P12864 (GLRX1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutaredoxin-1

Alternative name(s):
Thioltransferase-1
Short name=TTase-1

Gene names

Name:	GLRX
Synonyms:	GRX

Organism

Oryctolagus cuniculus (Rabbit) [Complete proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	106 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the glutaredoxin family. Contains 1 glutaredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Domain	Redox-active center
PTM	Acetylation Disulfide bond
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 106	106	Glutaredoxin-1		PRO_0000141603
Regions
	Domain	2 – 105	104	Glutaredoxin
Amino acid modifications
	Modified residue	1	1	N-acetylalanine
	Disulfide bond	22 ↔ 25		Redox-active
	Disulfide bond	78 ↔ 82

Sequences

	Sequence		Length	Mass (Da)
	P12864 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: F6A1D7CC096A2105	FASTA	106	11,822
	10 20 30 40 50 60 AQEFVNSKIQ PGKVVVFIKP TCPYCRKTQE ILSQLPFKQG LLEFVDITAT SDMSEIQDYL 70 80 90 100 QQLTGARTVP RVFLGKDCIG GCSDLIAMQE KGELLARLKE MGALRQ

References

[1]	"Glutaredoxin from rabbit bone marrow. Purification, characterization, and amino acid sequence determined by tandem mass spectrometry." Hopper S., Johnson R.S., Vath J.E., Biemann K. J. Biol. Chem. 264:20438-20447(1989) [PubMed: 2684977] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Bone marrow.
+	Additional computationally mapped references.

Cross-references

Sequence databases
PIR	GDRB. A32682.
3D structure databases
ProteinModelPortal	P12864.
SMR	P12864. Positions 1-105.
ModBase	Search...
Protein-protein interaction databases
STRING	P12864.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	maNOG20814.
GeneTree	ENSGT00390000003677.
HOVERGEN	HBG000283.
OrthoDB	EOG4N8R6D.
Family and domain databases
InterPro	IPR011767. GLR_AS. IPR002109. Glutaredoxin. IPR011899. Glutaredoxin_euk/vir. IPR014025. Glutaredoxin_subgr. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF00462. Glutaredoxin. 1 hit. [Graphical view]
PRINTS	PR00160. GLUTAREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMs	TIGR02180. GRX_euk. 1 hit.
PROSITE	PS00195. GLUTAREDOXIN_1. 1 hit. PS51354. GLUTAREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLRX1_RABIT

Accession

Primary (citable) accession number: P12864

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	November 16, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program