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Protein

Gamma-glutamyl hydrolase

Gene

Ggh

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

Functioni

Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Exhibits either endo- or exopeptidase activity depending upon the tissue of origin. When secreted, it acts primarily as an endopeptidase.

Catalytic activityi

Hydrolysis of a gamma-glutamyl bond.

Enzyme regulationi

Activity is altered by insulin and estrogen.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei133 – 1331NucleophilePROSITE-ProRule annotation
Active sitei243 – 2431Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • glutamine metabolic process Source: InterPro
  • response to drug Source: RGD
  • response to ethanol Source: RGD
  • response to insulin Source: RGD
  • response to zinc ion Source: RGD
  • tetrahydrofolylpolyglutamate metabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.4.19.9. 5301.

Protein family/group databases

MEROPSiC26.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyl hydrolase (EC:3.4.19.9)
Alternative name(s):
Conjugase
GH
Gamma-Glu-X carboxypeptidase
Gene namesi
Name:Ggh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi2682. Ggh.

Subcellular locationi

  • Secretedextracellular space By similarity
  • Lysosome By similarity
  • Melanosome By similarity

  • Note: While its intracellular location is primarily the lysosome, most of the enzyme activity is secreted.By similarity

GO - Cellular componenti

  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • lysosome Source: RGD
  • melanosome Source: UniProtKB-SubCell
  • nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 317293Gamma-glutamyl hydrolasePRO_0000026541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence analysis
Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence analysis
Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence analysis
Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence analysis
Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence analysis
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence analysis
Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ62867.
PRIDEiQ62867.

PTM databases

iPTMnetiQ62867.
UniCarbKBiQ62867.

Expressioni

Gene expression databases

GenevisibleiQ62867. RN.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009758.

Structurei

3D structure databases

ProteinModelPortaliQ62867.
SMRiQ62867. Positions 25-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 317293Gamma-glutamyl hydrolasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C26 family.Curated
Contains 1 gamma-glutamyl hydrolase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1559. Eukaryota.
ENOG410XQKI. LUCA.
GeneTreeiENSGT00490000043388.
HOGENOMiHOG000006721.
HOVERGENiHBG005833.
InParanoidiQ62867.
KOiK01307.
OMAiNFTMNEK.
OrthoDBiEOG7BCNC9.
PhylomeDBiQ62867.
TreeFamiTF323437.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR015527. Pept_C26_g-glut_hydrolase.
IPR011697. Peptidase_C26.
[Graphical view]
PANTHERiPTHR11315. PTHR11315. 1 hit.
PfamiPF07722. Peptidase_C26. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
PROSITEiPS51275. PEPTIDASE_C26_GGH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q62867-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLGRLLCA WVLLLCGLAS PGLSGSYERG SKRPIIGIIM QECYGNMTKL
60 70 80 90 100
GRFYIAASYV KFIESAGARV VPIRLDLNDA QYETLFRSIN GVLLPGGGAN
110 120 130 140 150
LTHSGYSRVA KIFFTKALES FDNGDYFPVW GTCLGLEELS VLVSNDNLLT
160 170 180 190 200
LTNTSSVKLP LNFTRDSKQS RMFRNLPEEL LNSLASENLT ANFHKWSLSV
210 220 230 240 250
KNFTENEKLK KFFNILTVNT DGKTEFISSM EGYKYPIYAV QWHPEKAPFE
260 270 280 290 300
WKKLRGISHA PNAVKTSFYL AKFFISEALK NDHHFENELE ETESLIYQFC
310
PVYTGNISSF QQAYMFN
Length:317
Mass (Da):35,830
Last modified:November 1, 1996 - v1
Checksum:iCB8D2499374CAEAF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38379 mRNA. Translation: AAC52506.1.
BC087602 mRNA. Translation: AAH87602.1.
RefSeqiNP_037092.1. NM_012960.2.
UniGeneiRn.10260.

Genome annotation databases

EnsembliENSRNOT00000009758; ENSRNOP00000009758; ENSRNOG00000007351.
GeneIDi25455.
KEGGirno:25455.
UCSCiRGD:2682. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38379 mRNA. Translation: AAC52506.1.
BC087602 mRNA. Translation: AAH87602.1.
RefSeqiNP_037092.1. NM_012960.2.
UniGeneiRn.10260.

3D structure databases

ProteinModelPortaliQ62867.
SMRiQ62867. Positions 25-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009758.

Protein family/group databases

MEROPSiC26.001.

PTM databases

iPTMnetiQ62867.
UniCarbKBiQ62867.

Proteomic databases

PaxDbiQ62867.
PRIDEiQ62867.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009758; ENSRNOP00000009758; ENSRNOG00000007351.
GeneIDi25455.
KEGGirno:25455.
UCSCiRGD:2682. rat.

Organism-specific databases

CTDi8836.
RGDi2682. Ggh.

Phylogenomic databases

eggNOGiKOG1559. Eukaryota.
ENOG410XQKI. LUCA.
GeneTreeiENSGT00490000043388.
HOGENOMiHOG000006721.
HOVERGENiHBG005833.
InParanoidiQ62867.
KOiK01307.
OMAiNFTMNEK.
OrthoDBiEOG7BCNC9.
PhylomeDBiQ62867.
TreeFamiTF323437.

Enzyme and pathway databases

BRENDAi3.4.19.9. 5301.

Miscellaneous databases

PROiQ62867.

Gene expression databases

GenevisibleiQ62867. RN.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR015527. Pept_C26_g-glut_hydrolase.
IPR011697. Peptidase_C26.
[Graphical view]
PANTHERiPTHR11315. PTHR11315. 1 hit.
PfamiPF07722. Peptidase_C26. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
PROSITEiPS51275. PEPTIDASE_C26_GGH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, cloning, and sequencing of a cDNA coding for rat gamma-glutamyl hydrolase."
    Yao R., Nimec Z., Ryan T.J., Galivan J.
    J. Biol. Chem. 271:8525-8528(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-39; 173-182 AND 231-240.
    Tissue: Hepatocyte.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "The properties of the secreted gamma-glutamyl hydrolases from H35 hepatoma cells."
    Wang Y., Nimec Z., Ryan T.J., Dias J.A., Galivan J.
    Biochim. Biophys. Acta 1164:227-235(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Tissue: Hepatocyte.

Entry informationi

Entry nameiGGH_RAT
AccessioniPrimary (citable) accession number: Q62867
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 114 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, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  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.