TXNIP_PIG
ID TXNIP_PIG Reviewed; 391 AA.
AC Q2HY40; A5J2A7; Q09W51;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Thioredoxin-interacting protein;
GN Name=TXNIP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17406940; DOI=10.1007/s00335-007-9006-8;
RA Yu M., Geiger B., Deeb N., Rothschild M.F.;
RT "Investigation of TXNIP (thioredoxin-interacting protein) and TRX
RT (thioredoxin) genes for growth-related traits in pigs.";
RL Mamm. Genome 18:197-209(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Xu D.Q., Ling X.F., Xiong Y.Z.;
RT "Polymorphism and association with production traits of porcine TXNIP
RT gene.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Xu D.Q., Xiong Y.Z.;
RT "Molecular cloning and characterization of porcine TXNIP.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; DQ991395; ABL84738.1; -; Genomic_DNA.
DR EMBL; DQ278874; ABB97472.1; -; Genomic_DNA.
DR EMBL; DQ365929; ABC94953.1; -; mRNA.
DR RefSeq; NP_001038079.1; NM_001044614.2.
DR AlphaFoldDB; Q2HY40; -.
DR SMR; Q2HY40; -.
DR STRING; 9823.ENSSSCP00000007124; -.
DR PaxDb; Q2HY40; -.
DR PeptideAtlas; Q2HY40; -.
DR PRIDE; Q2HY40; -.
DR Ensembl; ENSSSCT00000055984; ENSSSCP00000035217; ENSSSCG00000031262.
DR Ensembl; ENSSSCT00005038053; ENSSSCP00005023346; ENSSSCG00005023907.
DR Ensembl; ENSSSCT00015048815; ENSSSCP00015019435; ENSSSCG00015036534.
DR Ensembl; ENSSSCT00025096449; ENSSSCP00025042339; ENSSSCG00025069926.
DR Ensembl; ENSSSCT00030097657; ENSSSCP00030044985; ENSSSCG00030069782.
DR Ensembl; ENSSSCT00035093696; ENSSSCP00035039327; ENSSSCG00035069373.
DR Ensembl; ENSSSCT00040067050; ENSSSCP00040028462; ENSSSCG00040049344.
DR Ensembl; ENSSSCT00045054397; ENSSSCP00045037875; ENSSSCG00045031705.
DR Ensembl; ENSSSCT00050101744; ENSSSCP00050044295; ENSSSCG00050074320.
DR Ensembl; ENSSSCT00055053979; ENSSSCP00055043074; ENSSSCG00055027208.
DR Ensembl; ENSSSCT00060031550; ENSSSCP00060013521; ENSSSCG00060023252.
DR Ensembl; ENSSSCT00065000529; ENSSSCP00065000095; ENSSSCG00065000466.
DR Ensembl; ENSSSCT00070002822; ENSSSCP00070002327; ENSSSCG00070001501.
DR GeneID; 733688; -.
DR KEGG; ssc:733688; -.
DR CTD; 10628; -.
DR VGNC; VGNC:94610; TXNIP.
DR eggNOG; KOG3780; Eukaryota.
DR GeneTree; ENSGT00940000158522; -.
DR HOGENOM; CLU_039221_1_1_1; -.
DR InParanoid; Q2HY40; -.
DR OMA; MVMFKKV; -.
DR OrthoDB; 817924at2759; -.
DR TreeFam; TF313650; -.
DR Reactome; R-SSC-844456; The NLRP3 inflammasome.
DR Proteomes; UP000008227; Chromosome 4.
DR Proteomes; UP000314985; Chromosome 4.
DR Bgee; ENSSSCG00000031262; Expressed in subcutaneous adipose tissue and 43 other tissues.
DR ExpressionAtlas; Q2HY40; baseline and differential.
DR Genevisible; Q2HY40; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; 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 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..391
FT /note="Thioredoxin-interacting protein"
FT /id="PRO_0000250491"
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 391 AA; 43811 MW; 8A634496EDD36A0B CRC64;
MVMFKKIKSF EVVFNDPEKV YGCGEKVAGR VIVEVCEVTR IKAVRILACG VAKVLWMQGS
QQCKQTLDYL RYEDTLLLDD HPTGENEMVI MRPGNKYEYK FGFELPQGPL GTSFKGKYGC
VDYWVKAFLD RPSQPTQETK KHFEVMDLVD VNTPDLMAPV SAKKEKKVSC MFIPDGRVSV
SARIDRKGFC EGDEINIHAD FENTCSRIVV PKAAIVARHT YLANGQTKVL TQKLSSVRGN
HIISGTCASW RGKSLRVQKI RPSILGCNIL RVEYFLLIYV SVPGSKKVIL DLPLVIGSRS
GLSSRTSSMA SRTSSEMSWV DLNIPDTPEA PPCYMDIIPE DHRLESPTTP LLDDTDGSQD
SPIFMYAPEF KFMPPPTYSE VDPCILNNNV Q