Q9Z1B2 (GSTM5_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase Mu 5
EC=2.5.1.18

Alternative name(s):
GST class-mu 5

Gene names

Name:

Gstm5

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	225 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	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Ref.1.
Tissue specificity	Expressed in testis and brain. Very low expression in liver, kidney, heart and lung. Ref.1
Post-translational modification	The N-terminus is blocked Probable.
Sequence similarities	Belongs to the GST superfamily. Mu family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.
Biophysicochemical properties	Kinetic parameters: KM=0.14 mM for glutathione Ref.1

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutathione transferase activity Inferred from direct assay Ref.1. Source: MGI protein homodimerization activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 225	224	Glutathione S-transferase Mu 5		PRO_0000271421
Regions
	Domain	5 – 92	88	GST N-terminal
	Domain	94 – 212	119	GST C-terminal
	Region	11 – 12	2	Glutathione binding By similarity
	Region	50 – 54	5	Glutathione binding By similarity
	Region	63 – 64	2	Glutathione binding By similarity
	Region	76 – 77	2	Glutathione binding By similarity
Sites
	Binding site	120	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Z1B2 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 45A2DC2DDCE5ACA4	FASTA	225	26,629
	10 20 30 40 50 60 MSCSKSMVLG YWDIRGLAHA IRMLLEFTDT SYEEKQYTCG EAPDYDRSQW LDVKFKLDLD 70 80 90 100 110 120 FPNLPYLMDG KNKITQSNAI LRYIARKHNM CGDTEEEKIR VDIMENQIMD FRMQLVRLCY 130 140 150 160 170 180 NSNHESLKPQ YLEQLPAQLK QFSLFLGKFT WFAGEKLTFV DFLTYDVLDQ NRMFEPKCLD 190 200 210 220 EFPNLKAFMC RFEALEKIAA FLQSDRCFKM PINNKMAKWG NKSIC

References

[1]	"Rationale for reclassification of a distinctive subdivision of mammalian class Mu glutathione S-transferases that are primarily expressed in testis." Rowe J.D., Patskovsky Y.V., Patskovska L.N., Novikova E., Listowsky I. J. Biol. Chem. 273:9593-9601(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 6-27; 36-50; 57-71; 74-87; 89-120; 157-177; 179-186; 198-215 AND 219-224, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, KINETIC PARAMETERS. Strain: Sprague-Dawley. Tissue: Testis.
[2]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 157-172, INITIATOR METHIONINE, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U86635 mRNA. Translation: AAD00603.1.
IPI	IPI00208636.
RefSeq	NP_742035.1. NM_172038.1. XP_003749426.1. XM_003749378.1.
UniGene	Rn.9158.
3D structure databases
ProteinModelPortal	Q9Z1B2.
SMR	Q9Z1B2. Positions 2-225.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000025589.
2D gel databases
World-2DPAGE	0004:Q9Z1B2.
Proteomic databases
PaxDb	Q9Z1B2.
PRIDE	Q9Z1B2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000072342; ENSRNOP00000065389; ENSRNOG00000049743. ENSRNOT00000073649; ENSRNOP00000064813; ENSRNOG00000047034.
GeneID	100912430. 64352.
KEGG	rno:100912430. rno:64352.
UCSC	RGD:61964. rat.
Organism-specific databases
CTD	2949.
RGD	61964. Gstm5.
Phylogenomic databases
eggNOG	NOG300089.
GeneTree	ENSGT00550000074559.
HOGENOM	HOG000115735.
HOVERGEN	HBG106842.
InParanoid	Q9Z1B2.
KO	K00799.
OMA	MSCESSM.
OrthoDB	EOG47D9H2.
Gene expression databases
Genevestigator	Q9Z1B2.
Family and domain databases
Gene3D	1.20.1050.10. 1 hit. 3.40.30.10. 1 hit.
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR003081. GST_mu. IPR012336. Thioredoxin-like_fold. [Graphical view]
Pfam	PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view]
PRINTS	PR01267. GSTRNSFRASEM.
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	613032.

Entry information

Entry name

GSTM5_RAT

Accession

Primary (citable) accession number: Q9Z1B2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program