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UniProtKB - P07314 (GGT1_RAT)

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. The metabolism of glutathione 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. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 ‘Function’ 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_section">'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.
    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 ‘Function’ 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 ‘Function’ 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 sitei398GlutamateBy similarity1
    Binding sitei419GlutamateBy 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

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    <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

    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_and_taxonomy_section">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:
    Glutathione hydrolase 1 heavy chain
    Glutathione hydrolase 1 light chain
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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

    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

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 – 4CytoplasmicSequence analysis4
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 proteinCuratedAdd BLAST22
    Topological domaini27 – 568ExtracellularSequence analysisAdd 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

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000110641 – 379Glutathione hydrolase 1 heavy chainAdd BLAST379
    ChainiPRO_0000011065380 – 568Glutathione hydrolase 1 light chainAdd 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_processing_section">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_processing_section">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

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P07314

    PRoteomics IDEntifications database

    More...    PRIDEi    		P07314

    PTM databases

    GlyConnect protein glycosylation platform

    More...    GlyConnecti    		170

    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

    UniCarbKB; an annotated and curated database of glycan structures

    More...    UniCarbKBi    		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.

    <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_section">'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_section">'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.

    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

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		P07314

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

    More...    SMRi    		P07314

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		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>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

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...    HOVERGENi    		HBG005835

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P07314

    KEGG Orthology (KO)

    More...    KOi    		K18592

    Database of Orthologous Groups

    More...    OrthoDBi    		1419292at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P07314

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR000101 GGT_peptidase
    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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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: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>
    A0A1W2Q6L5A0A1W2Q6L5_RAT
    Glutathione hydrolase 1 proenzyme
    Ggt1
    		326Annotation 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>
    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 at positions 66 and 134.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

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Rn.10010

    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
    UniGeneiRn.10010

    3D structure databases

    ProteinModelPortaliP07314
    SMRiP07314
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    BindingDBiP07314
    ChEMBLiCHEMBL2943

    PTM databases

    GlyConnecti170
    iPTMnetiP07314
    PhosphoSitePlusiP07314
    UniCarbKBiP07314

    Proteomic databases

    jPOSTiP07314
    PRIDEiP07314

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi116568
    KEGGirno:116568

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		2678
    RGDi2683 Ggt1

    Phylogenomic databases

    HOVERGENiHBG005835
    InParanoidiP07314
    KOiK18592
    OrthoDBi1419292at2759
    PhylomeDBiP07314

    Enzyme and pathway databases

    UniPathwayi
    UPA00204

    BRENDAi2.3.2.2 5301

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P07314

    Family and domain databases

    InterProiView protein in InterPro
    IPR000101 GGT_peptidase
    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    <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_and_isoforms">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: January 16, 2019
    This is version 153 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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