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Protein

Thioredoxin domain-containing protein 2

Gene

Txndc2

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

Functioni

Probably plays a regulatory role in sperm development. May participate in regulation of fibrous sheath (FS) assembly by supporting the formation of disulfide bonds during sperm tail morphogenesis. May also be required to rectify incorrect disulfide pairing and generate suitable pairs between the FS constituents. Can reduce disulfide bonds in vitro in the presence of NADP and thioredoxin reductase.

GO - Molecular functioni

  1. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: GO_Central
  2. protein disulfide isomerase activity Source: MGI
  3. protein disulfide oxidoreductase activity Source: GO_Central
  4. thioredoxin-disulfide reductase activity Source: MGI

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. cell redox homeostasis Source: GO_Central
  3. cellular response to oxidative stress Source: GO_Central
  4. glycerol ether metabolic process Source: InterPro
  5. multicellular organismal development Source: UniProtKB-KW
  6. oxidation-reduction process Source: MGI
  7. protein folding Source: GOC
  8. spermatogenesis Source: UniProtKB-KW
  9. sulfate assimilation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Spermatogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin domain-containing protein 2
Alternative name(s):
Spermatid-specific thioredoxin-1
Short name:
Sptrx-1
Thioredoxin-4
Gene namesi
Name:Txndc2
Synonyms:Sptrx, Sptrx1, Trx4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2389312. Txndc2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. mitochondrion Source: GO_Central
  3. motile cilium Source: MGI
  4. nucleolus Source: MGI
  5. nucleoplasm Source: MGI
  6. nucleus Source: MGI
  7. outer dense fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515Thioredoxin domain-containing protein 2PRO_0000120154Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi442 ↔ 445Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ6P902.
PRIDEiQ6P902.

PTM databases

PhosphoSiteiQ6P902.

Expressioni

Tissue specificityi

Testis-specific. Strongly expressed in the testicular seminiferous tubules, mostly in the round spermatids.2 Publications

Developmental stagei

Expressed during spermiogenesis, restricted to the postmeiotic phase of spermatogenesis. First detected in elongating spermatids tails during steps 9 and 10 and is prominent in this region during steps 11-16. Also weakly present in the cytoplasmic lobe of these spermatids. During the last steps of spermiogenesis (steps 17-19), it strongly diminishes in the tail but appears to increase or become concentrated in the shrinking cytoplasmic lobe. By the last step of spermiogenesis (late step 19), cytoplasmic localization is barely detectable in the resulting residual body but still detectable in the cytoplasmic droplet (at protein level). Detected in testis of pre-pubertal animals at very low level.2 Publications

Gene expression databases

BgeeiQ6P902.
CleanExiMM_TXNDC2.
ExpressionAtlasiQ6P902. baseline.
GenevestigatoriQ6P902.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054909.

Structurei

3D structure databases

SMRiQ6P902. Positions 411-514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati92 – 106151Add
BLAST
Repeati107 – 121152Add
BLAST
Repeati122 – 136153Add
BLAST
Repeati137 – 151154Add
BLAST
Repeati152 – 166155Add
BLAST
Repeati167 – 181156Add
BLAST
Repeati182 – 196157Add
BLAST
Repeati197 – 211158Add
BLAST
Repeati212 – 226159Add
BLAST
Repeati227 – 2411510Add
BLAST
Repeati242 – 2561511Add
BLAST
Repeati257 – 2711512Add
BLAST
Repeati272 – 2861513Add
BLAST
Repeati287 – 3011514Add
BLAST
Repeati302 – 3161515Add
BLAST
Repeati317 – 3311516Add
BLAST
Repeati332 – 3461517Add
BLAST
Repeati347 – 3621618Add
BLAST
Repeati363 – 3751319Add
BLAST
Repeati376 – 3901520Add
BLAST
Repeati391 – 4051521Add
BLAST
Domaini398 – 515118ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni92 – 40531421 X 15 AA approximate tandem repeat of Q-P-K-X-G-D-I-P-K-S-[PS]-E-[KE]-X-IAdd
BLAST

