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Reviewed, UniProtKB/Swiss-Prot Q9QWE9 (GGT5_RAT)

Last modified October 13, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Gamma-glutamyltransferase 5
    EC=2.3.2.2
Alternative name(s):
    Gamma-glutamyltranspeptidase 5
      Short name=GGT 5
    Gamma-glutamyltransferase-like activity 1
    Gamma-glutamyl transpeptidase-related enzyme
      Short name=GGT-rel
    Gamma-glutamyl leukotrienase
      Short name=GGL
Cleaved into the following 2 chains:
    1- Recommended name:
            Gamma-glutamyltransferase 5 heavy chain
    2- Recommended name:
            Gamma-glutamyltransferase 5 light chain
Gene names
Name: Ggt5
Synonyms: Ggtla1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4).

Catalytic activity

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

Pathway

Sulfur metabolism; glutathione metabolism.

Lipid metabolism; leukotriene D4 biosynthesis.

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.

Tissue specificity

Widely expressed, but at low level, except in the airway epithelial cells. Detected in brain, heart, kidney, liver, lung, spleen, testis and trachea.

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 387387Gamma-glutamyltransferase 5 heavy chain By similarity
PRO_0000011076
Chain388 – 572185Gamma-glutamyltransferase 5 light chain By similarity
PRO_0000011077

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Signal-anchor for type II membrane protein Potential
Topological domain30 – 572543Extracellular Potential

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Potential
Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2771N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation3771N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9QWE9-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 25F394CAC37D842E

FASTA57261,609
        10         20         30         40         50         60 
MAWGHRTTVC LVLLGVSLGL AIIVLAVVLP HHQASCRPDA FTRAAVAADS KICSDIGRVI 

        70         80         90        100        110        120 
LQQQGSPVDA AIAALICTGV VNPQSMGLGG GVVFTIYNAS TGKVEVINAR ETVPASHDQR 

       130        140        150        160        170        180 
LLDQCTNALP LCTGAQWIGV PGELRGYAEA HRRYGRLPWA QLFQPTIALL REGFRVPPIL 

       190        200        210        220        230        240 
SQFLNTSFLQ PCLNSSTLRH LFFNGTETLR SQDPLPWPAL ANTLETVAKE GAEVLYTGKL 

       250        260        270        280        290        300 
GQTLVEDIAW QGSQLTVQDL AAFRPKVVEP LEMALGNYTL YSPPPPAGGA ILSFILNVLK 

       310        320        330        340        350        360 
GFNFSAETVA GPEGKVNMYH HLVETLKFAV GQRWRLWDPY SHPGIQNISQ DLLRETLAQH 

       370        380        390        400        410        420 
IRQQIDGRGD HQLSHYNLSG VRGNSMGTSH VSVLGEDGSA VAATSTINTP FGAMVYSPRT 

       430        440        450        460        470        480 
GILLNNELLD LCWRHKPGST VTPPPVPGEQ PPSSMVPSIL INEVQGSKLV IGGAGGELII 

       490        500        510        520        530        540 
SAVTQAIVNK LWLGFSLTDA IAAPILHVNS KGHVEYEPKF NQEVRKGLQD RGQSQSQSQR 

       550        560        570 
PVFLNSVQAV FQEGPCVYAA SDLRKAGKAS GY 

« Hide

References

[1]"Expression and regulation of gamma-glutamyl transpeptidase-related enzyme in tracheal cells."
Potdar P.D., Andrews K.L., Nettesheim P., Ostrowski L.E.
Am. J. Physiol. 273:L1082-L1089(1997) [PubMed: 9374738] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Fischer 344/N.
Tissue: Trachea.
+Additional computationally mapped references.

Cross-references

Sequence databases

U76252 mRNA. Translation: AAC23546.1.
IPIIPI00212106.
UniGeneRn.44367

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPST03.002.

Proteomic databases

PRIDEQ9QWE9.

Organism-specific databases

RGD2684. Ggt5.

Phylogenomic databases

HOVERGENQ9QWE9.

Enzyme and pathway databases

BRENDA2.3.2.2. 248.

Gene expression databases

GenevestigatorQ9QWE9.

Family and domain databases

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

Entry information

Entry nameGGT5_RAT
AccessionPrimary (citable) accession number: Q9QWE9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: May 1, 2000
Last modified: October 13, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents