TXNIP_RAT
ID TXNIP_RAT Reviewed; 394 AA.
AC Q5M7W1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Thioredoxin-interacting protein;
DE AltName: Full=Vitamin D3 up-regulated protein 1;
GN Name=Txnip; Synonyms=Vdup1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with TXN/thioredoxin
CC through its redox-active site. Interacts with transcriptional
CC repressors ZBTB16, ZBTB32 and HDAC1 (By similarity). Interacts (via C-
CC terminus) with ITCH (via WW domains). Interacts with DDIT4 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Ubiquitinated; undergoes polyubiquitination catalyzed by ITCH
CC resulting in proteasomal degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC088411; AAH88411.1; -; mRNA.
DR RefSeq; NP_001008767.1; NM_001008767.1.
DR AlphaFoldDB; Q5M7W1; -.
DR SMR; Q5M7W1; -.
DR BioGRID; 250736; 1.
DR IntAct; Q5M7W1; 1.
DR STRING; 10116.ENSRNOP00000028793; -.
DR PhosphoSitePlus; Q5M7W1; -.
DR PaxDb; Q5M7W1; -.
DR PRIDE; Q5M7W1; -.
DR Ensembl; ENSRNOT00000028793; ENSRNOP00000028793; ENSRNOG00000021201.
DR GeneID; 117514; -.
DR KEGG; rno:117514; -.
DR UCSC; RGD:620886; rat.
DR CTD; 10628; -.
DR RGD; 620886; Txnip.
DR eggNOG; KOG3780; Eukaryota.
DR GeneTree; ENSGT00940000158522; -.
DR HOGENOM; CLU_039221_1_1_1; -.
DR InParanoid; Q5M7W1; -.
DR OMA; MVMFKKV; -.
DR OrthoDB; 817924at2759; -.
DR PhylomeDB; Q5M7W1; -.
DR Reactome; R-RNO-844456; The NLRP3 inflammasome.
DR PRO; PR:Q5M7W1; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000021201; Expressed in lung and 20 other tissues.
DR Genevisible; Q5M7W1; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
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:RGD.
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; ISO:RGD.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 2: Evidence at transcript level;
KW Cell cycle; Cytoplasm; Disulfide bond; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation.
FT CHAIN 1..394
FT /note="Thioredoxin-interacting protein"
FT /id="PRO_0000250493"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3M7"
FT DISULFID 63
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9H3M7"
SQ SEQUENCE 394 AA; 44018 MW; 6CE164C68D4B0CBC CRC64;
MVMFKKIKSF EVVFNDPEKV YGSGEKVAGR VTVEVCEVTR VKAVRILACG VAKVLWMQGS
QQCKQTLDYL RYEDTLLLED QPTGENEMVI MRPGNKYEYK FGFELPQGPL GTSFKGKYGC
VDYWVKAFLD RPSQPTQEAK KNFEVMDLVD VNTPDLMAPV SAKKEKKVSC MFIPDGRVSV
SARIDRKGFC EGDDISIHAD FENTCSRIVV PKAAIVARHT YLANGQTKVL TQKLSSVRGN
HIISGTCASW RGKSLRVQKI RPSILGCNIL RVEYSLLIYV SVPGSKKVIL DLPLVIGSRS
GLSSRTSSMA SRTSSEMSWI DLNIPDTPEA PPCYMDVIPE DHRLESPTTP LLDDVDDSQD
SPIFMYAPEF QFMPPPTYTE VDPCVLNNNN NNVQ
