Full text data of TXNL1
TXNL1
(TRP32, TXL, TXNL)
[Confidence: low (only semi-automatic identification from reviews)]
Thioredoxin-like protein 1 (32 kDa thioredoxin-related protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Thioredoxin-like protein 1 (32 kDa thioredoxin-related protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43396
ID TXNL1_HUMAN Reviewed; 289 AA.
AC O43396;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 134.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT thioredoxin-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
RT novel 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;
RA Miranda-Vizuete A., Spyrou G.;
RT "Genomic structure and chromosomal localization of human thioredoxin-
RT like 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 238-259, AND 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.,
RA Hendil K.B., 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.,
RA Buerckstuemmer T., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
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 [13]
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
CC mV.
CC -!- SUBUNIT: Component of the 19S regulatory cap of the 26S
CC proteasome. Interacts with PSMD14/RPN11. Interacts with, and
CC reduces EEF1A1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=At least 85% of the
CC cellular TXNL1 is proteasome-associated.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 1 PITH domain.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; JC5938; JC5938.
DR RefSeq; NP_004777.1; NM_004786.2.
DR UniGene; Hs.114412; -.
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 ProteinModelPortal; O43396; -.
DR SMR; O43396; 2-108, 123-279.
DR IntAct; O43396; 4.
DR MINT; MINT-5005836; -.
DR STRING; 9606.ENSP00000217515; -.
DR PhosphoSite; O43396; -.
DR OGP; O43396; -.
DR REPRODUCTION-2DPAGE; IPI00305692; -.
DR PaxDb; O43396; -.
DR PRIDE; O43396; -.
DR DNASU; 9352; -.
DR Ensembl; ENST00000217515; ENSP00000217515; ENSG00000091164.
DR Ensembl; ENST00000590954; ENSP00000464918; ENSG00000091164.
DR GeneID; 9352; -.
DR KEGG; hsa:9352; -.
DR UCSC; uc002lgg.3; human.
DR CTD; 9352; -.
DR GeneCards; GC18M054264; -.
DR HGNC; HGNC:12436; TXNL1.
DR HPA; CAB016446; -.
DR HPA; HPA002828; -.
DR HPA; HPA002829; -.
DR MIM; 603049; gene.
DR neXtProt; NX_O43396; -.
DR PharmGKB; PA134967488; -.
DR eggNOG; COG0526; -.
DR HOGENOM; HOG000189802; -.
DR HOVERGEN; HBG055982; -.
DR InParanoid; O43396; -.
DR OMA; SFLESDC; -.
DR OrthoDB; EOG7H4DX9; -.
DR PhylomeDB; O43396; -.
DR ChiTaRS; TXNL1; human.
DR EvolutionaryTrace; O43396; -.
DR GeneWiki; TXNL1; -.
DR GenomeRNAi; 9352; -.
DR NextBio; 35021; -.
DR PRO; PR:O43396; -.
DR ArrayExpress; O43396; -.
DR Bgee; O43396; -.
DR CleanEx; HS_TXNL1; -.
DR Genevestigator; O43396; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.470; -; 1.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR010400; PITH_dom.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10438; PTHR10438; 1.
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.
DR PROSITE; PS51352; THIOREDOXIN_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Electron transport; Nucleus; Phosphoprotein;
KW Proteasome; Redox-active center; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 289 Thioredoxin-like protein 1.
FT /FTId=PRO_0000120016.
FT DOMAIN 2 109 Thioredoxin.
FT DOMAIN 115 285 PITH.
FT MOD_RES 113 113 Phosphoserine.
FT DISULFID 34 37 Redox-active.
FT STRAND 4 7
FT HELIX 10 12
FT HELIX 13 19
FT TURN 20 22
FT STRAND 25 30
FT HELIX 35 50
FT STRAND 54 60
FT TURN 61 63
FT HELIX 65 70
FT STRAND 75 83
FT STRAND 86 94
FT HELIX 96 107
FT HELIX 127 129
FT TURN 132 134
FT STRAND 136 139
FT STRAND 142 144
FT STRAND 150 154
FT STRAND 166 182
FT STRAND 186 188
FT STRAND 193 199
FT HELIX 208 211
FT TURN 222 224
FT TURN 235 237
FT STRAND 241 248
FT STRAND 263 271
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
//
ID TXNL1_HUMAN Reviewed; 289 AA.
