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Reviewed, UniProtKB/Swiss-Prot Q5NVA2 (TRXR1_PONAB)

Last modified June 16, 2009. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Thioredoxin reductase 1, cytoplasmic
      Short name=TR
    EC=1.8.1.9
Alternative name(s):
    Thioredoxin reductase TR1
Gene names
Name: TXNRD1
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversitySelenocysteine
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
Selenium
   Molecular functionOxidoreductase
   PTMDisulfide bond
Phosphoprotein
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

NADP or NADPH binding

Inferred from electronic annotation. Source: InterPro

selenium binding

Inferred from electronic annotation. Source: UniProtKB-KW

thioredoxin-disulfide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Thioredoxin reductase 1, cytoplasmic
PRO_0000067984

Regions

Nucleotide binding42 – 5918FAD By similarity

Sites

Active site4721Proton acceptor By similarity

Amino acid modifications

Non-standard residue4981Selenocysteine
Modified residue111Phosphotyrosine By similarity
Modified residue131Phosphotyrosine By similarity
Modified residue1311Phosphotyrosine By similarity
Modified residue4221Phosphotyrosine By similarity
Disulfide bond59 ↔ 64Redox-active By similarity
Cross-link497 ↔ 498Cysteinyl-selenocysteine (Cys-Sec) By similarity

Experimental info

Sequence conflict561G → E in CAH92925. Ref.1
Sequence conflict1081H → R in CAI30275. Ref.1
Sequence conflict2541I → V in CAI30275. Ref.1
Sequence conflict2571E → G in CAH92925. Ref.1
Sequence conflict4111W → R in CAH92925. Ref.1
Sequence conflict4851T → A in CAI30275. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5NVA2-1 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: D0535BE1F2405DA7

FASTA49954,751
        10         20         30         40         50         60 
MNGPEDLPES YDYDLIIIGG GSGGLAAAKE AAQYGKKVMV LDFVTPTPLG TRWGLGGTCV 

        70         80         90        100        110        120 
NVGCIPKKLM HQAALLGQAL QDSRNYGWKV EETVKHDWDR MIEAVQNHIG SLNWGYRVAL 

       130        140        150        160        170        180 
REKKVVYENA YGQFIGPHRI KATNNKGKEK IYSAERFLIA TGERPRYLGI PGDKEYCISS 

       190        200        210        220        230        240 
DDLFSLPYCP GKTLIVGASY VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM 

       250        260        270        280        290        300 
EEHGIKFIRQ FVPIKVEQIE AGTPGRLRVV AQSTNSEEII EGEYNTVLLA IGRDACTRKI 

       310        320        330        340        350        360 
GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEDKV ELTPVAIQAG RLLAQRLYAG 

       370        380        390        400        410        420 
STVKCDYENV PTTVFTPLEY GACGLSEEKA VEKFGEENIE VYHSYFWPLE WTIPSRDNNK 

       430        440        450        460        470        480 
CYAKIICNTK DNERVVGFHV LGPNAGEVTQ GFAAALKCGL TKKQLDSTIG IHPVCAEVFT 

       490 
TLSVTKRSGA SILQAGCUG 

« Hide

References

[1]The German cDNA consortium
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex and Kidney.

Cross-references

Sequence databases

CR860816 mRNA. Translation: CAH92925.2.
CR926483 mRNA. Translation: CAI30275.1.
RefSeqNP_001127133.1.
UniGenePab.18374
Pab.4920

3D structure databases

SMRQ5NVA2. Positions 10-493.
ModBaseSearch...

Genome annotation databases

GeneID100174180.

Phylogenomic databases

HOVERGENQ5NVA2.

Enzyme and pathway databases

BRENDA1.8.1.9. 269192.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
IPR006338. Reduct_Se.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHERPTHR22912:SF23. Reduct_Se. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01438. TGR. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRXR1_PONAB
AccessionPrimary (citable) accession number: Q5NVA2
Secondary accession number(s): Q5R5P1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 26, 2008
Last modified: June 16, 2009
This is version 34 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents