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Protein

Thioredoxin-like protein 1

Gene

Txnl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Active thioredoxin with a redox potential of about -250 mV.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-like protein 1
Alternative name(s):
32 kDa thioredoxin-related protein
Gene namesi
Name:Txnl1
Synonyms:Trp32, Txnl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1860078. Txnl1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: At least 85% of the cellular TXNL1 is proteasome-associated.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 289288Thioredoxin-like protein 1PRO_0000120017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 37Redox-activeBy similarity
Modified residuei113 – 1131PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ8CDN6.
MaxQBiQ8CDN6.
PaxDbiQ8CDN6.
PRIDEiQ8CDN6.

2D gel databases

REPRODUCTION-2DPAGEQ8CDN6.

PTM databases

iPTMnetiQ8CDN6.
PhosphoSiteiQ8CDN6.
SwissPalmiQ8CDN6.

Expressioni

Gene expression databases

BgeeiQ8CDN6.
CleanExiMM_TXNL1.
GenevisibleiQ8CDN6. MM.

Interactioni

Subunit structurei

Component of the 19S regulatory cap of the 26S proteasome. Interacts with PSMD14/RPN11. Interacts with, and reduces EEF1A1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi207304. 2 interactions.
IntActiQ8CDN6. 2 interactions.
MINTiMINT-4138869.
STRINGi10090.ENSMUSP00000025476.

Structurei

3D structure databases

ProteinModelPortaliQ8CDN6.
SMRiQ8CDN6. Positions 2-108, 123-279.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 109108ThioredoxinAdd
BLAST
Domaini115 – 285171PITHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PITH domain.PROSITE-ProRule annotation
Contains 1 thioredoxin domain.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0908. Eukaryota.
ENOG410YQ2G. LUCA.
GeneTreeiENSGT00530000063008.
HOVERGENiHBG055982.
InParanoidiQ8CDN6.
OMAiMSVRVIN.
OrthoDBiEOG7H4DX9.
PhylomeDBiQ8CDN6.
TreeFamiTF314399.

Family and domain databases

Gene3Di2.60.120.470. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR010400. PITH_dom.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF06201. PITH. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS51532. PITH. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8CDN6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK
60 70 80 90 100
YPQAVFLEVD VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE
110 120 130 140 150
EKIKQHLEND PGSNEDADIP KGYMDLMPFI NKAGCECLNE SDEHGFDNCL
160 170 180 190 200
RKDMSFLESD CDEQLLITVA FNQPVKLYSM KFQGPDNGQG PKYVKIFINL
210 220 230 240 250
PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN VNSVTLFVQS
260 270 280
NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH
Length:289
Mass (Da):32,237
Last modified:January 23, 2007 - v3
Checksum:i4BE29C6C1D1DFA0A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511N → K in AAC40183 (PubMed:9668102).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052660 mRNA. Translation: AAC40183.1.
AK029807 mRNA. Translation: BAC26626.1.
AK150326 mRNA. Translation: BAE29469.1.
AK167954 mRNA. Translation: BAE39954.1.
AK168712 mRNA. Translation: BAE40554.1.
BC061123 mRNA. Translation: AAH61123.1.
CCDSiCCDS29297.1.
RefSeqiNP_058072.2. NM_016792.4.
UniGeneiMm.19169.

Genome annotation databases

EnsembliENSMUST00000025476; ENSMUSP00000025476; ENSMUSG00000024583.
GeneIDi53382.
KEGGimmu:53382.
UCSCiuc008fdx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052660 mRNA. Translation: AAC40183.1.
AK029807 mRNA. Translation: BAC26626.1.
AK150326 mRNA. Translation: BAE29469.1.
AK167954 mRNA. Translation: BAE39954.1.
AK168712 mRNA. Translation: BAE40554.1.
BC061123 mRNA. Translation: AAH61123.1.
CCDSiCCDS29297.1.
RefSeqiNP_058072.2. NM_016792.4.
UniGeneiMm.19169.

3D structure databases

ProteinModelPortaliQ8CDN6.
SMRiQ8CDN6. Positions 2-108, 123-279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207304. 2 interactions.
IntActiQ8CDN6. 2 interactions.
MINTiMINT-4138869.
STRINGi10090.ENSMUSP00000025476.

PTM databases

iPTMnetiQ8CDN6.
PhosphoSiteiQ8CDN6.
SwissPalmiQ8CDN6.

2D gel databases

REPRODUCTION-2DPAGEQ8CDN6.

Proteomic databases

EPDiQ8CDN6.
MaxQBiQ8CDN6.
PaxDbiQ8CDN6.
PRIDEiQ8CDN6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025476; ENSMUSP00000025476; ENSMUSG00000024583.
GeneIDi53382.
KEGGimmu:53382.
UCSCiuc008fdx.1. mouse.

Organism-specific databases

CTDi9352.
MGIiMGI:1860078. Txnl1.

Phylogenomic databases

eggNOGiKOG0908. Eukaryota.
ENOG410YQ2G. LUCA.
GeneTreeiENSGT00530000063008.
HOVERGENiHBG055982.
InParanoidiQ8CDN6.
OMAiMSVRVIN.
OrthoDBiEOG7H4DX9.
PhylomeDBiQ8CDN6.
TreeFamiTF314399.

Miscellaneous databases

ChiTaRSiTxnl1. mouse.
PROiQ8CDN6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CDN6.
CleanExiMM_TXNL1.
GenevisibleiQ8CDN6. MM.

Family and domain databases

Gene3Di2.60.120.470. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR010400. PITH_dom.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF06201. PITH. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS51532. PITH. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification, molecular cloning, and characterization of TRP32, a novel thioredoxin-related mammalian protein of 32 kDa."
    Lee K.-K., Murakawa M., Takahashi S., Tsubuki S., Kawashima S., Sakamaki K., Yonehara S.
    J. Biol. Chem. 273:19160-19166(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Amnion, Bone marrow and Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiTXNL1_MOUSE
AccessioniPrimary (citable) accession number: Q8CDN6
Secondary accession number(s): O70379, Q3TI92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.