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Q9Z0L8

- GGH_MOUSE

UniProt

Q9Z0L8 - GGH_MOUSE

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Protein

Gamma-glutamyl hydrolase

Gene

Ggh

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. Acts as endopeptidase. Lysosomal enzyme is activated by sulfhydryl compounds.

Catalytic activityi

Hydrolysis of a gamma-glutamyl bond.

pH dependencei

Optimum pH is 4. Active from pH 3 to 5.

Sites

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

GO - Molecular functioni

  1. gamma-glutamyl-peptidase activity Source: UniProtKB

GO - Biological processi

  1. glutamine metabolic process Source: InterPro
  2. proteolysis Source: GOC
  3. response to drug Source: Ensembl
  4. response to ethanol Source: Ensembl
  5. response to insulin Source: Ensembl
  6. response to zinc ion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

MEROPSiC26.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyl hydrolase (EC:3.4.19.9)
Alternative name(s):
Conjugase
FGPH
Folylpolyglutamate hydrolase
GH
Gamma-Glu-x carboxypeptidase
Gene namesi
Name:Ggh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1329035. 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

  1. cytosol Source: Ensembl
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. lysosome Source: MGI
  5. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424By similarityAdd
BLAST
Chaini25 – 317293Gamma-glutamyl hydrolasePRO_0000026540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi100 – 1001N-linked (GlcNAc...) (high mannose)1 Publication
Glycosylationi162 – 1621N-linked (GlcNAc...) (high mannose)1 Publication
Glycosylationi188 – 1881N-linked (GlcNAc...) (high mannose)1 Publication
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9Z0L8.
PaxDbiQ9Z0L8.
PRIDEiQ9Z0L8.

PTM databases

PhosphoSiteiQ9Z0L8.

Expressioni

Tissue specificityi

Isoform I (more expressed than isoform II in all tissues) is highly expressed in salivary gland, followed by kidney, liver, lung, stomach and uterus, and weakly expressed in small intestine, brain and fetal liver. Also expressed at a lower level in thymus, spleen and skeletal muscle. Also expressed in tumors.

Gene expression databases

BgeeiQ9Z0L8.
CleanExiMM_GGH.
GenevestigatoriQ9Z0L8.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9Z0L8.
SMRiQ9Z0L8. Positions 30-317.
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

eggNOGiNOG251450.
GeneTreeiENSGT00490000043388.
HOGENOMiHOG000006721.
HOVERGENiHBG005833.
InParanoidiQ9Z0L8.
KOiK01307.
OMAiNFTMNEK.
OrthoDBiEOG7BCNC9.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform I (identifier: Q9Z0L8-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MANLGYLLCL LGLLLCGLSS PGMSRPYNHG SERPIIGVVM QECFGKMAKL
60 70 80 90 100
GNYYIAASYV KYIESAGARV VPIRPDLSDA EYEELFRSIN GVLLPGGGAN
110 120 130 140 150
LTDSGYSRVA KIFFSKALES FDNGDHFPVW GTCLGFEELS VLVSGENLLT
160 170 180 190 200
STDTKSKKLP LNFTEGARKS RMFKHFPTEL LDSLALENLT ANFHKWSLSV
210 220 230 240 250
KNFTENEKLK KFFNILTTNT DGKTEFISSM EGFKYPVYAV QWHPEKAAFE
260 270 280 290 300
WKNLGGISHA PNAVKTSFYL AEFLVSEARK NSHHFENVVK ETASLIYKFN
310
PIYTGNISSF QQAYMFD
Length:317
Mass (Da):35,470
Last modified:July 27, 2011 - v2
Checksum:i139F56E1EFE6F801
GO
Isoform II (identifier: Q9Z0L8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MANLGYLLCLLGLLLC → MVRGWRLLGVLMLS

Show »
Length:315
Mass (Da):35,377
Checksum:i331F7F9C9D2A9B62
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251D → G in AAC70002. (PubMed:9756990)Curated
Sequence conflicti125 – 1251D → G in AAC70003. (PubMed:9756990)Curated
Sequence conflicti125 – 1251D → G in AAD47388. (PubMed:10393243)Curated
Sequence conflicti170 – 1712SR → NK in AAC70002. (PubMed:9756990)Curated
Sequence conflicti170 – 1712SR → NK in AAC70003. (PubMed:9756990)Curated
Sequence conflicti170 – 1712SR → NK in AAD47388. (PubMed:10393243)Curated
Sequence conflicti248 – 2481A → P in AAC70002. (PubMed:9756990)Curated
Sequence conflicti248 – 2481A → P in AAC70003. (PubMed:9756990)Curated
Sequence conflicti248 – 2481A → P in AAD47388. (PubMed:10393243)Curated
Sequence conflicti299 – 3002FN → VY in AAC70002. (PubMed:9756990)Curated
Sequence conflicti299 – 3002FN → VY in AAC70003. (PubMed:9756990)Curated
Sequence conflicti299 – 3002FN → VY in AAD47388. (PubMed:10393243)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1616MANLG…GLLLC → MVRGWRLLGVLMLS in isoform II. CuratedVSP_005447Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF051102 mRNA. Translation: AAC70002.1.
AF051103 mRNA. Translation: AAC70003.1.
AF090732
, AF090725, AF090726, AF090727, AF090728, AF090729, AF090730, AF090731 Genomic DNA. Translation: AAD47388.1.
AL732527, CR931798 Genomic DNA. Translation: CAM18838.2.
CR931798, AL732527 Genomic DNA. Translation: CAO78172.1.
CCDSiCCDS51126.1. [Q9Z0L8-1]
RefSeqiNP_034411.2. NM_010281.2. [Q9Z0L8-1]
UniGeneiMm.20461.

Genome annotation databases

EnsembliENSMUST00000098242; ENSMUSP00000095843; ENSMUSG00000073987. [Q9Z0L8-1]
GeneIDi14590.
KEGGimmu:14590.
UCSCiuc008sck.1. mouse. [Q9Z0L8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF051102 mRNA. Translation: AAC70002.1 .
AF051103 mRNA. Translation: AAC70003.1 .
AF090732
, AF090725 , AF090726 , AF090727 , AF090728 , AF090729 , AF090730 , AF090731 Genomic DNA. Translation: AAD47388.1 .
AL732527 , CR931798 Genomic DNA. Translation: CAM18838.2 .
CR931798 , AL732527 Genomic DNA. Translation: CAO78172.1 .
CCDSi CCDS51126.1. [Q9Z0L8-1 ]
RefSeqi NP_034411.2. NM_010281.2. [Q9Z0L8-1 ]
UniGenei Mm.20461.

3D structure databases

ProteinModelPortali Q9Z0L8.
SMRi Q9Z0L8. Positions 30-317.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C26.001.

PTM databases

PhosphoSitei Q9Z0L8.

Proteomic databases

MaxQBi Q9Z0L8.
PaxDbi Q9Z0L8.
PRIDEi Q9Z0L8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000098242 ; ENSMUSP00000095843 ; ENSMUSG00000073987 . [Q9Z0L8-1 ]
GeneIDi 14590.
KEGGi mmu:14590.
UCSCi uc008sck.1. mouse. [Q9Z0L8-1 ]

Organism-specific databases

CTDi 8836.
MGIi MGI:1329035. Ggh.

Phylogenomic databases

eggNOGi NOG251450.
GeneTreei ENSGT00490000043388.
HOGENOMi HOG000006721.
HOVERGENi HBG005833.
InParanoidi Q9Z0L8.
KOi K01307.
OMAi NFTMNEK.
OrthoDBi EOG7BCNC9.
TreeFami TF323437.

Miscellaneous databases

ChiTaRSi GGH. mouse.
NextBioi 286342.
PROi Q9Z0L8.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z0L8.
CleanExi MM_GGH.
Genevestigatori Q9Z0L8.

Family and domain databases

Gene3Di 3.40.50.880. 1 hit.
InterProi IPR029062. Class_I_gatase-like.
IPR015527. Pept_C26_g-glut_hydrolase.
IPR011697. Peptidase_C26.
[Graphical view ]
PANTHERi PTHR11315. PTHR11315. 1 hit.
Pfami PF07722. Peptidase_C26. 1 hit.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
PROSITEi PS51275. PEPTIDASE_C26_GGH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of mouse gamma-glutamyl hydrolase in the form of two cDNA variants with different 5' ends and encoding alternate leader peptide sequences."
    Esaki T., Roy K., Yao R., Galivan J., Sirotnak F.M.
    Gene 219:37-44(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Strain: 129/SvJ and BALB/c.
    Tissue: Liver.
  2. "Organization and structure of the mouse gamma-glutamyl hydrolase gene and the functional identification of its promoter."
    Esaki T., Masumoto N., Hayes P., Chen J., Sirotnak F.M.
    Gene 234:93-100(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis."
    Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K., Nishimura S.
    Mol. Cell. Proteomics 4:1977-1989(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-100; ASN-162 AND ASN-188.
    Tissue: Epidermis.

Entry informationi

Entry nameiGGH_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0L8
Secondary accession number(s): B1AWC1, Q9Z0L7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 111 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3