Q5NVA2 (TRXR1_PONAB) Reviewed, UniProtKB/Swiss-Prot

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

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
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
Molecular function	Oxidoreductase
PTM	Acetylation Disulfide bond Phosphoprotein
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro 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_0000067984
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	89	1	N6-acetyllysine 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
Experimental info
	Sequence conflict	56	1	G → E in CAH92925. Ref.1
	Sequence conflict	108	1	H → R in CAI30275. Ref.1
	Sequence conflict	254	1	I → V in CAI30275. Ref.1
	Sequence conflict	257	1	E → G in CAH92925. Ref.1
	Sequence conflict	411	1	W → R in CAH92925. Ref.1
	Sequence conflict	485	1	T → A in CAI30275. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q5NVA2 [UniParc]. Last modified February 26, 2008. Version 3. Checksum: D0535BE1F2405DA7	FASTA	499	54,751
	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

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
EMBL GenBank DDBJ	CR860816 mRNA. Translation: CAH92925.2. CR926483 mRNA. Translation: CAI30275.1.
RefSeq	NP_001127133.1. NM_001133661.1.
UniGene	Pab.4920.
3D structure databases
ProteinModelPortal	Q5NVA2.
ModBase	Search...
Proteomic databases
PRIDE	Q5NVA2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100174180.
KEGG	pon:100174180.
Organism-specific databases
CTD	7296.
Phylogenomic databases
HOVERGEN	HBG004959.
Family and domain databases
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. IPR006338. Thioredoxin/glutathione_Rdtase. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KO	K00384.
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.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01438. TGR. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRXR1_PONAB

Accession

Primary (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:	November 16, 2011
This is version 55 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program