB; -.
DR PDBsum; 2ZZC; -.
DR PDBsum; 3QFA; -.
DR PDBsum; 3QFB; -.
DR SMR; Q16881; -.
DR BioGRID; 113147; 68.
DR IntAct; Q16881; 17.
DR MINT; Q16881; -.
DR STRING; 9606.ENSP00000434516; -.
DR BindingDB; Q16881; -.
DR ChEMBL; CHEMBL1927; -.
DR DrugBank; DB01169; Arsenic trioxide.
DR DrugBank; DB00126; Ascorbic acid.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB04106; Fotemustine.
DR DrugBank; DB05428; Motexafin gadolinium.
DR DrugBank; DB02338; NADPH.
DR DrugBank; DB05448; PX-12.
DR DrugBank; DB11127; Selenious acid.
DR DrugBank; DB11135; Selenium.
DR DrugBank; DB03566; Spermidine.
DR DrugCentral; Q16881; -.
DR GlyGen; Q16881; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16881; -.
DR MetOSite; Q16881; -.
DR PhosphoSitePlus; Q16881; -.
DR SwissPalm; Q16881; -.
DR BioMuta; TXNRD1; -.
DR DMDM; 172046253; -.
DR REPRODUCTION-2DPAGE; IPI00554786; -.
DR EPD; Q16881; -.
DR jPOST; Q16881; -.
DR MassIVE; Q16881; -.
DR MaxQB; Q16881; -.
DR PaxDb; Q16881; -.
DR PeptideAtlas; Q16881; -.
DR PRIDE; Q16881; -.
DR ProteomicsDB; 22254; -.
DR ProteomicsDB; 27407; -.
DR ProteomicsDB; 61119; -. [Q16881-1]
DR ProteomicsDB; 61120; -. [Q16881-2]
DR ProteomicsDB; 61121; -. [Q16881-3]
DR ProteomicsDB; 61122; -. [Q16881-4]
DR ProteomicsDB; 61123; -. [Q16881-5]
DR ProteomicsDB; 61124; -. [Q16881-6]
DR Antibodypedia; 3897; 466 antibodies from 43 providers.
DR DNASU; 7296; -.
DR Ensembl; ENST00000503506.6; ENSP00000421934.2; ENSG00000198431.17. [Q16881-5]
DR Ensembl; ENST00000524698.5; ENSP00000433425.1; ENSG00000198431.17. [Q16881-5]
DR Ensembl; ENST00000525566.6; ENSP00000434516.1; ENSG00000198431.17. [Q16881-1]
DR Ensembl; ENST00000526390.5; ENSP00000435123.1; ENSG00000198431.17. [Q16881-2]
DR Ensembl; ENST00000526691.5; ENSP00000435929.1; ENSG00000198431.17. [Q16881-4]
DR Ensembl; ENST00000529546.5; ENSP00000434919.1; ENSG00000198431.17. [Q16881-7]
DR GeneID; 7296; -.
DR KEGG; hsa:7296; -.
DR MANE-Select; ENST00000525566.6; ENSP00000434516.1; NM_001093771.3; NP_001087240.1.
DR UCSC; uc010swp.4; human. [Q16881-1]
DR CTD; 7296; -.
DR DisGeNET; 7296; -.
DR GeneCards; TXNRD1; -.
DR HGNC; HGNC:12437; TXNRD1.
DR HPA; ENSG00000198431; Low tissue specificity.
DR MIM; 601112; gene.
DR neXtProt; NX_Q16881; -.
DR OpenTargets; ENSG00000198431; -.
DR PharmGKB; PA37093; -.
DR VEuPathDB; HostDB:ENSG00000198431; -.
DR eggNOG; KOG1752; Eukaryota.
DR eggNOG; KOG4716; Eukaryota.
DR GeneTree; ENSGT00940000160180; -.
DR HOGENOM; CLU_016755_2_4_1; -.
DR InParanoid; Q16881; -.
DR OrthoDB; 581771at2759; -.
DR PhylomeDB; Q16881; -.
