TXNIP_MOUSE
ID TXNIP_MOUSE Reviewed; 397 AA.
AC Q8BG60; Q8BGQ0; Q8K2B2; Q9DC00; Q9EP90; Q9R115;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Thioredoxin-interacting protein;
DE AltName: Full=Vitamin D3 up-regulated protein 1;
GN Name=Txnip; Synonyms=Vdup1;
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), INTERACTION WITH TXN, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10843682; DOI=10.4049/jimmunol.164.12.6287;
RA Junn E., Han S.H., Im J.Y., Yang Y., Cho E.W., Um H.D., Kim D.K., Lee K.W.,
RA Han P.L., Rhee S.G., Choi I.;
RT "Vitamin D3 up-regulated protein 1 mediates oxidative stress via
RT suppressing the thioredoxin function.";
RL J. Immunol. 164:6287-6295(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=11376942; DOI=10.1016/s0378-1119(01)00455-3;
RA Ludwig D.L., Kotanides H., Le T., Chavkin D., Bohlen P., Witte L.;
RT "Cloning, genetic characterization, and chromosomal mapping of the mouse
RT VDUP1 gene.";
RL Gene 269:103-112(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Lung, and Thymus;
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=Czech II; 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 FUNCTION, AND INTERACTION WITH COPS5.
RX PubMed=15930262; DOI=10.1158/0008-5472.can-04-2271;
RA Jeon J.H., Lee K.N., Hwang C.Y., Kwon K.S., You K.H., Choi I.;
RT "Tumor suppressor VDUP1 increases p27(kip1) stability by inhibiting JAB1.";
RL Cancer Res. 65:4485-4489(2005).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15723808; DOI=10.1016/j.immuni.2004.12.012;
RA Lee K.N., Kang H.S., Jeon J.H., Kim E.M., Yoon S.R., Song H., Lyu C.Y.,
RA Piao Z.H., Kim S.U., Han Y.H., Song S.S., Lee Y.H., Song K.S., Kim Y.M.,
RA Yu D.Y., Choi I.;
RT "VDUP1 is required for the development of natural killer cells.";
RL Immunity 22:195-208(2005).
CC -!- FUNCTION: May act as an oxidative stress mediator by inhibiting
CC thioredoxin activity or by limiting its bioavailability. Interacts with
CC COPS5 and restores COPS5-induced suppression of CDKN1B stability,
CC blocking the COPS5-mediated translocation of CDKN1B from the nucleus to
CC the cytoplasm. Inhibits the proteasomal degradation of DDIT4, and
CC thereby contributes to the inhibition of the mammalian target of
CC rapamycin complex 1 (mTORC1) (By similarity). Functions as a
CC transcriptional repressor, possibly by acting as a bridge molecule
CC between transcription factors and corepressor complexes, and over-
CC expression will induce G0/G1 cell cycle arrest. Required for the
CC maturation of natural killer cells. Acts as a suppressor of tumor cell
CC growth. {ECO:0000250, ECO:0000269|PubMed:15723808,
CC ECO:0000269|PubMed:15930262}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with TXN/thioredoxin
CC through its redox-active site. Interacts with transcriptional
CC repressors ZBTB16, ZBTB32 and HDAC1. Interacts (via C-terminus) with
CC ITCH (via WW domains). Interacts with DDIT4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10843682}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BG60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BG60-2; Sequence=VSP_020653;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10843682}.
CC -!- PTM: Ubiquitinated; undergoes polyubiquitination catalyzed by ITCH
CC resulting in proteasomal degradation. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Marked reduction in the numbers of natural killer
CC cells, low levels of Il2rb expression in the precursor hematopoietic
CC stem cells and severe lymphoid hyperplasia in the small intestine.
CC {ECO:0000269|PubMed:15723808}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; AF173681; AAD48499.1; -; mRNA.
DR EMBL; AF282825; AAG32665.1; -; Genomic_DNA.
DR EMBL; AF282826; AAG32666.1; -; mRNA.
DR EMBL; AK004653; BAB23444.1; -; mRNA.
DR EMBL; AK082476; BAC38504.1; -; mRNA.
DR EMBL; AK088870; BAC40625.1; -; mRNA.
DR EMBL; AK089304; BAC40834.1; -; mRNA.
DR EMBL; AK089351; BAC40850.1; -; mRNA.
DR EMBL; AK089403; BAC40868.1; -; mRNA.
DR EMBL; AK155517; BAE33304.1; -; mRNA.
DR EMBL; AK171205; BAE42311.1; -; mRNA.
DR EMBL; AK171312; BAE42386.1; -; mRNA.
DR EMBL; AK171425; BAE42444.1; -; mRNA.
DR EMBL; AK171456; BAE42465.1; -; mRNA.
DR EMBL; AK171464; BAE42470.1; -; mRNA.
