ID   TXNL1_RAT               Reviewed;         289 AA.
AC   Q920J4;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Thioredoxin-like protein 1;
DE   AltName: Full=Thioredoxin-related protein;
GN   Name=Txnl1; Synonyms=Trp;
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 [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Tang H.B., Ip F.C.F., Cheung W.M.W., Ip N.Y.;
RT   "Cloning a novel rat thioredoxin-related protein.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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   [3]
RP   PROTEIN SEQUENCE OF 238-259, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Chen W.-Q.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Active thioredoxin with a redox potential of about -250 mV.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the 19S regulatory cap of the 26S proteasome.
CC       Interacts with PSMD14/RPN11. Interacts with, and reduces EEF1A1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=At least 85% of the cellular TXNL1 is proteasome-associated.
CC       {ECO:0000250}.
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DR   EMBL; AF140358; AAK98516.1; -; mRNA.
DR   EMBL; BC098908; AAH98908.1; -; mRNA.
DR   RefSeq; NP_543163.1; NM_080887.2.
DR   AlphaFoldDB; Q920J4; -.
DR   BMRB; Q920J4; -.
DR   SMR; Q920J4; -.
DR   BioGRID; 250856; 2.
DR   IntAct; Q920J4; 3.
DR   MINT; Q920J4; -.
DR   STRING; 10116.ENSRNOP00000025510; -.
DR   iPTMnet; Q920J4; -.
DR   PhosphoSitePlus; Q920J4; -.
DR   jPOST; Q920J4; -.
DR   PaxDb; Q920J4; -.
DR   PRIDE; Q920J4; -.
DR   Ensembl; ENSRNOT00000025510; ENSRNOP00000025510; ENSRNOG00000018818.
DR   GeneID; 140922; -.
DR   KEGG; rno:140922; -.
DR   UCSC; RGD:621717; rat.
DR   CTD; 9352; -.
DR   RGD; 621717; Txnl1.
DR   eggNOG; KOG0908; Eukaryota.
DR   GeneTree; ENSGT00940000156170; -.
DR   HOGENOM; CLU_072377_0_2_1; -.
DR   InParanoid; Q920J4; -.
DR   Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR   Reactome; R-RNO-9013420; RHOU GTPase cycle.
DR   Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR   Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR   Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR   Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR   Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR   PRO; PR:Q920J4; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Bgee; ENSRNOG00000018818; Expressed in thymus and 20 other tissues.
DR   ExpressionAtlas; Q920J4; baseline and differential.
DR   Genevisible; Q920J4; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; ISO:RGD.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR   Gene3D; 2.60.120.470; -; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR010400; PITH_dom.
DR   InterPro; IPR037047; PITH_dom_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF06201; PITH; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51532; PITH; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Disulfide bond; Electron transport;
KW   Nucleus; Phosphoprotein; Proteasome; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..289
FT                   /note="Thioredoxin-like protein 1"
FT                   /id="PRO_0000120018"
FT   DOMAIN          2..109
FT                   /note="Thioredoxin"
FT   DOMAIN          115..285
FT                   /note="PITH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00864"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   DISULFID        34..37
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  32249 MW;  208973DC16B61E01 CRC64;
     MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK YPQAVFLEVD
     VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE EKIKQHLEND PGSNEDTDIP
     KGYMDLMPFI NKAGCECLNE SDEHGFDNCL RKDLSFLESD CDEQLLITVA FNQPVKLYSM
     KFQGPDNGQG PKYVKIFINL PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN
     VNSVTLFVQS NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH