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Q6IE08 (GGT6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length498 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.

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   Cellular componentMembrane
   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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ?Gamma-glutamyltransferase 6 heavy chainPRO_0000314958
Chain? – 498Gamma-glutamyltransferase 6 light chainPRO_0000314959

Regions

Topological domain1 – 4949Cytoplasmic Potential
Transmembrane50 – 7021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain71 – 498428Extracellular Potential
Compositional bias21 – 3010Poly-Glu

Amino acid modifications

Glycosylation1621N-linked (GlcNAc...) Potential
Glycosylation1671N-linked (GlcNAc...) Potential
Glycosylation3761N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q6IE08 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D88B4463EE6BE62F

FASTA49851,559
        10         20         30         40         50         60 
MDATTGAVLY QKLQLWEPGM ESEEEEEEEE IAEPLVLSLR RLQNTPGNKV GGLPGAWTRL 

        70         80         90        100        110        120 
LAGLLLLAVS SSLALRQLQG RNSPKGNLGP VDLPASRHSH HPGVYHHSAV ISPAATCSRL 

       130        140        150        160        170        180 
GQELLVAGGN VVDAGVGAAL CLAVVHPHAT GLGATFWGLF YNSSSGNSTA LTAGPAQILA 

       190        200        210        220        230        240 
PGLGLPTALP ALHLLHTHFG RLPWSHLLAK PAMLAQKGFE VDAPLASALA AQGTEGLCPL 

       250        260        270        280        290        300 
FCHTNGTPLG LGAQVTNPNL AAVLLREALA SSPDLVGNAL LNLLVRDLGL ELPSVQPKPS 

       310        320        330        340        350        360 
LEPALQLLLP QGVLFTTPGP SAGPELMGLL ESTLHSKTPS PASCSSLLQT AETPVSSALA 

       370        380        390        400        410        420 
TVDSHGSMLL LTSSLNSSFG SGHLSPSTGV LLSNLEASSV PSTWACPLIL RGNLDDTEDD 

       430        440        450        460        470        480 
MLGLVASGIP RGAKAMACTL FNHLTTPQTQ QQVQHQAQQR PTESPGICGK EALLQVVVHA 

       490 
EHAQVSSIPS GCCPFQGY

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed: 15057822] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"A genomic analysis of rat proteases and protease inhibitors."
Puente X.S., Lopez-Otin C.
Genome Res. 14:609-622(2004) [PubMed: 15060002] [Abstract]
Cited for: IDENTIFICATION.
Strain: Sprague-Dawley.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC095632 Genomic DNA. No translation available.
BN000385 mRNA. Translation: CAE51911.1.
IPIIPI00421740.
RefSeqNP_001002820.1. NM_001002820.1.
UniGeneRn.113458.

3D structure databases

ProteinModelPortalQ6IE08.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6IE08.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000045100; ENSRNOP00000039691; ENSRNOG00000015210.
GeneID408206.
KEGGrno:408206.

Organism-specific databases

CTD124975.
RGD1303335. Ggt6.

Phylogenomic databases

eggNOGroNOG10080.
GeneTreeENSGT00550000074591.
HOVERGENHBG055504.
InParanoidQ6IE08.
OMACPLLCHA.
OrthoDBEOG4D26QR.
PhylomeDBQ6IE08.

Gene expression databases

GenevestigatorQ6IE08.

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

NextBio696406.

Entry information

Entry nameGGT6_RAT
AccessionPrimary (citable) accession number: Q6IE08
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: November 16, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

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