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Entry version 168 (23 Feb 2022)
Sequence version 4 (01 May 2007)
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Protein

Glutathione hydrolase 1 proenzyme

Gene

Ggt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates and other gamma-glutamyl compounds, such as leukotriene C4 (LTC4). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4.

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by autocatalytic cleavage.By similarity

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=5.9 µM for leukotriene C41 Publication
  2. KM=5.7 µM for glutathione1 Publication
  3. KM=5.8 µM for gamma-glutamyl-p-anilide1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glutathione metabolism

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei106GlutamateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei380NucleophileBy similarity1
Binding sitei419GlutamateBy similarity1
Binding sitei422GlutamateBy similarity1
Binding sitei473Glutamate; via amide nitrogenBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Hydrolase, Protease, Transferase
Biological processGlutathione biosynthesis
LigandSialic acid

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.2.2, 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-174403, Glutathione synthesis and recycling
R-RNO-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-RNO-5423646, Aflatoxin activation and detoxification

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00204

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glutathione hydrolase 1 proenzyme (EC:3.4.19.131 Publication)
Alternative name(s):
Gamma-glutamyltransferase 1
Gamma-glutamyltranspeptidase 1 (EC:2.3.2.21 Publication)
Short name:
GGT 1
Leukotriene-C4 hydrolase (EC:3.4.19.141 Publication)
CD_antigen: CD224
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ggt1
Synonyms:Ggt
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2683, Ggt1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 4Cytoplasmic1 Publication4
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei5 – 26Helical; Signal-anchor for type II membrane protein1 PublicationAdd BLAST22
Topological domaini27 – 568Extracellular1 PublicationAdd BLAST542

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2943

DrugCentral

More...
DrugCentrali
P07314

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000110641 – 379Glutathione hydrolase 1 heavy chainAdd BLAST379
ChainiPRO_0000011065380 – 568Glutathione hydrolase 1 light chain1 PublicationAdd BLAST189

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi49 ↔ 73By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi94N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi114N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi119N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi191 ↔ 195By similarity
Glycosylationi229N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi343N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi427N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi510N-linked (GlcNAc...) asparagineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated on both chains; contains sialic acid residues. It is not known if the sialic acid residues are present on N-linked or on O-linked glycans.1 Publication
O-glycosylated; close to the membrane anchor on the heavy chain and on the light chain. The sugar moieties are localized to the stretch Thr-28 to Ser-30. Contains sialic acid residues. It is not known if the sialic acid residues are present on N-linked or on O-linked glycans.1 Publication
Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P07314

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
170, 1 O-Linked glycan

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P07314, 8 sites, 2 N-linked glycans (1 site), 2 O-linked glycans (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07314

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P07314

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in adult kidney and mammary gland, and in fetal liver.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

By similarity

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P07314

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P07314

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni398 – 400Glutamate bindingBy similarity3
Regioni450 – 451Glutamate bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07314

Identification of Orthologs from Complete Genome Data

More...
OMAi
CYSIDAR

Database of Orthologous Groups

More...
OrthoDBi
1419292at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P07314

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.246.130, 1 hit
3.60.20.40, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR043138, GGT_lsub_C
IPR000101, GGT_peptidase
IPR043137, GGT_ssub
IPR029055, Ntn_hydrolases_N

