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Protein

Gamma-glutamyl hydrolase

Gene

Ggh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei133NucleophilePROSITE-ProRule annotation1
Active sitei243Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • 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

Keywordsi

Molecular functionHydrolase

Enzyme and pathway databases

BRENDAi3.4.19.9 5301
ReactomeiR-RNO-6798695 Neutrophil degranulation

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi2682 Ggh

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000002654125 – 317Gamma-glutamyl hydrolaseAdd BLAST293

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi46N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi100N-linked (GlcNAc...) asparagine; alternateSequence analysis1
Glycosylationi100N-linked (HexNAc...) asparagine; alternateCombined sources1
Glycosylationi153N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi162N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi188N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi202N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi306N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ62867
PRIDEiQ62867

PTM databases

iPTMnetiQ62867
PhosphoSitePlusiQ62867
UniCarbKBiQ62867

Expressioni

Gene expression databases

BgeeiENSRNOG00000007351
GenevisibleiQ62867 RN

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009758

Structurei

3D structure databases

ProteinModelPortaliQ62867
SMRiQ62867
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 317Gamma-glutamyl hydrolasePROSITE-ProRule annotationAdd BLAST293

Sequence similaritiesi

Belongs to the peptidase C26 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1559 Eukaryota
ENOG410XQKI LUCA
GeneTreeiENSGT00490000043388
HOGENOMiHOG000006721
HOVERGENiHBG005833
InParanoidiQ62867
KOiK01307
OMAiGILMQKC
OrthoDBiEOG091G0E82
PhylomeDBiQ62867
TreeFamiTF323437

Family and domain databases

Gene3Di3.40.50.880, 1 hit
InterProiView protein in InterPro
IPR029062 Class_I_gatase-like
IPR015527 Pept_C26_g-glut_hydrolase
IPR011697 Peptidase_C26
PANTHERiPTHR11315 PTHR11315, 1 hit
PfamiView protein in Pfam
PF07722 Peptidase_C26, 1 hit
SUPFAMiSSF52317 SSF52317, 1 hit
PROSITEiView protein in PROSITE
PS51275 PEPTIDASE_C26_GGH, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiGGH_RAT
AccessioniPrimary (citable) accession number: Q62867
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 127 of the entry and version 1 of the sequence. See 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

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