TXNL1_HUMAN
ID TXNL1_HUMAN Reviewed; 289 AA.
AC O43396;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Thioredoxin-like protein 1;
DE AltName: Full=32 kDa thioredoxin-related protein;
GN Name=TXNL1; Synonyms=TRP32, TXL, TXNL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9473519; DOI=10.1006/bbrc.1997.8003;
RA Miranda-Vizuete A., Gustafsson J.-A., Spyrou G.;
RT "Molecular cloning and expression of a cDNA encoding a human thioredoxin-
RT like protein.";
RL Biochem. Biophys. Res. Commun. 243:284-288(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9668102; DOI=10.1074/jbc.273.30.19160;
RA Lee K.-K., Murakawa M., Takahashi S., Tsubuki S., Kawashima S.,
RA Sakamaki K., Yonehara S.;
RT "Purification, molecular cloning, and characterization of TRP32, a novel
RT thioredoxin-related mammalian protein of 32 kDa.";
RL J. Biol. Chem. 273:19160-19166(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10826702; DOI=10.3109/10425170009015613;
RA Miranda-Vizuete A., Spyrou G.;
RT "Genomic structure and chromosomal localization of human thioredoxin-like
RT protein gene (txl).";
RL DNA Seq. 10:419-424(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Zhou Y., Pan M.H., Yuan J.G., Qiang B.Q.;
RT "The discovery of a new gene that has high homology to the human
RT thioredoxin gene.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP PROTEIN SEQUENCE OF 2-23.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 238-259, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP FUNCTION, INTERACTION WITH PSMD14/RPN11 AND EEF1A1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19349277; DOI=10.1074/jbc.m900016200;
RA Andersen K.M., Madsen L., Prag S., Johnsen A.H., Semple C.A., Hendil K.B.,
RA Hartmann-Petersen R.;
RT "Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S
RT proteasome.";
RL J. Biol. Chem. 284:15246-15254(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-108, AND DISULFIDE BOND.
RX PubMed=11985582; DOI=10.1046/j.1432-1033.2002.02844.x;
RA Jin J., Chen X., Zhou Y., Bartlam M., Guo Q., Liu Y., Sun Y., Gao Y.,
RA Ye S., Li G., Rao Z., Qiang B., Yuan J.;
RT "Crystal structure of the catalytic domain of a human thioredoxin-like
RT protein.";
RL Eur. J. Biochem. 269:2060-2068(2002).
RN [14]
RP STRUCTURE BY NMR OF 122-279.
RX PubMed=20455272; DOI=10.1002/prot.22719;
RA Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Inoue M., Tanaka A.,
RA Sugano S., Kigawa T., Yokoyama S.;
RT "Solution structure of the C-terminal DUF1000 domain of the human
RT thioredoxin-like 1 protein.";
RL Proteins 78:2176-2180(2010).
CC -!- FUNCTION: Active thioredoxin with a redox potential of about -250 mV.
CC {ECO:0000269|PubMed:19349277}.
CC -!- SUBUNIT: Component of the 19S regulatory cap of the 26S proteasome.
CC Interacts with PSMD14/RPN11. Interacts with, and reduces EEF1A1.
CC {ECO:0000269|PubMed:19349277}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19349277}. Nucleus
CC {ECO:0000269|PubMed:19349277}. Note=At least 85% of the cellular TXNL1
CC is proteasome-associated.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
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DR EMBL; AF003938; AAC39599.1; -; mRNA.
DR EMBL; AF052659; AAC39898.1; -; mRNA.
DR EMBL; AF143897; AAF66676.1; -; Genomic_DNA.
DR EMBL; AF143890; AAF66676.1; JOINED; Genomic_DNA.
DR EMBL; AF143891; AAF66676.1; JOINED; Genomic_DNA.
DR EMBL; AF143892; AAF66676.1; JOINED; Genomic_DNA.
DR EMBL; AF143893; AAF66676.1; JOINED; Genomic_DNA.
DR EMBL; AF143894; AAF66676.1; JOINED; Genomic_DNA.
DR EMBL; AF143895; AAF66676.1; JOINED; Genomic_DNA.
DR EMBL; AF143896; AAF66676.1; JOINED; Genomic_DNA.
DR EMBL; AF051896; AAC05830.1; -; mRNA.
DR EMBL; BC001156; AAH01156.1; -; mRNA.
DR CCDS; CCDS11961.1; -.
DR PIR; JC5938; JC5938.
DR RefSeq; NP_004777.1; NM_004786.2.
