Reviewed, UniProtKB/Swiss-Prot O77462 (GST1A_ANOGA)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase 1, isoform A
    EC=2.5.1.18
Alternative name(s):
    GST class-theta
    AgGst1-alpha
    Aggst1-3

Gene names

Name:	GstD1
Synonyms:	GST1a
ORF Names:	AGAP004164

Organism

Anopheles gambiae (African malaria mosquito) [Complete proteome]

Taxonomic identifier

7165 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles

Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles By similarity. UniProtKB P30711
Catalytic activity	RX + glutathione = HX + R-S-glutathione. UniProtKB P30711
Enzyme regulation	Inhibited by S-hexylglutathione By similarity.
Subunit structure	Homodimer. Binds one molecule of S-hexylglutathione inhibitor per subunit By similarity.
Sequence similarities	Belongs to the GST superfamily. Theta family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutathione metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	extracellular region Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	glutathione transferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform A Ref.1 (identifier: O77462-1)

Also known as: 1-3;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B Ref.1 (identifier: O77473-1)

Also known as: 1-4;

The sequence of this isoform can be found in the external entry O77473-1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform C Ref.1 (identifier: Q93112-1)

Also known as: 1-5;

The sequence of this isoform can be found in the external entry Q93112-1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform D Ref.1 (identifier: Q93113-1)

Also known as: 1-1; 1-6; 2-1;

The sequence of this isoform can be found in the external entry Q93113-1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 218	218	Glutathione S-transferase 1, isoform A		PRO_0000283092
Regions
	Domain	1 – 81	81	GST N-terminal
	Domain	92 – 219	128	GST C-terminal
	Region	6 – 11	6	S-hexylglutathione-binding By similarity
	Region	50 – 53	4	S-hexylglutathione-binding By similarity
	Region	65 – 67	3	S-hexylglutathione-binding By similarity
	Region	211 – 215	5	S-hexylglutathione-binding By similarity
Sites
	Active site	9	1	By similarity
	Binding site	33	1	S-hexylglutathione By similarity
	Binding site	38	1	S-hexylglutathione By similarity
	Binding site	111	1	S-hexylglutathione By similarity
	Binding site	119	1	S-hexylglutathione By similarity
Experimental info
	Sequence conflict	170 – 171	2	FW → S in AAC79992. Ref.1
	Sequence conflict	170 – 171	2	FW → S in AAC79999. Ref.1
	Sequence conflict	199	1	V → A in AAC79992. Ref.1
	Sequence conflict	199	1	V → A in AAC79999. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (1-3) [UniParc]. Last modified December 4, 2007. Version 2. Checksum: E67C7A96BE7653B5	FASTA	219	25,203
	10 20 30 40 50 60 MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKLNPQH CIPTLVDEDG 70 80 90 100 110 120 FVLWESRAIQ IYLVEKYCAH DPALAERLYP GDPRRRAVVH QRLFFDVAIL YQRFAEYYYP 130 140 150 160 170 180 QIFGKKVAGD PDRLRSMEQA LEFLNTFLEG ERFVAGGDDP TIADFSILAF WIATFDAAGY 190 200 210 DLRRYENIHR WYEQTGNIVP AADKNLAGAK IFGLYFRQK
	Isoform B (1-4). See O77473.	FASTA	–	–
	Isoform C (1-5). See Q93112.	FASTA	–	–
	Isoform D (1-1) (1-6) (2-1). See Q93113.	FASTA	–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The role of alternative mRNA splicing in generating heterogeneity within the Anopheles gambiae class I glutathione S-transferase family." Ranson H., Collins F.H., Hemingway J. Proc. Natl. Acad. Sci. U.S.A. 95:14284-14289(1998) [PubMed: 9826692] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING. Strain: ZAN/U.
[2]	"The genome sequence of the malaria mosquito Anopheles gambiae." Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L. Science 298:129-149(2002) [PubMed: 12364791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF071163 mRNA. Translation: AAC79999.1. AF071160 Genomic DNA. Translation: AAC79992.1. AAAB01008880 Genomic DNA. Translation: EAL40658.1.
RefSeq	XP_562680.1.
3D structure databases
HSSP	HSSP built from PDB template 1JLW based on UniProtKB Q9GN60.
SMR	O77462. Positions 1-215.
ModBase	Search...
Genome annotation databases
Ensembl	AGAP004164. Anopheles gambiae. [Contig view]
GeneID	1273988.
VectorBase	AGAP004163. Anopheles gambiae.
Phylogenomic databases
OMA	O77462. RSAIALE.
Enzyme and pathway databases
BRENDA	2.5.1.18. 165157.
Family and domain databases
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:1.20.1050.10. GST_C_like. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF02798. GST_N. 1 hit. [Graphical view]
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GST1A_ANOGA

Accession

Primary (citable) accession number: O77462
Secondary accession number(s): Q5TTE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	December 4, 2007
Last modified:	June 16, 2009
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)