DR EMBL; AK171527; BAE42508.1; -; mRNA.
DR EMBL; BC031850; AAH31850.1; -; mRNA.
DR CCDS; CCDS17640.1; -. [Q8BG60-2]
DR CCDS; CCDS38555.1; -. [Q8BG60-1]
DR RefSeq; NP_001009935.1; NM_001009935.2. [Q8BG60-1]
DR RefSeq; NP_076208.2; NM_023719.2. [Q8BG60-2]
DR AlphaFoldDB; Q8BG60; -.
DR SMR; Q8BG60; -.
DR BioGRID; 207912; 1.
DR CORUM; Q8BG60; -.
DR IntAct; Q8BG60; 2.
DR MINT; Q8BG60; -.
DR STRING; 10090.ENSMUSP00000102710; -.
DR iPTMnet; Q8BG60; -.
DR PhosphoSitePlus; Q8BG60; -.
DR EPD; Q8BG60; -.
DR MaxQB; Q8BG60; -.
DR PaxDb; Q8BG60; -.
DR PeptideAtlas; Q8BG60; -.
DR PRIDE; Q8BG60; -.
DR ProteomicsDB; 298044; -. [Q8BG60-1]
DR ProteomicsDB; 298045; -. [Q8BG60-2]
DR Antibodypedia; 73170; 372 antibodies from 35 providers.
DR DNASU; 56338; -.
DR Ensembl; ENSMUST00000049093; ENSMUSP00000041467; ENSMUSG00000038393. [Q8BG60-2]
DR Ensembl; ENSMUST00000074519; ENSMUSP00000102710; ENSMUSG00000038393. [Q8BG60-1]
DR GeneID; 56338; -.
DR KEGG; mmu:56338; -.
DR UCSC; uc008qnc.2; mouse. [Q8BG60-1]
DR UCSC; uc008qnd.2; mouse. [Q8BG60-2]
DR CTD; 10628; -.
DR MGI; MGI:1889549; Txnip.
DR VEuPathDB; HostDB:ENSMUSG00000038393; -.
DR eggNOG; KOG3780; Eukaryota.
DR GeneTree; ENSGT00940000158522; -.
DR HOGENOM; CLU_039221_1_1_1; -.
DR InParanoid; Q8BG60; -.
DR OMA; MVMFKKV; -.
DR OrthoDB; 817924at2759; -.
DR PhylomeDB; Q8BG60; -.
DR TreeFam; TF313650; -.
DR Reactome; R-MMU-844456; The NLRP3 inflammasome.
DR BioGRID-ORCS; 56338; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Txnip; mouse.
DR PRO; PR:Q8BG60; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BG60; protein.
DR Bgee; ENSMUSG00000038393; Expressed in right lung and 276 other tissues.
DR Genevisible; Q8BG60; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071228; P:cellular response to tumor cell; ISS:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:MGI.
DR GO; GO:0051782; P:negative regulation of cell division; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 2.60.40.640; -; 2.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011021; Arrestin-like_N.
DR InterPro; IPR011022; Arrestin_C-like.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR SMART; SM01017; Arrestin_C; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cytoplasm; Disulfide bond;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..397
FT /note="Thioredoxin-interacting protein"
FT /id="PRO_0000250490"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3M7"
FT DISULFID 63
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9H3M7"
FT VAR_SEQ 84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10843682,
FT ECO:0000303|PubMed:11376942, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_020653"
FT CONFLICT 79
FT /note="E -> G (in Ref. 3; BAB23444)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="K -> E (in Ref. 1; AAD48499)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="P -> R (in Ref. 1; AAD48499)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="S -> F (in Ref. 2; AAG32665/AAG32666)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="N -> NN (in Ref. 4; AAH31850)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="Missing (in Ref. 1; AAD48499)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 44363 MW; C160781B207C99A6 CRC64;
MVMFKKIKSF EVVFNDPEKV YGSGEKVAGR VIVEVCEVTR VKAVRILACG VAKVLWMQGS
QQCKQTLDYL RYEDTLLLEE QPTAGENEMV IMRPGNKYEY KFGFELPQGP LGTSFKGKYG
CVDYWVKAFL DRPSQPTQEA KKNFEVMDLV DVNTPDLMAP VSAKKEKKVS CMFIPDGRVS
VSARIDRKGF CEGDDISIHA DFENTCSRIV VPKAAIVARH TYLANGQTKV FTQKLSSVRG
NHIISGTCAS WRGKSLRVQK IRPSILGCNI LKVEYSLLIY VSVPGSKKVI LDLPLVIGSR
SGLSSRTSSM ASRTSSEMSW IDLNIPDTPE APPCYMDIIP EDHRLESPTT PLLDDVDDSQ
DSPIFMYAPE FQFMPPPTYT EVDPCVLNNN NNNNNVQ