DR TreeFam; TF314782; -.
DR BRENDA; 1.8.1.9; 2681.
DR PathwayCommons; Q16881; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2408550; Metabolism of ingested H2SeO4 and H2SeO3 into H2Se.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-HSA-5263617; Metabolism of ingested MeSeO2H into MeSeH.
DR Reactome; R-HSA-5336415; Uptake and function of diphtheria toxin.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR SignaLink; Q16881; -.
DR BioGRID-ORCS; 7296; 331 hits in 1096 CRISPR screens.
DR ChiTaRS; TXNRD1; human.
DR EvolutionaryTrace; Q16881; -.
DR GeneWiki; TXNRD1; -.
DR GenomeRNAi; 7296; -.
DR Pharos; Q16881; Tclin.
DR PRO; PR:Q16881; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q16881; protein.
DR Bgee; ENSG00000198431; Expressed in stromal cell of endometrium and 212 other tissues.
DR ExpressionAtlas; Q16881; baseline and differential.
DR Genevisible; Q16881; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0050137; F:NADPH peroxidase activity; IDA:UniProtKB.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
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; IPR002109; Glutaredoxin.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01438; TGR; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Electron transport; FAD;
KW Flavoprotein; NADP; Nucleus; Oxidoreductase; Phosphoprotein;
KW Redox-active center; Reference proteome; Selenocysteine; Transport;
KW Ubl conjugation.
FT CHAIN 1..649
FT /note="Thioredoxin reductase 1, cytoplasmic"
FT /id="PRO_0000030286"
FT DOMAIN 56..156
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..149
FT /note="Required for interaction with ESR1 and ESR2"
FT /evidence="ECO:0000269|PubMed:15199063"
FT COMPBIAS 21..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 622
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 172..173
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 192..193
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 208..209
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 213..217
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 281..282
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2J3N"
FT BINDING 316
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 348..354
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 350
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2ZZ0, ECO:0007744|PDB:2ZZB,
FT ECO:0007744|PDB:3QFA"
FT BINDING 371..372
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 376..378
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 376
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O89049"
FT BINDING 442..443
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 465
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 484
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 491..493
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT BINDING 491
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:2J3N"
FT BINDING 622
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17512005,
FT ECO:0007744|PDB:2J3N"
FT NON_STD 648
FT /note="Selenocysteine"
FT /evidence="ECO:0000269|PubMed:8650234"
FT MOD_RES 218
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH6"
FT MOD_RES 281
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT DISULFID 209..214
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CROSSLNK 647..648
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..188
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053819"
FT VAR_SEQ 1..150
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7589432, ECO:0000303|PubMed:9774665,
FT ECO:0000303|Ref.5, ECO:0000303|Ref.6, ECO:0000303|Ref.8,
FT ECO:0000303|Ref.9"
FT /id="VSP_031558"
FT VAR_SEQ 1..139
FT /note="MGCAEGKAVAAAAPTELQTKGKNGDGRRRSAKDHHPGKTLPENPAGFTSTAT
FT ADSRALLQAYIDGHSVVIFSRSTCTRCTEVKKLFKSLCVPYFVLELDQTEDGRALEGTL
FT SELAAETDLPVVFVKQRKIGGHGPTLKA -> MPVDDYWLCLPASCARPFVQTVRVVQS
FT CPHCCWFPGVLPSVPEPLRMPAMLPTGSHSAVLPPSHCSTAPPSTSQEPSSSADPKLCL
FT SPPTSDSRQERNVQFGLA (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_031559"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_031560"
FT VAR_SEQ 1..98
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8999974"
