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UniProtKB/Swiss-Prot entry P24472


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GSTA4_MOUSE
Primary accession number P24472
Secondary accession numbers Q9CQ81 Q9CTY7 Q9CY87 Q9D038
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on January 23, 2002 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 96)
Name and origin of the protein
Protein name Glutathione S-transferase A4
Synonyms EC 2.5.1.18
GST A4-4
GSTA4-4
Glutathione S-transferase 5.7
GST 5.7
GST class-alpha member 4
Gene name
Name: Gsta4
Synonyms: Gsta
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
DOI=10.1016/0014-5793(92)81438-R; PubMed=1426286 [NCBI, ExPASy, EBI, Israel, Japan]
Zimniak P., Eckles M.A., Saxena M., Awasthi Y.C.;
"A subgroup of class alpha glutathione S-transferases. Cloning of cDNA for mouse lung glutathione S-transferase GST 5.7.";
FEBS Lett. 313:173-176(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Embryo, Small intestine, and Tongue;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 106-120 AND 167-184.
STRAIN=CD-1;
TISSUE=Liver, and Lung;
PubMed=1898365 [NCBI, ExPASy, EBI, Israel, Japan]
Medh R.D., Saxena M., Singhal S.S., Ahmad H., Awasthi Y.C.;
"Characterization of a novel glutathione S-transferase isoenzyme from mouse lung and liver having structural similarity to rat glutathione S-transferase 8-8.";
Biochem. J. 278:793-799(1991).
[5]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
TISSUE=Lung;
DOI=10.1016/S0014-5793(98)00026-X; PubMed=9498801 [NCBI, ExPASy, EBI, Israel, Japan]
Krengel U., Schroter K.H., Hoier H., Arkema A., Kalk K.H., Zimniak P., Dijkstra B.W.;
"Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress.";
FEBS Lett. 422:285-290(1998).
[6]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
TISSUE=Lung;
DOI=10.1021/bi990468i; PubMed=10508391 [NCBI, ExPASy, EBI, Israel, Japan]
Xiao B., Singh S.P., Nanduri B., Awasthi Y.C., Zimniak P., Ji X.;
"Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: evidence of signaling across the dimer interface.";
Biochemistry 38:11887-11894(1999).
Comments
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
L06047; AAA37754.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008189; BAB25520.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008193; BAB25524.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008400; BAB25649.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008490; BAB25696.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK009668; BAB26429.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK010098; BAB26701.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011177; BAB27449.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011841; BAB27873.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK019100; BAB31546.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK019271; BAB31640.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012639; AAH12639.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S27234; S27234.
RefSeq NP_034487.2; -.
UniGene Mm.2662
3D structure databases
PDB
1B48; X-ray; 2.60 A; A/B=2-222.[ExPASy / RCSB / EBI]
1GUK; X-ray; 2.90 A; A/B=1-222.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1B48; -.
1GUK; -.
ModBase P24472.
PTM databases
PhosphoSite P24472; -.
2D gel databases
REPRODUCTION-2DPAGE P24472; -.
Organism-specific databases
MGI MGI:1309515; Gsta4.
Gene expression databases
ArrayExpress P24472; -.
CleanEx MM_GSTA4; -.
GermOnline ENSMUSG00000032348; Mus musculus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004364; Molecular function: glutathione transferase activity (traceable author statement from MGI).
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 P24472.
Genome annotation databases
Ensembl ENSMUSG00000032348; Mus musculus. [Contig view]
GeneID 14860; -.
KEGG mmu:14860; -.
NMPDR fig|10090.3.peg.20538; -.
Phylogenomic databases
HOGENOM P24472; -.
HOVERGEN P24472; -.
Other
DrugBank DB00143; Glutathione.
LinkHub P24472; -.
NextBio 287101; -.
SOURCE Gsta4; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Polymorphism; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   222  222     Glutathione S-transferase A4. PRO_0000185791
DOMAIN   3    83  81     GST N-terminal. 
DOMAIN   85   208  124     GST C-terminal. 
VARIANT   115   115  1     K -> P (requires 2 nucleotide substitutions). 
VARIANT   167   167  1     V -> G. 
VARIANT   179   180  2     PL -> GE. 
CONFLICT   36    36        E -> D (in Ref. 2; BAB31640). 
CONFLICT   205   206        KP -> SA (in Ref. 2; BAB27873). 
CONFLICT   218   218        T -> I (in Ref. 1; AAA37754). 
STRAND   6     9  4      
TURN   14    16  3      
HELIX   17    26  10      
HELIX   38    45  8      
TURN   46    48  3      
STRAND   50    53  4      
STRAND   57    60  4      
STRAND   63    65  3      
HELIX   68    78  11      
HELIX   86   108  23      
HELIX   109   111  3      
HELIX   114   131  18      
HELIX   133   142  10      
STRAND   145   152  8      
HELIX   155   168  14      
HELIX   174   177  4      
HELIX   179   189  11      
HELIX   192   198  7      
HELIX   210   219  10      
Sequence information
Length: 222 AA [This is the length of the unprocessed precursor] Molecular weight: 25564 Da [This is the MW of the unprocessed precursor] CRC64: B580E3415289424D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAKPKLYYF NGRGRMESIR WLLAAAGVEF EEEFLETREQ YEKMQKDGHL LFGQVPLVEI 

        70         80         90        100        110        120 
DGMMLTQTRA ILSYLAAKYN LYGKDLKERV RIDMYADGTQ DLMMMIAVAP FKTPKEKEES 

       130        140        150        160        170        180 
YDLILSRAKT RYFPVFEKIL KDHGEAFLVG NQLSWADIQL LEAILMVEEL SAPVLSDFPL 

       190        200        210        220 
LQAFKTRISN IPTIKKFLQP GSQRKPPPDG PYVEVVRTVL KF 

P24472 in FASTA format

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