DR RefSeq; XP_016881582.1; XM_017026093.1.
DR PDB; 1GH2; X-ray; 2.22 A; A=2-108.
DR PDB; 1WWY; NMR; -; A=122-279.
DR PDBsum; 1GH2; -.
DR PDBsum; 1WWY; -.
DR AlphaFoldDB; O43396; -.
DR BMRB; O43396; -.
DR SMR; O43396; -.
DR BioGRID; 114755; 174.
DR IntAct; O43396; 16.
DR MINT; O43396; -.
DR STRING; 9606.ENSP00000217515; -.
DR ChEMBL; CHEMBL4295663; -.
DR GlyGen; O43396; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43396; -.
DR MetOSite; O43396; -.
DR PhosphoSitePlus; O43396; -.
DR SwissPalm; O43396; -.
DR BioMuta; TXNL1; -.
DR OGP; O43396; -.
DR REPRODUCTION-2DPAGE; IPI00305692; -.
DR EPD; O43396; -.
DR jPOST; O43396; -.
DR MassIVE; O43396; -.
DR PaxDb; O43396; -.
DR PeptideAtlas; O43396; -.
DR PRIDE; O43396; -.
DR ProteomicsDB; 48922; -.
DR TopDownProteomics; O43396; -.
DR Antibodypedia; 1038; 211 antibodies from 28 providers.
DR DNASU; 9352; -.
DR Ensembl; ENST00000217515.11; ENSP00000217515.5; ENSG00000091164.13.
DR Ensembl; ENST00000590954.5; ENSP00000464918.1; ENSG00000091164.13.
DR GeneID; 9352; -.
DR KEGG; hsa:9352; -.
DR MANE-Select; ENST00000217515.11; ENSP00000217515.5; NM_004786.3; NP_004777.1.
DR CTD; 9352; -.
DR DisGeNET; 9352; -.
DR GeneCards; TXNL1; -.
DR HGNC; HGNC:12436; TXNL1.
DR HPA; ENSG00000091164; Low tissue specificity.
DR MIM; 603049; gene.
DR neXtProt; NX_O43396; -.
DR OpenTargets; ENSG00000091164; -.
DR PharmGKB; PA134967488; -.
DR VEuPathDB; HostDB:ENSG00000091164; -.
DR eggNOG; KOG0908; Eukaryota.
DR GeneTree; ENSGT00940000156170; -.
DR HOGENOM; CLU_072377_0_2_1; -.
DR InParanoid; O43396; -.
DR OMA; PIFEMFP; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; O43396; -.
DR TreeFam; TF314399; -.
DR PathwayCommons; O43396; -.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; O43396; -.
DR BioGRID-ORCS; 9352; 23 hits in 1079 CRISPR screens.
DR ChiTaRS; TXNL1; human.
DR EvolutionaryTrace; O43396; -.
DR GeneWiki; TXNL1; -.
DR GenomeRNAi; 9352; -.
DR Pharos; O43396; Tbio.
DR PRO; PR:O43396; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; O43396; protein.
DR Bgee; ENSG00000091164; Expressed in parotid gland and 209 other tissues.
DR ExpressionAtlas; O43396; baseline and differential.
DR Genevisible; O43396; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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; IDA:UniProtKB.
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 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Electron transport; Nucleus; Phosphoprotein; Proteasome;
KW Redox-active center; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..289
FT /note="Thioredoxin-like protein 1"
FT /id="PRO_0000120016"
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:23186163"
FT DISULFID 34..37
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:11985582"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1GH2"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1GH2"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:1GH2"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:1GH2"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:1GH2"
FT HELIX 35..50
FT /evidence="ECO:0007829|PDB:1GH2"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1GH2"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1GH2"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:1GH2"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:1GH2"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:1GH2"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:1GH2"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1WWY"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1WWY"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1WWY"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1WWY"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:1WWY"
FT STRAND 166..182
FT /evidence="ECO:0007829|PDB:1WWY"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1WWY"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:1WWY"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:1WWY"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:1WWY"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:1WWY"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:1WWY"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:1WWY"
SQ SEQUENCE 289 AA; 32251 MW; B2CC0BD8042225C2 CRC64;
MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK YPQAVFLEVD
VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE EKIKQHLEND PGSNEDTDIP
KGYMDLMPFI NKAGCECLNE SDEHGFDNCL RKDTTFLESD CDEQLLITVA FNQPVKLYSM
KFQGPDNGQG PKYVKIFINL PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN
VNSVTIFVQS NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH
