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Q6PDE7 (GGT6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-glutamyltransferase 6
Short name=GGT 6
EC=2.3.2.2
Alternative name(s):
Gamma-glutamyltranspeptidase 6

Cleaved into the following 2 chains:

  1. Gamma-glutamyltransferase 6 heavy chain
  2. Gamma-glutamyltransferase 6 light chain
Gene names
Name:Ggt6
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cleaves glutathione conjugates By similarity.

Catalytic activity

(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid.

Glutathione + H2O = L-cysteinylglycine + L-glutamate.

Pathway

Sulfur metabolism; glutathione metabolism.

Subunit structure

Heterodimer composed of the light and heavy chains. The active site is located in the light chain By similarity.

Subcellular location

Membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Sequence caution

The sequence BAB31233.1 differs from that shown. Reason: Erroneous termination at position 354. Translated as Glu.

The sequence BAB31233.1 differs from that shown. Reason: Frameshift at positions 329 and 338.

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   PTMGlycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglutathione biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiongamma-glutamyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PDE7-1)

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 2 (identifier: Q6PDE7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     117-154: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ?Gamma-glutamyltransferase 6 heavy chainPRO_0000314956
Chain? – 497Gamma-glutamyltransferase 6 light chainPRO_0000314957

Regions

Topological domain1 – 5151Cytoplasmic Potential
Transmembrane52 – 7221Helical; Signal-anchor for type II membrane protein; Potential
Topological domain73 – 497425Extracellular Potential
Compositional bias21 – 3212Poly-Glu

Amino acid modifications

Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation1691N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence117 – 15438Missing in isoform 2.
VSP_030452

Experimental info

Sequence conflict3041E → K in BAB31233. Ref.1
Sequence conflict315 – 3195VLFTT → GLLTN in BAB31233. Ref.1
Sequence conflict3291V → G in BAB31233. Ref.1
Sequence conflict3341S → F in BAB31233. Ref.1
Sequence conflict3391R → G in BAB31233. Ref.1
Sequence conflict3431S → F in BAB31233. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 2E9C8CCD73F8AD42

FASTA49751,467
        10         20         30         40         50         60 
MDATTGPVHY HKLQLWEPGV ESEEEEEEEE EEIAEPLVLS LRRLQNTPRN EVGGLPGAWA 

        70         80         90        100        110        120 
RLLAGLLLLA VSSSLALRQL HSRDSPRGNL GSVAPPASRH SHRPGVYHHS AIISPAATCS 

       130        140        150        160        170        180 
QLGQELLVAG GNVVDAGVGA ALCLAVVHPH ATGLGATFWG LFYNSSSGNS TALTAGPTQL 

       190        200        210        220        230        240 
LAPGLGLPTG LPALHLLHAH FGRLPWPHLL TKPAMLAEKG FEVDAPLANA LAIQGTKGLC 

       250        260        270        280        290        300 
PLFCHTNGTP LGLGARATNP NLAAVLRSAA LASSPDLAGK ALLNPLVRDL GLELPSAQPV 

       310        320        330        340        350        360 
PSLEPALQLL LPRGVLFTTP GPSAGPELVE LLESTLHSRT PSSAPCPPFL QTAETPVSSA 

       370        380        390        400        410        420 
LATVDSNGSM LLLISSINSS FGSGHLSPST GVLLSNLEAS PAPSAWACPL ILRDNLDDTE 

       430        440        450        460        470        480 
ADMLGMVASG ISRGAKAMTC TLLNHLATPQ IPQQPQHQRP TESPGICGQG ALLQAVVHAE 

       490 
HAHVSSVPSG CCPFQGY

« Hide

Isoform 2 [UniParc].

Checksum: 6DA5E6BCD9C3F71D
Show »

FASTA45947,872

References

[1]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Colon.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK018485 mRNA. Translation: BAB31233.1. Sequence problems.
AL662812 Genomic DNA. Translation: CAI52002.1.
AL662812 Genomic DNA. Translation: CAI52003.1.
BC058747 mRNA. Translation: AAH58747.1.
IPIIPI00420791.
IPI00648222.
RefSeqNP_082095.2. NM_027819.2.
UniGeneMm.23336.

3D structure databases

ProteinModelPortalQ6PDE7.
SMRQ6PDE7. Positions 100-333.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6PDE7.

Protein family/group databases

MEROPST03.022.

Proteomic databases

PRIDEQ6PDE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000076443; ENSMUSP00000075773; ENSMUSG00000040471.
ENSMUST00000100903; ENSMUSP00000098463; ENSMUSG00000040471.
GeneID71522.
KEGGmmu:71522.
UCSCuc007jyw.1. mouse.

Organism-specific databases

CTD124975.
MGIMGI:1918772. Ggt6.

Phylogenomic databases

HOGENOMHBG505865.
HOVERGENHBG055504.
InParanoidQ6PDE7.
OMACPLLCHA.
PhylomeDBQ6PDE7.

Gene expression databases

ArrayExpressQ6PDE7.
BgeeQ6PDE7.
CleanExMM_GGT6.
GenevestigatorQ6PDE7.

Family and domain databases

InterProIPR000101. GGT_peptidase.
[Graphical view]
KOK00681.
PANTHERPTHR11686. GGT_peptidase. 1 hit.
PfamPF01019. G_glu_transpept. 2 hits.
[Graphical view]
PRINTSPR01210. GGTRANSPTASE.
PROSITEPS00462. G_GLU_TRANSPEPTIDASE. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio333939.
SOURCESearch...

Entry information

Entry nameGGT6_MOUSE
AccessionPrimary (citable) accession number: Q6PDE7
Secondary accession number(s): Q5F245, Q9D347
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: November 16, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents