P12309 (GLRX1_PIG) 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

Sus scrofa (Pig) [Complete proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	106 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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	3D-structure 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

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 106

105

Glutaredoxin-1

PRO_0000141602

Regions

Domain

3 – 106

104

Glutaredoxin

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.1

Disulfide bond

23 ↔ 26

Redox-active

Disulfide bond

79 ↔ 83

Ref.3

Experimental info

Sequence conflict

2 – 3

2

AQ → QA AA sequence Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

106

Helix Strand Turn

Details...

Helix

3 – 9

7

Beta strand

15 – 19

5

Helix

24 – 35

12

Beta strand

42 – 47

6

Helix

48 – 50

3

Helix

54 – 65

12

Beta strand

72 – 75

4

Beta strand

78 – 82

5

Helix

83 – 91

9

Helix

94 – 102

9

Sequences

	Sequence		Length	Mass (Da)
	P12309 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: FEA9B18376E1D5B0	FASTA	106	11,828
	10 20 30 40 50 60 MAQAFVNSKI QPGKVVVFIK PTCPFCRKTQ ELLSQLPFKE GLLEFVDITA TSDTNEIQDY 70 80 90 100 LQQLTGARTV PRVFIGKECI GGCTDLESMH KRGELLTRLQ QIGALK

References

[1]	"Cloning and sequencing the cDNA encoding pig liver thioltransferase." Yang Y., Gan Z.-R., Wells W.W. Gene 83:339-346(1989) [PubMed: 2583530] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Cloning and sequencing of the cDNA for pig liver thioltransferase (glutaredoxin)." Yang Y., Wells W.W. J. Cell Biol. 107:747A-747A(1988) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"The primary structure of pig liver thioltransferase." Gan Z.-R., Wells W.W. J. Biol. Chem. 262:6699-6703(1987) [PubMed: 3571278] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-106. Tissue: Liver.
[4]	"Crystal structure of thioltransferase at 2.2-A resolution." Katti S.K., Robbins A.R., Yang Y., Wells W.W. Protein Sci. 4:1998-2005(1995) [PubMed: 8535236] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M31453 mRNA. Translation: AAA31132.1.

PIR

GDPG. JQ0117.

RefSeq

NP_999398.1. NM_214233.1.

UniGene

Ssc.54096.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KTE	X-ray	2.20	A	2-104	[»]

ProteinModelPortal

P12309.

SMR

P12309. Positions 2-106.

ModBase

Search...

Protein-protein interaction databases

STRING

P12309.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSSSCT00000015476; ENSSSCP00000015066; ENSSSCG00000014167.

GeneID

397463.

KEGG

ssc:397463.

Organism-specific databases

CTD

2745.

Phylogenomic databases

HOVERGEN

HBG000283.

OMA

TNAIQDY.

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.

KO

K03676.

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_PIG

Accession

Primary (citable) accession number: P12309

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program