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Protein

Gamma-glutamyltransferase 5

Gene

Ggt5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.
Glutathione + H2O = L-cysteinylglycine + L-glutamate.
Leukotriene C4 + H2O = leukotriene D4 + L-glutamate.

Pathwayi: glutathione metabolism

This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.

Pathwayi: leukotriene D4 biosynthesis

This protein is involved in the pathway leukotriene D4 biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway leukotriene D4 biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101GlutamateBy similarity
Active sitei388 – 3881NucleophileBy similarity
Binding sitei406 – 4061GlutamateBy similarity
Binding sitei427 – 4271GlutamateBy similarity

GO - Molecular functioni

GO - Biological processi

  • glutathione biosynthetic process Source: UniProtKB-KW
  • leukotriene biosynthetic process Source: UniProtKB-KW
  • response to organonitrogen compound Source: RGD
  • response to oxidative stress Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Hydrolase, Protease, Transferase

Keywords - Biological processi

Glutathione biosynthesis, Leukotriene biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00204.
UPA00880.

Protein family/group databases

MEROPSiT03.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyltransferase 5 (EC:2.3.2.2)
Short name:
GGT 5
Alternative name(s):
Gamma-glutamyl leukotrienase
Short name:
GGL
Gamma-glutamyl transpeptidase-related enzyme
Short name:
GGT-rel
Gamma-glutamyltransferase-like activity 1
Gamma-glutamyltranspeptidase 5
Glutathione hydrolase 5 (EC:3.4.19.13)
Leukotriene-C4 hydrolase (EC:3.4.19.14)
Cleaved into the following 2 chains:
Gene namesi
Name:Ggt5
Synonyms:Ggtla1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2684. Ggt5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini30 – 572543ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 387387Gamma-glutamyltransferase 5 heavy chainBy similarityPRO_0000011076Add
BLAST
Chaini388 – 572185Gamma-glutamyltransferase 5 light chainBy similarityPRO_0000011077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence analysis
Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence analysis
Glycosylationi194 – 1941N-linked (GlcNAc...)Sequence analysis
Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence analysis
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence analysis
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence analysis
Glycosylationi377 – 3771N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Cleaved by autocatalysis into a large and a small subunit.By similarity

Keywords - PTMi

Glycoprotein, Zymogen

Proteomic databases

PRIDEiQ9QWE9.

PTM databases

PhosphoSiteiQ9QWE9.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ9QWE9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni453 – 4542Glutamate bindingBy similarity

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG005835.
InParanoidiQ9QWE9.
PhylomeDBiQ9QWE9.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QWE9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWGHRTTVC LVLLGVSLGL AIIVLAVVLP HHQASCRPDA FTRAAVAADS
60 70 80 90 100
KICSDIGRVI LQQQGSPVDA AIAALICTGV VNPQSMGLGG GVVFTIYNAS
110 120 130 140 150
TGKVEVINAR ETVPASHDQR LLDQCTNALP LCTGAQWIGV PGELRGYAEA
160 170 180 190 200
HRRYGRLPWA QLFQPTIALL REGFRVPPIL SQFLNTSFLQ PCLNSSTLRH
210 220 230 240 250
LFFNGTETLR SQDPLPWPAL ANTLETVAKE GAEVLYTGKL GQTLVEDIAW
260 270 280 290 300
QGSQLTVQDL AAFRPKVVEP LEMALGNYTL YSPPPPAGGA ILSFILNVLK
310 320 330 340 350
GFNFSAETVA GPEGKVNMYH HLVETLKFAV GQRWRLWDPY SHPGIQNISQ
360 370 380 390 400
DLLRETLAQH IRQQIDGRGD HQLSHYNLSG VRGNSMGTSH VSVLGEDGSA
410 420 430 440 450
VAATSTINTP FGAMVYSPRT GILLNNELLD LCWRHKPGST VTPPPVPGEQ
460 470 480 490 500
PPSSMVPSIL INEVQGSKLV IGGAGGELII SAVTQAIVNK LWLGFSLTDA
510 520 530 540 550
IAAPILHVNS KGHVEYEPKF NQEVRKGLQD RGQSQSQSQR PVFLNSVQAV
560 570
FQEGPCVYAA SDLRKAGKAS GY
Length:572
Mass (Da):61,609
Last modified:May 1, 2000 - v1
Checksum:i25F394CAC37D842E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76252 mRNA. Translation: AAC23546.1.
UniGeneiRn.44367.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76252 mRNA. Translation: AAC23546.1.
UniGeneiRn.44367.

3D structure databases

ProteinModelPortaliQ9QWE9.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiT03.002.

PTM databases

PhosphoSiteiQ9QWE9.

Proteomic databases

PRIDEiQ9QWE9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi2684. Ggt5.

Phylogenomic databases

HOVERGENiHBG005835.
InParanoidiQ9QWE9.
PhylomeDBiQ9QWE9.

Enzyme and pathway databases

UniPathwayiUPA00204.
UPA00880.

Miscellaneous databases

PROiQ9QWE9.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer 344/N.
    Tissue: Trachea.

Entry informationi

Entry nameiGGT5_RAT
AccessioniPrimary (citable) accession number: Q9QWE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 84 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.