AC O43396;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 134.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT thioredoxin-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
RT novel 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;
RA Miranda-Vizuete A., Spyrou G.;
RT "Genomic structure and chromosomal localization of human thioredoxin-
RT like 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 238-259, AND 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.,
RA Hendil K.B., 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.,
RA Buerckstuemmer T., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
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 [13]
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
CC mV.
CC -!- SUBUNIT: Component of the 19S regulatory cap of the 26S
CC proteasome. Interacts with PSMD14/RPN11. Interacts with, and
CC reduces EEF1A1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=At least 85% of the
CC cellular TXNL1 is proteasome-associated.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 1 PITH domain.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; JC5938; JC5938.
DR RefSeq; NP_004777.1; NM_004786.2.
DR UniGene; Hs.114412; -.
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 ProteinModelPortal; O43396; -.
DR SMR; O43396; 2-108, 123-279.
DR IntAct; O43396; 4.
DR MINT; MINT-5005836; -.
DR STRING; 9606.ENSP00000217515; -.
DR PhosphoSite; O43396; -.
DR OGP; O43396; -.
DR REPRODUCTION-2DPAGE; IPI00305692; -.
DR PaxDb; O43396; -.
DR PRIDE; O43396; -.
DR DNASU; 9352; -.
DR Ensembl; ENST00000217515; ENSP00000217515; ENSG00000091164.
DR Ensembl; ENST00000590954; ENSP00000464918; ENSG00000091164.
DR GeneID; 9352; -.
DR KEGG; hsa:9352; -.
DR UCSC; uc002lgg.3; human.
DR CTD; 9352; -.
DR GeneCards; GC18M054264; -.
DR HGNC; HGNC:12436; TXNL1.
DR HPA; CAB016446; -.
DR HPA; HPA002828; -.
DR HPA; HPA002829; -.
DR MIM; 603049; gene.
DR neXtProt; NX_O43396; -.
DR PharmGKB; PA134967488; -.
DR eggNOG; COG0526; -.
DR HOGENOM; HOG000189802; -.
DR HOVERGEN; HBG055982; -.
DR InParanoid; O43396; -.
DR OMA; SFLESDC; -.
DR OrthoDB; EOG7H4DX9; -.
DR PhylomeDB; O43396; -.
DR ChiTaRS; TXNL1; human.
DR EvolutionaryTrace; O43396; -.
DR GeneWiki; TXNL1; -.
DR GenomeRNAi; 9352; -.
DR NextBio; 35021; -.
DR PRO; PR:O43396; -.
DR ArrayExpress; O43396; -.
DR Bgee; O43396; -.
DR CleanEx; HS_TXNL1; -.
DR Genevestigator; O43396; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.470; -; 1.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR010400; PITH_dom.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10438; PTHR10438; 1.
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.
DR PROSITE; PS51352; THIOREDOXIN_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Electron transport; Nucleus; Phosphoprotein;
KW Proteasome; Redox-active center; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 289 Thioredoxin-like protein 1.
FT /FTId=PRO_0000120016.
FT DOMAIN 2 109 Thioredoxin.
FT DOMAIN 115 285 PITH.
FT MOD_RES 113 113 Phosphoserine.
FT DISULFID 34 37 Redox-active.
FT STRAND 4 7
FT HELIX 10 12
FT HELIX 13 19
FT TURN 20 22
FT STRAND 25 30
FT HELIX 35 50
FT STRAND 54 60
FT TURN 61 63
FT HELIX 65 70
FT STRAND 75 83
FT STRAND 86 94
FT HELIX 96 107
FT HELIX 127 129
FT TURN 132 134
FT STRAND 136 139
FT STRAND 142 144
FT STRAND 150 154
FT STRAND 166 182
FT STRAND 186 188
FT STRAND 193 199
FT HELIX 208 211
FT TURN 222 224
FT TURN 235 237
FT STRAND 241 248
FT STRAND 263 271
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
//
MIM
603049
*RECORD*
*FIELD* NO
603049
*FIELD* TI
*603049 THIOREDOXIN-LIKE 1; TXNL1
;;THIOREDOXIN-LIKE; TXNL;;
TXL
*FIELD* TX
DESCRIPTION
read more
Thioredoxins are a group of small redox active proteins that have a
conserved active site sequence. Proteins with thioredoxin-like domains,
e.g., TXNL1, have many of the conserved residues in thioredoxins present
at the same position but different active site residues (summary by
Miranda-Vizuete et al., 1998).
