Reviewed, UniProtKB/Swiss-Prot Q9MYY8 (TRXR1_PIG)

Names and origin

Protein names

Recommended name:
    Thioredoxin reductase 1, cytoplasmic
      Short name=TR
    EC=1.8.1.9
Alternative name(s):
    Thioredoxin reductase TR1

Gene names

Name:

TXNRD1

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 component	Cytoplasm
Coding sequence diversity	Selenocysteine
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP Selenium
Molecular function	Oxidoreductase
PTM	Acetylation Disulfide bond Phosphoprotein
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro electron carrier activity 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 499	499	Thioredoxin reductase 1, cytoplasmic		PRO_0000067983
Regions
	Nucleotide binding	42 – 59	18	FAD By similarity
Sites
	Active site	472	1	Proton acceptor By similarity
Amino acid modifications
	Non-standard residue	498	1	Selenocysteine
	Modified residue	11	1	Phosphotyrosine By similarity
	Modified residue	13	1	Phosphotyrosine By similarity
	Modified residue	131	1	Phosphotyrosine By similarity
	Modified residue	255	1	N6-acetyllysine By similarity
	Modified residue	422	1	Phosphotyrosine By similarity
	Disulfide bond	59 ↔ 64		Redox-active By similarity
	Cross-link	497 ↔ 498		Cysteinyl-selenocysteine (Cys-Sec) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9MYY8-1 [UniParc]. Last modified February 26, 2008. Version 3. Checksum: CFE9C9F51998FBB4	FASTA	499	54,904
	10 20 30 40 50 60 MNGAEELPEM YDYDLIIIGG GSGGLAAAKE AARFNKRVMV LDFVTPTPLG TRWGLGGTCV 70 80 90 100 110 120 NVSCIPKKLM HQAALLGQAL RDSRNYGWNV EETIKHDWER MTEAVQNHIG SLNWGYRVAL 130 140 150 160 170 180 REKKVTYENA YGQFVGPHRI KATNNKGKEK IYSAEKFLIA TGERPRYLGI PGDKEYCISS 190 200 210 220 230 240 DDLFSLPYCP GKTLVVGASY VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM 250 260 270 280 290 300 EEHGIKFIRQ FVPIKVEQIE AGTPGRLRVV AQSTNSEEII EGEYNTVMLA 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

References

[1]	"Cloning and sequencing of thioredoxin reductase gene from porcine reticulocyte." Lee K.S., Xu L., Xu J.Y., Cheung P.Y. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF277894 mRNA. Translation: AAF78791.1.
UniGene	Ssc.15974
3D structure databases
HSSP	HSSP built from PDB template 1ONF based on UniProtKB Q94655.
SMR	Q9MYY8. Positions 11-493.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q9MYY8.
Enzyme and pathway databases
BRENDA	1.8.1.9. 249.
Family and domain databases
InterPro	IPR013027. 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. Thioredoxin/glutathione_Rdtase. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHER	PTHR22912:SF23. Reduct_Se. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00945. HGRDTASE.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01438. TGR. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRXR1_PIG

Accession

Primary (citable) accession number: Q9MYY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	February 26, 2008
Last modified:	November 3, 2009
This is version 60 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)