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000154719.
HOVERGENiHBG087115.
InParanoidiQ6P902.
PhylomeDBiQ6P902.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6P902-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLNNGGKAN ERGSNENPLQ ALSKNEAFLV PEFLDTAQSK EKAIASKVSN
60 70 80 90 100
TLHMSTEESE FPQQVSSTPM FSENTVHPRH EVSPKPSSKN TQLKQENISK
110 120 130 140 150
SSGYSKQTNY SNTPKSLAKT THPKQGSTLK PATNSTHYRE DDIPKSSEDI
160 170 180 190 200
IQPKKGDRPK SSEDIIQSKK EDRPKSSEDI IQSKKEDRPK SSEDIIQSKK
210 220 230 240 250
EDRPKSSEDI IQSKKEDRPK SSEDIIQPKK EDRPKSSEDS VPSKKGDRPK
260 270 280 290 300
SSEDSVQPKK EDRPKSSEDS VQSKEGEVHK PLKDSIQSKE TKVPKSPQDS
310 320 330 340 350
IQSKEDKTHR PLKDSVQSKE SEEPKSSHES IQSKEDKIHK PLKDSIPSKE
360 370 380 390 400
GDIPKSPEDT IQSQEEITAS EEDTIQSQEG NTIKSSEEDV QLSESKLLGL
410 420 430 440 450
GAEIETLEEG LVRVIKDKEE FEEVLKDAGE KLVAVDFSAA WCGPCRMMKP
460 470 480 490 500
LFHSLSLKHE DVIFLEVDTE DCEQLVQDCE IFHLPTFQFY KNEEKVGEFS
510
GALVGKLERS ISELK
Length:515
Mass (Da):57,767
Last modified:July 5, 2004 - v1
Checksum:i46F178558C27A71A
GO

Sequence cautioni

The sequence AAM94687.2 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF196282 mRNA. Translation: AAM94687.2. Different initiation.
BC060981 mRNA. Translation: AAH60981.1.
RefSeqiNP_001139474.1. NM_001146002.1.
NP_705739.2. NM_153519.2.
UniGeneiMm.255732.

Genome annotation databases

GeneIDi213272.
KEGGimmu:213272.
UCSCiuc008dge.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF196282 mRNA. Translation: AAM94687.2. Different initiation.
BC060981 mRNA. Translation: AAH60981.1.
RefSeqiNP_001139474.1. NM_001146002.1.
NP_705739.2. NM_153519.2.
UniGeneiMm.255732.

3D structure databases

SMRiQ6P902. Positions 411-514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054909.

PTM databases

PhosphoSiteiQ6P902.

Proteomic databases

PaxDbiQ6P902.
PRIDEiQ6P902.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi213272.
KEGGimmu:213272.
UCSCiuc008dge.2. mouse.

Organism-specific databases

CTDi84203.
MGIiMGI:2389312. Txndc2.

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000154719.
HOVERGENiHBG087115.
InParanoidiQ6P902.
PhylomeDBiQ6P902.

Miscellaneous databases

NextBioi373905.
PROiQ6P902.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P902.
CleanExiMM_TXNDC2.
ExpressionAtlasiQ6P902. baseline.
GenevestigatoriQ6P902.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression and characterization of mouse spermatid specific thioredoxin-1 gene and protein."
    Jimenez A., Oko R., Gustafsson J.-A., Spyrou G., Pelto-Huikko M., Miranda-Vizuete A.
    Mol. Hum. Reprod. 8:710-718(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, ENZYME ACTIVITY IN VITRO.
  2. "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: Testis.
  3. "Developmental expression of spermatid-specific thioredoxin-1 protein: transient association to the longitudinal columns of the fibrous sheath during sperm tail formation."
    Yu Y., Oko R., Miranda-Vizuete A.
    Biol. Reprod. 67:1546-1554(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  4. "Absolute mRNA levels and transcriptional regulation of the mouse testis-specific thioredoxins."
    Jimenez A., Prieto-Alamo M.J., Fuentes-Almagro C.A., Jurado J., Gustafsson J.-A., Pueyo C., Miranda-Vizuete A.
    Biochem. Biophys. Res. Commun. 330:65-74(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiTXND2_MOUSE
AccessioniPrimary (citable) accession number: Q6P902
Secondary accession number(s): Q8CJD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2004
Last modified: April 29, 2015
This is version 98 of the entry and version 1 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

External Data

Dasty 3

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 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.