FT /id="VSP_031561"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_031562"
FT VAR_SEQ 52..100
FT /note="TADSRALLQAYIDGHSVVIFSRSTCTRCTEVKKLFKSLCVPYFVLELDQ ->
FT MQQVMLTCKGVNRGHAVPAGPGRKPRPRRSSRLLAGEKHLTRSALLLCH (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_031563"
FT VAR_SEQ 99..101
FT /note="DQT -> MSC (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8999974"
FT /id="VSP_031564"
FT VAR_SEQ 107..138
FT /note="LEGTLSELAAETDLPVVFVKQRKIGGHGPTLK -> MLSRLVLNSWAQAIIR
FT PRPPKVLGLQVTTFSE (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_031565"
FT VARIANT 365
FT /note="D -> G (in dbSNP:rs1127954)"
FT /evidence="ECO:0000269|PubMed:14980707,
FT ECO:0000269|PubMed:7589432"
FT /id="VAR_051776"
FT CONFLICT 153
FT /note="G -> S (in Ref. 4; AAQ62473)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="A -> P (in Ref. 6; AAF15900)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="V -> G (in Ref. 6; AAF15900)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="G -> E (in Ref. 4; AAQ62469)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="R -> K (in Ref. 4; AAQ62463)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="I -> N (in Ref. 4; AAQ62463)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="G -> D (in Ref. 7; BAH11490)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="R -> S (in Ref. 1; AAB35418/CAA62629 and 4;
FT AAL15432)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="D -> N (in Ref. 3; AAC69621)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="V -> A (in Ref. 7; BAH12374)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="I -> M (in Ref. 7; BAH12374)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="K -> R (in Ref. 8; CAG38744)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="S -> R (in Ref. 3; AAC69621)"
FT /evidence="ECO:0000305"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 214..233
FT /evidence="ECO:0007829|PDB:3QFA"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 248..272
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:2ZZ0"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 366..372
FT /evidence="ECO:0007829|PDB:3QFA"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:2ZZ0"
FT HELIX 380..392
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 396..410
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2J3N"
FT STRAND 416..427
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 429..439
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:3QFA"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:3QFA"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 493..508
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 537..544
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 549..556
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 559..562
FT /evidence="ECO:0007829|PDB:3QFA"
FT TURN 563..565
FT /evidence="ECO:0007829|PDB:3QFA"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 571..578
FT /evidence="ECO:0007829|PDB:3QFA"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:3QFA"
FT STRAND 584..592
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 595..607
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 612..617
FT /evidence="ECO:0007829|PDB:3QFA"
FT HELIX 625..631
FT /evidence="ECO:0007829|PDB:3QFA"
FT TURN 636..639
FT /evidence="ECO:0007829|PDB:3QFA"
FT MOD_RES Q16881-5:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
SQ SEQUENCE 649 AA; 70906 MW; 5A51C3F77EB03EFE CRC64;
MGCAEGKAVA AAAPTELQTK GKNGDGRRRS AKDHHPGKTL PENPAGFTST ATADSRALLQ
AYIDGHSVVI FSRSTCTRCT EVKKLFKSLC VPYFVLELDQ TEDGRALEGT LSELAAETDL
PVVFVKQRKI GGHGPTLKAY QEGRLQKLLK MNGPEDLPKS YDYDLIIIGG GSGGLAAAKE
AAQYGKKVMV LDFVTPTPLG TRWGLGGTCV NVGCIPKKLM HQAALLGQAL QDSRNYGWKV
EETVKHDWDR MIEAVQNHIG SLNWGYRVAL REKKVVYENA YGQFIGPHRI KATNNKGKEK
IYSAERFLIA TGERPRYLGI PGDKEYCISS DDLFSLPYCP GKTLVVGASY VALECAGFLA
GIGLDVTVMV RSILLRGFDQ DMANKIGEHM EEHGIKFIRQ FVPIKVEQIE AGTPGRLRVV
AQSTNSEEII EGEYNTVMLA IGRDACTRKI GLETVGVKIN EKTGKIPVTD EEQTNVPYIY
AIGDILEDKV ELTPVAIQAG RLLAQRLYAG STVKCDYENV PTTVFTPLEY GACGLSEEKA
VEKFGEENIE VYHSYFWPLE WTIPSRDNNK CYAKIICNTK DNERVVGFHV LGPNAGEVTQ
GFAAALKCGL TKKQLDSTIG IHPVCAEVFT TLSVTKRSGA SILQAGCUG
