P46088 (GST_OMMSL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Glutathione S-transferase EC=2.5.1.18 Alternative name(s): GST class-sigma
Organism	Ommastrephes sloanei (Arrow squid) (Sloane's squid)
Taxonomic identifier	215440 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Mollusca › Cephalopoda › Coleoidea › Neocoleoidea › Decapodiformes › Teuthida › Oegopsina › Ommastrephidae › Nototodarus

Protein attributes

Sequence length	203 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	High activity toward 1-chloro-2,4-dinitrobenzene. Not very efficient at catalyzing the addition of GSH to enones and epoxides. Ref.2
Catalytic activity	RX + glutathione = HX + R-S-glutathione. Ref.2
Subunit structure	Homodimer. Ref.2
Subcellular location	Cytoplasm.
Tissue specificity	More abundant in the digestive gland than in the testis, mantle, or lens.
Sequence similarities	Belongs to the GST superfamily. Sigma family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutathione transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 203

203

Glutathione S-transferase

PRO_0000185920

Regions

Domain

2 – 79

78

GST N-terminal

Domain

81 – 203

123

GST C-terminal

Region

49 – 51

3

Glutathione binding

Region

63 – 64

2

Glutathione binding

Sites

Binding site

8

1

Glutathione

Binding site

39

1

Glutathione

Binding site

43

1

Glutathione

Natural variations

Natural variant

124

1

C → Y.

Experimental info

Mutagenesis

107

1

F → Y: Improves action on epones and epoxides.

Secondary structure

1

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203

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Beta strand

10 – 12

3

Helix

13 – 15

3

Helix

16 – 24

9

Beta strand

30 – 33

4

Turn

36 – 38

3

Helix

39 – 42

4

Helix

43 – 45

3

Helix

47 – 49

3

Beta strand

53 – 56

4

Beta strand

59 – 61

3

Helix

64 – 74

11

Helix

82 – 106

25

Helix

113 – 136

24

Turn

137 – 140

4

Beta strand

141 – 143

3

Helix

152 – 167

16

Turn

169 – 174

6

Helix

176 – 186

11

Helix

189 – 197

9

Sequences

	Sequence		Length	Mass (Da)
	P46088 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: F46F56682F1C9591	FASTA	203	22,919
	10 20 30 40 50 60 MPKYTLHYFP LMGRAELCRF VLAAHGEEFT DRVVEMADWP NLKATMYSNA MPVLDIDGTK 70 80 90 100 110 120 MSQSMCIARH LAREFGLDGK TSLEKYRVDE ITETLQDIFN DVVKIKFAPE AAKEAVQQNY 130 140 150 160 170 180 EKSCKRLAPF LEGLLVSNGG GDGFFVGNSM TLADLHCYVA LEVPLKHTPE LLKDCPKIVA 190 200 LRKRVAECPK IAAYLKKRPV RDF

References

[1]	"Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods." Tomarev S.I., Zinovieva R.D., Guo K., Piatigorsky J. J. Biol. Chem. 268:4534-4542(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-60 AND 86-104. Strain: Pacificus. Tissue: Digestive gland.
[2]	"Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods." Ji X., von Rosenvinge E.C., Johnson W.W., Tomarev S.I., Piatigorsky J., Armstrong R.N., Gilliland G.L. Biochemistry 34:5317-5328(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
[3]	"Location of a potential transport binding site in a sigma class glutathione transferase by X-ray crystallography." Ji X., von Rosenvinge E.C., Johnson W.W., Armstrong R.N., Gilliland G.L. Proc. Natl. Acad. Sci. U.S.A. 93:8208-8213(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L02054 , L02053, L02052, L02051, L02050 Genomic DNA. Translation: AAA92066.1.

PIR

A45463.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GSQ	X-ray	2.40	A	2-203	[»]
2GSQ	X-ray	2.20	A	2-203	[»]

ProteinModelPortal

P46088.

SMR

P46088. Positions 2-203.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

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.
IPR003083. S-crystallin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PRINTS

PR01269. SCRYSTALLIN.

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

EvolutionaryTrace

P46088.

Entry information

Entry name

GST_OMMSL

Accession

Primary (citable) accession number: P46088

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)