The PANTHER Classification System

More...
PANTHERi
PTHR11686, PTHR11686, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56235, SSF56235, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00066, g_glut_trans, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00462, G_GLU_TRANSPEPTIDASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P07314-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKNRFLVLGL VAVVLVFVII GLCIWLPTTS GKPDHVYSRA AVATDAKRCS
60 70 80 90 100
EIGRDMLQEG GSVVDAAIAS LLCMGLINAH SMGIGGGLFF TIYNSTTRKA
110 120 130 140 150
EVINAREMAP RLANTSMFNN SKDSEEGGLS VAVPGEIRGY ELAHQRHGRL
160 170 180 190 200
PWARLFQPSI QLARHGFPVG KGLARALDKK RDIIEKTPAL CEVFCRQGKV
210 220 230 240 250
LQEGETVTMP KLADTLQILA QEGARAFYNG SLTAQIVKDI QEAGGIMTVE
260 270 280 290 300
DLNNYRAEVI EHPMSIGLGD STLYVPSAPL SGPVLILILN ILKGYNFSPK
310 320 330 340 350
SVATPEQKAL TYHRIVEAFR FAYAKRTMLG DPKFVDVSQV IRNMSSEFYA
360 370 380 390 400
TQLRARITDE TTHPTAYYEP EFYLPDDGGT AHLSVVSEDG SAVAATSTIN
410 420 430 440 450
LYFGSKVLSR VSGILFNDEM DDFSSPNFTN QFGVAPSPAN FIKPGKQPLS
460 470 480 490 500
SMCPSIIVDK DGKVRMVVGA SGGTQITTSV ALAIINSLWF GYDVKRAVEE
510 520 530 540 550
PRLHNQLLPN TTTVEKNIDQ VVTAGLKTRH HHTEVTPDFI AVVQAVVRTS
560
GGWAAASDSR KGGEPAGY
Length:568
Mass (Da):61,610
Last modified:May 1, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i24DC62A1DEEEA38C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0R8W8M0R8W8_RAT
Glutathione hydrolase 1 proenzyme
Ggt1
447Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1W2Q6L5A0A1W2Q6L5_RAT
Glutathione hydrolase 1 proenzyme
Ggt1
326Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1W2Q6N5A0A1W2Q6N5_RAT
Glutathione hydrolase 1 proenzyme
Ggt1
48Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA27224 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti9G → A in AAA41217 (PubMed:1671556).Curated1
Sequence conflicti39R → K in AAA57295 (PubMed:2869484).Curated1
Sequence conflicti39R → K in AAB59698 (PubMed:2869484).Curated1
Sequence conflicti111R → K in AAB59698 (PubMed:2869484).Curated1
Sequence conflicti370P → A in AAA57295 (PubMed:2869484).Curated1
Sequence conflicti370P → A in AAB59698 (PubMed:2869484).Curated1
Sequence conflicti370P → A in CAA27224 (PubMed:2869471).Curated1
Sequence conflicti397S → M in CAA27224 (PubMed:2869471).Curated1
Sequence conflicti416F → V in CAA27224 (PubMed:2869471).Curated1
Sequence conflicti444P → L in AAA57295 (PubMed:2869484).Curated1
Sequence conflicti444P → L in AAB59698 (PubMed:2869484).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X15443 mRNA Translation: CAA33483.1
M33821 mRNA Translation: AAA57295.1 Sequence problems.
M33822 mRNA Translation: AAB59698.1
BC078768 mRNA Translation: AAH78768.1
L29167 mRNA Translation: AAA41218.1
M57672 Genomic DNA Translation: AAA41217.1
X03518 mRNA Translation: CAA27224.1 Frameshift.

Protein sequence database of the Protein Information Resource

More...
PIRi
A05225

NCBI Reference Sequences

More...
RefSeqi
NP_446292.2, NM_053840.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
116568

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:116568

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15443 mRNA Translation: CAA33483.1
M33821 mRNA Translation: AAA57295.1 Sequence problems.
M33822 mRNA Translation: AAB59698.1
BC078768 mRNA Translation: AAH78768.1
L29167 mRNA Translation: AAA41218.1
M57672 Genomic DNA Translation: AAA41217.1
X03518 mRNA Translation: CAA27224.1 Frameshift.
PIRiA05225
RefSeqiNP_446292.2, NM_053840.2

3D structure databases

SMRiP07314
ModBaseiSearch...

Chemistry databases

BindingDBiP07314
ChEMBLiCHEMBL2943
DrugCentraliP07314

PTM databases

GlyConnecti170, 1 O-Linked glycan
GlyGeniP07314, 8 sites, 2 N-linked glycans (1 site), 2 O-linked glycans (1 site)
iPTMnetiP07314
PhosphoSitePlusiP07314

Proteomic databases

PRIDEiP07314

Genome annotation databases

GeneIDi116568
KEGGirno:116568

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2678
RGDi2683, Ggt1

Phylogenomic databases

InParanoidiP07314
OMAiCYSIDAR
OrthoDBi1419292at2759
PhylomeDBiP07314

Enzyme and pathway databases

UniPathwayiUPA00204
BRENDAi2.3.2.2, 5301
ReactomeiR-RNO-174403, Glutathione synthesis and recycling
R-RNO-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-RNO-5423646, Aflatoxin activation and detoxification

Miscellaneous databases

Protein Ontology

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PROi
PR:P07314

Family and domain databases

Gene3Di1.10.246.130, 1 hit
3.60.20.40, 1 hit
InterProiView protein in InterPro
IPR043138, GGT_lsub_C
IPR000101, GGT_peptidase
IPR043137, GGT_ssub
IPR029055, Ntn_hydrolases_N
PANTHERiPTHR11686, PTHR11686, 1 hit
SUPFAMiSSF56235, SSF56235, 1 hit
TIGRFAMsiTIGR00066, g_glut_trans, 1 hit
PROSITEiView protein in PROSITE
PS00462, G_GLU_TRANSPEPTIDASE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGGT1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07314
Secondary accession number(s): Q63217, Q63218, Q6AZ32
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: May 1, 2007
Last modified: February 23, 2022
This is version 168 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

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