CLONING
By searching EST databases with the region centered on the active site
of human thioredoxin (TXN; 187700), followed by PCR on human testis
cDNA, Miranda-Vizuete et al. (1998) isolated a cDNA encoding TXL. The
predicted 289-amino acid, 32.3-kD protein has 2 distinct domains: an
N-terminal domain, which is 43% identical to human TXN, and a C-terminal
domain, which showed no homology to other proteins in the sequence
databases. The active site sequence, located within the N-terminal
domain, is that of a thioredoxin-like protein; compared to the active
site sequence of TXN, it has a single amino acid substitution. Unlike
other thioredoxin-like proteins, TXL did not act as a substrate for
thioredoxin reductase in an insulin assay. Since TXL has an additional
184 amino acids at its C terminus relative to other mammalian
thioredoxins, the authors tested a TXL protein that lacked the
C-terminal domain and found that this truncated form was also unable to
act as a substrate in an insulin assay. Northern blot analysis detected
a 1.3-kb TXL transcript in all human tissues tested.
MAPPING
Gross (2012) mapped the TXNL1 gene to chromosome 18q21.31 based on an
alignment of the TXNL1 sequence (GenBank GENBANK AB209263) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 6/18/2012.
2. Miranda-Vizuete, A.; Gustafsson, J.-A.; Spyrou, G.: Molecular
cloning and expression of a cDNA encoding a human thioredoxin-like
protein. Biochem. Biophys. Res. Commun. 243: 284-288, 1998.
*FIELD* CN
Matthew B. Gross - updated: 06/18/2012
*FIELD* CD
Sheryl A. Jankowski: 9/21/1998
*FIELD* ED
mgross: 06/18/2012
carol: 6/18/2012
carol: 6/14/2012
psherman: 12/4/1998
psherman: 9/22/1998
*RECORD*
*FIELD* NO
603049
*FIELD* TI
*603049 THIOREDOXIN-LIKE 1; TXNL1
;;THIOREDOXIN-LIKE; TXNL;;
TXL
*FIELD* TX
DESCRIPTION
read more
Thioredoxins are a group of small redox active proteins that have a
conserved active site sequence. Proteins with thioredoxin-like domains,
e.g., TXNL1, have many of the conserved residues in thioredoxins present
at the same position but different active site residues (summary by
Miranda-Vizuete et al., 1998).
CLONING
By searching EST databases with the region centered on the active site
of human thioredoxin (TXN; 187700), followed by PCR on human testis
cDNA, Miranda-Vizuete et al. (1998) isolated a cDNA encoding TXL. The
predicted 289-amino acid, 32.3-kD protein has 2 distinct domains: an
N-terminal domain, which is 43% identical to human TXN, and a C-terminal
domain, which showed no homology to other proteins in the sequence
databases. The active site sequence, located within the N-terminal
domain, is that of a thioredoxin-like protein; compared to the active
site sequence of TXN, it has a single amino acid substitution. Unlike
other thioredoxin-like proteins, TXL did not act as a substrate for
thioredoxin reductase in an insulin assay. Since TXL has an additional
184 amino acids at its C terminus relative to other mammalian
thioredoxins, the authors tested a TXL protein that lacked the
C-terminal domain and found that this truncated form was also unable to
act as a substrate in an insulin assay. Northern blot analysis detected
a 1.3-kb TXL transcript in all human tissues tested.
MAPPING
Gross (2012) mapped the TXNL1 gene to chromosome 18q21.31 based on an
alignment of the TXNL1 sequence (GenBank GENBANK AB209263) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 6/18/2012.
2. Miranda-Vizuete, A.; Gustafsson, J.-A.; Spyrou, G.: Molecular
cloning and expression of a cDNA encoding a human thioredoxin-like
protein. Biochem. Biophys. Res. Commun. 243: 284-288, 1998.
*FIELD* CN
Matthew B. Gross - updated: 06/18/2012
*FIELD* CD
Sheryl A. Jankowski: 9/21/1998
*FIELD* ED
mgross: 06/18/2012
carol: 6/18/2012
carol: 6/14/2012
psherman: 12/4/1998
psherman: 9/22/1998