NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=White leghorn;
TISSUE=Liver;
PubMed=1339283 [NCBI, ExPASy, EBI, Israel, Japan]
Chang L.-H., Fan J.-Y., Liu L.-F., Tsai S.-P., Tam M.F.;
"Cloning and expression of a chick liver glutathione S-transferase CL 3 subunit with the use of a baculovirus expression system.";
Biochem. J. 281:545-551(1992).

Comments

FUNCTION: Catalyzes the conjugation of GSH to a wide variety of electrophilic alkylating agents. Also involved in the metabolism of lipid hydroperoxides, prostaglandins and leukotriene A4 and in binding of non-substrate hydrophobic ligands such as bile acids, a number of drugs and thyroid hormones. This GST does not exhibit peroxidase activity.
CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
SUBUNIT: Homodimer or heterodimer (with a subunit from group CL-4).
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: The variations were found from AA sequencing and imply there are multiple forms of CL-3.
SIMILARITY: Belongs to the GST superfamily. Alpha family.
SIMILARITY: Contains 1 GST C-terminal domain.
SIMILARITY: Contains 1 GST N-terminal domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M38219; AAA62731.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S19734; S19734.

NP_990743.1; -.

3D structure databases

PDB

1VF1; X-ray; 1.77 A; A=1-229.	[ExPASy / RCSB / EBI]
1VF2; X-ray; 2.15 A; A/B=1-229.	[ExPASy / RCSB / EBI]
1VF3; X-ray; 2.15 A; A/B=1-229.	[ExPASy / RCSB / EBI]
1VF4; X-ray; 2.45 A; A=1-229.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1VF1; -.
1VF2; -.
1VF3; -.
1VF4; -.

ModBase

P26697.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004364;	Molecular function: glutathione transferase activity (inferred from electronic annotation from InterPro).
GO:0008152;	Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR010987; Glutathione-S-Trfase_C-like.
IPR003080; GST_alpha.
IPR004046; GST_C.
IPR004045; GST_N.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.1050.10; GST_C_like; 1.
G3DSA:3.40.30.10; Thioredoxin_fold; 1.

PANTHER

PTHR11571:SF4; GST_alpha; 1.

Pfam

PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR01266; GSTRNSFRASEA.

PROSITE

PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P26697.

Genome annotation databases

Ensembl

ENSGALG00000016322; Gallus gallus. [Contig view]

GeneID

396380; -.

KEGG

gga:396380; -.

Phylogenomic databases

HOGENOM

P26697; -.

HOVERGEN

P26697; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; Polymorphism; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 229`	`228`	`Glutathione S-transferase 3.`	`PRO_0000185800`
`DOMAIN`	`3 83`	`81`	`GST N-terminal.`
`DOMAIN`	`85 207`	`123`	`GST C-terminal.`
`MOD_RES`	`2 2`		`Blocked amino end (Ala).`
`VARIANT`	`45 45`	`1`	`L -> V.`
`VARIANT`	`47 47`	`1`	`S -> A.`
`VARIANT`	`49 49`	`1`	`I -> F.`
`VARIANT`	`49 49`	`1`	`I -> V.`
`VARIANT`	`52 52`	`1`	`F -> R.`
`VARIANT`	`129 130`	`2`	`TS -> AN.`
`VARIANT`	`135 136`	`2`	`AY -> VF.`
`VARIANT`	`155 155`	`1`	`W -> R.`
`VARIANT`	`158 159`	`2`	`IH -> VV.`
`VARIANT`	`163 163`	`1`	`A -> T.`
`VARIANT`	`166 166`	`1`	`M -> A.`
`VARIANT`	`168 168`	`1`	`E -> V.`
`STRAND`	`6 9`	`4`
`TURN`	`14 16`	`3`
`HELIX`	`17 25`	`9`
`STRAND`	`31 34`	`4`
`HELIX`	`38 47`	`10`
`STRAND`	`57 60`	`4`
`STRAND`	`63 67`	`5`
`HELIX`	`68 78`	`11`
`HELIX`	`86 104`	`19`
`HELIX`	`109 111`	`3`
`HELIX`	`114 130`	`17`
`HELIX`	`132 143`	`12`
`STRAND`	`146 149`	`4`
`HELIX`	`155 170`	`16`
`TURN`	`172 177`	`6`
`HELIX`	`179 190`	`12`
`HELIX`	`192 198`	`7`
`HELIX`	`210 220`	`11`

Sequence information

Length: 229 AA [This is the length of the unprocessed precursor]

Molecular weight: 26326 Da [This is the MW of the unprocessed precursor]

CRC64: EA30D949034BD8DB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAKPVLYYF NGRGKMESIR WLLAAAGVEF EEVFLETREQ YEKLLQSGIL MFQQVPMVEI 

        70         80         90        100        110        120 
DGMKLVQTRA ILNYIAGKYN LYGKDLKERA LIDMYVGGTD DLMGFLLSFP FLSAEDKVKQ 

       130        140        150        160        170        180 
CAFVVEKATS RYFPAYEKVL KDHGQDFLVG NRLSWADIHL LEAILMVEEK KSDALSGFPL 

       190        200        210        220 
LQAFKKRISS IPTIKKFLAP GSKRKPISDD KYVETVRRVL RMYYDVKPH

P26697 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools