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Q99JP7 (GGT7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-glutamyltransferase 7
Short name=GGT 7
EC=2.3.2.2
Alternative name(s):
Gamma-glutamyltransferase-like 3
Gamma-glutamyltranspeptidase 7

Cleaved into the following 2 chains:

  1. Gamma-glutamyltransferase 7 heavy chain
  2. Gamma-glutamyltransferase 7 light chain
Gene names
Name:Ggt7
Synonyms:Ggtl3
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 length662 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Interacts with FAM57A By similarity.

Subcellular location

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

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   Cellular componentMembrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   PTMGlycoprotein
Phosphoprotein
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Gamma-glutamyltransferase 7 heavy chain By similarity
PRO_0000011068
Chain473 – 662190Gamma-glutamyltransferase 7 light chain By similarity
PRO_0000011069

Regions

Topological domain1 – 106106Cytoplasmic Potential
Transmembrane107 – 12721Helical; Signal-anchor for type II membrane protein; Potential
Topological domain128 – 662535Extracellular Potential

Amino acid modifications

Modified residue721Phosphoserine By similarity
Modified residue831Phosphoserine Ref.5
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Glycosylation3941N-linked (GlcNAc...) Potential
Glycosylation5191N-linked (GlcNAc...) Potential
Glycosylation5231N-linked (GlcNAc...) Potential
Glycosylation5861N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1481S → H in AAH05772. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q99JP7 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: BA7F3413D694F381

FASTA66270,251
        10         20         30         40         50         60 
MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAAP LRGRKDEDAF LGDPDTDPDS 

        70         80         90        100        110        120 
FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAAAEC SCRQDGLTVI VTACLTFATG 

       130        140        150        160        170        180 
VTVALVMQIY FGDPQIFQQG AVVTDASSCT ALGMEVLSKQ GSSVDAAVAA ALCLGIVAPH 

       190        200        210        220        230        240 
SSGLGGGGVM LVHDIRRNES HLIDFRESAP GALREEALQR SWDTKPGLLV GVPGMVKGLH 

       250        260        270        280        290        300 
EAHQLYGRLP WSQVLAFAAA VAQDGFNVTH DLAHALAEQL PPNASDRFLD TFLPLGHPPL 

       310        320        330        340        350        360 
PGSLLRRPDL AEVLDILGTS GPAAFYNGGN LTLEMVAEAQ HAGGVITEED FSNYSALTEK 

       370        380        390        400        410        420 
PVCGVYRGHL VLSPPPPHTG PALISALNIL EGFNLTSLVS REQALHWVAE TLKIALALAS 

       430        440        450        460        470        480 
RLGDPVYDST ITESMDDMLS KVEAANFRGH ISDSQAAPAP LLPVYELDGA PTAAQVLVMG 

       490        500        510        520        530        540 
PDDFIVAMVS SLNRPFGSGL LTPSGILLNS QMLDFSWPNR TANHSAPSLE NSVQPGKRPL 

       550        560        570        580        590        600 
SFLLPTVVRP AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL 

       610        620        630        640        650        660 
QSNLLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNTFIIGVKD PRSPDAAGAT 


IL

« Hide

References

« Hide 'large scale' 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].
Strain: C57BL/6J.
Tissue: Medulla oblongata.
[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/6.
[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].
Tissue: Mammary cancer.
[4]"High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
Mamm. Genome 12:657-663(2001) [PubMed: 11471062] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-662.
Strain: ILS and ISS.
[5]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY.
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK032051 mRNA. Translation: BAC27672.1.
AL844852 Genomic DNA. Translation: CAM18929.1.
BC005772 mRNA. Translation: AAH05772.1.
AF332053 mRNA. Translation: AAK56082.1.
AF332054 mRNA. Translation: AAK56083.1.
IPIIPI00115429.
RefSeqNP_659035.2. NM_144786.2.
UniGeneMm.41757.

3D structure databases

ProteinModelPortalQ99JP7.
SMRQ99JP7. Positions 134-659.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ99JP7.

Protein family/group databases

MEROPST03.017.

PTM databases

PhosphoSiteQ99JP7.

Proteomic databases

PRIDEQ99JP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029131; ENSMUSP00000029131; ENSMUSG00000027603.
GeneID207182.
KEGGmmu:207182.

Organism-specific databases

CTD2686.
MGIMGI:1913385. Ggt7.

Phylogenomic databases

GeneTreeENSGT00550000074591.
HOGENOMHBG738311.
HOVERGENHBG039468.
InParanoidQ99JP7.
OrthoDBEOG483D48.
PhylomeDBQ99JP7.

Gene expression databases

ArrayExpressQ99JP7.
BgeeQ99JP7.
CleanExMM_GGT7.
GenevestigatorQ99JP7.
GermOnlineENSMUSG00000027603. Mus musculus.

Family and domain databases

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

Other

NextBio371879.
SOURCESearch...

Entry information

Entry nameGGT7_MOUSE
AccessionPrimary (citable) accession number: Q99JP7
Secondary accession number(s): A2AQN1, Q91V91
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: July 27, 2011
Last modified: November 16, 2011
This is version 84 of the entry and version 2 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents