Reviewed, UniProtKB/Swiss-Prot Q9UTI2 (GLRX2_SCHPO)

Names and origin

Protein names

Recommended name:
    Glutaredoxin-2

Gene names

Name:	grx2
ORF Names:	SPAC15E1.09

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	110 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function

The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase. Thioltransferase catalyzes cellular thiol-disulfide transhydrogenation reactions. It transfers reducing equivalents to cytosolic protein and nonprotein disulfides By similarity.

Sequence similarities

Belongs to the glutaredoxin family. Contains 1 glutaredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Domain	Redox-active center
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro cellular response to oxidative stress Inferred from genetic interaction. Source: GeneDB_SPombe electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: GeneDB_SPombe
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 – 110	110	Glutaredoxin-2		PRO_0000141611
Regions
	Domain	6 – 106	101	Glutaredoxin
Amino acid modifications
	Disulfide bond	26 ↔ 29		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9UTI2-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 93B4FEA9DBEA2287	FASTA	110	12,235
	10 20 30 40 50 60 MTSIAKAFVE KAISNNPVTV FSKSFCPFCK AAKNTLTKYS APYKAYELDK IENGSDIQAY 70 80 90 100 110 LHEKTKQSTV PSIFFRNQFI GGNSDLNKLR SSGTLTKMIA ELKENKSSIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of glutaredoxin 2 (thioltransferase 2) from Schizosaccharomyces pombe." Kim H.-G., Cho Y.-W., Lee Y.-Y., Lim C.-J. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF380128 Genomic DNA. Translation: AAK55420.1. CU329670 Genomic DNA. Translation: CAB52428.1.
PIR	T37724.
RefSeq	NP_594310.1.
3D structure databases
HSSP	HSSP built from PDB template 1KTE based on UniProtKB P12309.
ModBase	Search...
Genome annotation databases
GeneID	2542807.
KEGG	spo:SPAC15E1.09.
NMPDR	fig|4896.1.peg.4280.
Organism-specific databases
GeneDB_Spombe	SPAC15E1.09.
Phylogenomic databases
OMA	Q9UTI2. RNDGDEI.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001913-MON.
Gene expression databases
ArrayExpress	Q9UTI2.
Family and domain databases
InterPro	IPR011767. GLR_AS. IPR002109. Glutaredoxin. IPR014025. Glutaredoxin_sub. IPR011899. GRX_euk. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF00462. Glutaredoxin. 1 hit. [Graphical view]
PRINTS	PR00160. GLUTAREDOXIN.
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

GLRX2_SCHPO

Accession

Primary (citable) accession number: Q9UTI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 5, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)