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Protein

Glutathione S-transferase Mu 5

Gene

Gstm5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191SubstrateBy similarity

GO - Molecular functioni

  • enzyme binding Source: MGI
  • glutathione binding Source: MGI
  • glutathione transferase activity Source: MGI
  • identical protein binding Source: MGI
  • protein homodimerization activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_317599. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 5 (EC:2.5.1.18)
Alternative name(s):
Fibrous sheath component 2
Short name:
Fsc2
GST class-mu 5
Gene namesi
Name:Gstm5
Synonyms:Fsc2, Gstm3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1309466. Gstm5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • nucleus Source: MGI
  • sperm fibrous sheath Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 224224Glutathione S-transferase Mu 5PRO_0000185829Add
BLAST

Proteomic databases

MaxQBiP48774.
PaxDbiP48774.
PRIDEiP48774.

PTM databases

PhosphoSiteiP48774.

Expressioni

Gene expression databases

BgeeiP48774.
CleanExiMM_GSTM3.
MM_GSTM5.
ExpressionAtlasiP48774. baseline and differential.
GenevisibleiP48774. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with PFKM isoform 2 and isoform 3 (via N-terminal testis-specific region) (PubMed:19889946).By similarity1 Publication

Protein-protein interaction databases

IntActiP48774. 2 interactions.
MINTiMINT-4096984.
STRINGi10090.ENSMUSP00000004134.

Structurei

3D structure databases

ProteinModelPortaliP48774.
SMRiP48774. Positions 5-224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 9188GST N-terminalAdd
BLAST
Domaini93 – 211119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 112Glutathione bindingBy similarity
Regioni49 – 535Glutathione bindingBy similarity
Regioni62 – 632Glutathione bindingBy similarity
Regioni75 – 762Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP48774.
KOiK00799.
OMAiMSCESSM.
OrthoDBiEOG7KH9M3.
PhylomeDBiP48774.
TreeFamiTF353040.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48774-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKSMVLGY WDIRGLAHAI RMLLEFTDTS YEEKRYICGE APDYDRSQWL
60 70 80 90 100
DVKFKLDLDF PNLPYLMDGK NKITQSNAIL RYIARKHNMC GDTEEEKIRV
110 120 130 140 150
DIMENQIMDF RMQLVRLCYN SNHENLKPQY LEQLPAQLKQ FSLFLGKFTW
160 170 180 190 200
FAGEKLTFVD FLTYDVLDQN RIFEPKCLDE FPNLKAFMCR FEALEKIAAF
210 220
LQSDRFFKMP INNKMAKWGN KCLC
Length:224
Mass (Da):26,635
Last modified:February 1, 1996 - v1
Checksum:i70122FD0682237E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24428 mRNA. Translation: AAB04096.1.
AK002750 mRNA. Translation: BAB22327.1.
AK019317 mRNA. Translation: BAB31661.1.
AK028098 mRNA. Translation: BAC25746.1.
BC008206 mRNA. Translation: AAH08206.1.
CCDSiCCDS17741.1.
RefSeqiNP_034490.1. NM_010360.2.
UniGeneiMm.282351.

Genome annotation databases

EnsembliENSMUST00000004134; ENSMUSP00000004134; ENSMUSG00000004032.
GeneIDi14866.
KEGGimmu:14866.
UCSCiuc008qxs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24428 mRNA. Translation: AAB04096.1.
AK002750 mRNA. Translation: BAB22327.1.
AK019317 mRNA. Translation: BAB31661.1.
AK028098 mRNA. Translation: BAC25746.1.
BC008206 mRNA. Translation: AAH08206.1.
CCDSiCCDS17741.1.
RefSeqiNP_034490.1. NM_010360.2.
UniGeneiMm.282351.

3D structure databases

ProteinModelPortaliP48774.
SMRiP48774. Positions 5-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP48774. 2 interactions.
MINTiMINT-4096984.
STRINGi10090.ENSMUSP00000004134.

PTM databases

PhosphoSiteiP48774.

Proteomic databases

MaxQBiP48774.
PaxDbiP48774.
PRIDEiP48774.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004134; ENSMUSP00000004134; ENSMUSG00000004032.
GeneIDi14866.
KEGGimmu:14866.
UCSCiuc008qxs.1. mouse.

Organism-specific databases

CTDi2949.
MGIiMGI:1309466. Gstm5.

Phylogenomic databases

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP48774.
KOiK00799.
OMAiMSCESSM.
OrthoDBiEOG7KH9M3.
PhylomeDBiP48774.
TreeFamiTF353040.

Enzyme and pathway databases

ReactomeiREACT_317599. Glutathione conjugation.

Miscellaneous databases

ChiTaRSiGstm5. mouse.
NextBioi287121.
PROiP48774.
SOURCEiSearch...

Gene expression databases

BgeeiP48774.
CleanExiMM_GSTM3.
MM_GSTM5.
ExpressionAtlasiP48774. baseline and differential.
GenevisibleiP48774. MM.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a unique mu-class glutathione S-transferase in mouse spermatogenic cells."
    Fulcher K.D., Welch J.E., Klapper D.G., O'Brien D.A., Eddy E.M.
    Mol. Reprod. Dev. 42:415-424(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hippocampus, Kidney and Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  4. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 22-34; 54-70; 71-81; 156-171 AND 197-205, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. "Molecular complex of three testis-specific isozymes associated with the mouse sperm fibrous sheath: hexokinase 1, phosphofructokinase M, and glutathione S-transferase mu class 5."
    Nakamura N., Mori C., Eddy E.M.
    Biol. Reprod. 82:504-515(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PFKM.

Entry informationi

Entry nameiGSTM5_MOUSE
AccessioniPrimary (citable) accession number: P48774
Secondary accession number(s): Q545W5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 24, 2015
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.