ID   TXNIP_PONAB             Reviewed;         391 AA.
AC   Q5R811;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Thioredoxin-interacting protein;
GN   Name=TXNIP;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR859944; CAH92099.1; -; mRNA.
DR   RefSeq; NP_001127507.1; NM_001134035.2.
DR   AlphaFoldDB; Q5R811; -.
DR   SMR; Q5R811; -.
DR   STRING; 9601.ENSPPYP00000001080; -.
DR   GeneID; 100174583; -.
DR   KEGG; pon:100174583; -.
DR   CTD; 10628; -.
DR   eggNOG; KOG3780; Eukaryota.
DR   InParanoid; Q5R811; -.
DR   OrthoDB; 817924at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0051782; P:negative regulation of cell division; ISS:UniProtKB.
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_0000250492"
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;  43604 MW;  B4B45215D8126233 CRC64;
     MVMFKKIKSF EVVFNDPEKV YGSGEKVAGR VIVEVCEVTR VKAVRILACG VAKVLWMQGS
     QQCKQTSEYL RYEDTLLLED QPTGENEMVI MRPGNKYEYK FGFELPQGPL GTSFKGKYGC
     VDYWVKAFLD RPSQPTQGTK KNFEVVDLVD VNTPDLMAPV SAKKEKKVSC MFIPDGRVSV
     SARIDRKGFC EGDEISIHAD FENTCSRIVV PKAAIVARHT YLANGQTKVL TQELSSVRGN
     HIISGTCASW RGKSLRVQKI RPSILGCNIL RVEYSLLIYV SVPGSKKVIL DLPLVIGSRS
     GLSSRTSSMA SRTSSEMSWV DLNIPDTPEA PPCYMDIIPE DHRLESPTTP LLDDMDGSQD
     SPIFMYAPEF KFMPPPTYTE VDPCILNNNV Q