P30635 (GSHR_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable glutathione reductase 2
Short name=GR
Short name=GRase
EC=1.8.1.7

Gene names

Name:	trxr-2
ORF Names:	ZK637.10

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Maintains high levels of reduced glutathione in the cytosol.
Catalytic activity	2 glutathione + NADP+ = glutathione disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
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 glutathione-disulfide reductase activity Inferred from electronic annotation. Source: EC thioredoxin-disulfide reductase activity Inferred from direct assay PubMed 17661444. Source: WormBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 503	503	Probable glutathione reductase 2		PRO_0000067958
Regions
	Nucleotide binding	58 – 67	10	FAD By similarity
Sites
	Active site	476	1	Proton acceptor By similarity
Amino acid modifications
	Disulfide bond	67 ↔ 72		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30635 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: CE2385C9ACBD9AD2	FASTA	503	55,046
	10 20 30 40 50 60 MLLSTFKRHL PIRRLFSSNK FDLIVIGAGS GGLSCSKRAA DLGANVALID AVEPTPHGHS 70 80 90 100 110 120 WGIGGTCANV GCIPKKLMHQ AAIVGKELKH ADKYGWNGID QEKIKHDWNV LSKNVNDRVK 130 140 150 160 170 180 ANNWIYRVQL NQKKINYFNA YAEFVDKDKI VITGTDKNKT KNFLSAPNVV ISTGLRPKYP 190 200 210 220 230 240 NIPGAELGIT SDDLFTLASV PGKTLIVGGG YVALECAGFL SAFNQNVEVL VRSIPLKGFD 250 260 270 280 290 300 RDCVHFVMEH LKTTGVKVKE HVEVERVEAV GSKKKVTFTG NGGVEEYDTV IWAAGRVPNL 310 320 330 340 350 360 KSLNLDNAGV RTDKRSGKIL ADEFDRASCN GVYAVGDIVQ DRQELTPLAI QSGKLLADRL 370 380 390 400 410 420 FSNSKQIVRF DGVATTVFTP LELSTVGLTE EEAIQKHGED SIEVFHSHFT PFEYVVPQNK 430 440 450 460 470 480 DSGFCYVKAV CTRDESQKIL GLHFVGPNAA EVIQGYAVAF RVGISMSDLQ NTIAIHPCSS 490 500 EEFVKLHITK RSGQDPRTQG CCG

References

[1]	"The C. elegans genome sequencing project: a beginning." Sulston J., Du Z., Thomas K., Wilson R., Hillier L., Staden R., Halloran N., Green P., Thierry-Mieg J., Qiu L., Dear S., Coulson A., Craxton M., Durbin R., Berks M., Metzstein M., Hawkins T., Ainscough R., Waterston R. Nature 356:37-41(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z11115 Genomic DNA. Translation: CAA77459.1.
PIR	D88542. S15798.
RefSeq	NP_498971.1. NM_066570.4.
3D structure databases
ProteinModelPortal	P30635.
SMR	P30635. Positions 18-496.
ModBase	Search...
Protein-protein interaction databases
STRING	6239.ZK637.10.
Proteomic databases
PaxDb	P30635.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	ZK637.10.1; ZK637.10.1; ZK637.10. ZK637.10.2; ZK637.10.2; ZK637.10.
GeneID	176259.
KEGG	cel:CELE_ZK637.10.
UCSC	ZK637.10. c. elegans.
Organism-specific databases
CTD	40475.
WormBase	ZK637.10; CE15373; WBGene00014028; trxr-2.
Phylogenomic databases
eggNOG	COG1249.
GeneTree	ENSGT00390000007578.
HOGENOM	HOG000276712.
InParanoid	P30635.
KO	K00383.
OMA	YAVAFRV.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
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]
PANTHER	PTHR22912:SF23. PTHR22912:SF23. 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...
Other
NextBio	891814.

Entry information

Entry name

GSHR_CAEEL

Accession

Primary (citable) accession number: P30635

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project