Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 82 (13 Feb 2019)
Sequence version 1 (07 Mar 2006)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Lysosomal acid glucosylceramidase

Gene

GBA

Organism
Bos taurus (Bovine)
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 transcript 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

Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramide/GlcCer into free ceramide and glucose. Thereby, plays a central role in the degradation of complex lipids and the turnover of cellular membranes. Through the production of ceramides, participates to the PKC-activated salvage pathway of ceramide formation. Also plays a role in cholesterol metabolism. May either catalyze the glucosylation of cholesterol, through a transglucosylation reaction that transfers glucose from glucosylceramide to cholesterol. The short chain saturated C8:0-GlcCer and the mono-unsaturated C18:0-GlcCer being the most effective glucose donors for that transglucosylation reaction. Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl-beta-D-glucoside to ceramide. Finally, may also hydrolyze cholesteryl-beta-D-glucoside to produce D-glucose and cholesterol.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 <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: cholesterol metabolism

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

Pathwayi: Sphingolipid metabolism

This protein is involved in Sphingolipid metabolism.By similarity
View all proteins of this organism that are known to be involved in Sphingolipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei274Proton donorBy similarity1
Active sitei379NucleophileBy 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 functionGlycosidase, Glycosyltransferase, Hydrolase, Transferase
Biological processCholesterol metabolism, Lipid metabolism, Sphingolipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00296

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH30 Glycoside Hydrolase Family 30

<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:
Lysosomal acid glucosylceramidaseCurated (EC:3.2.1.45By similarity)
Alternative name(s):
Acid beta-glucosidase
Beta-glucocerebrosidase
Cholesterol glucosyltransferaseBy similarity (EC:2.4.1.-By similarity)
Short name:
SGTaseBy similarity
Cholesteryl-beta-glucosidaseBy similarity (EC:3.2.1.104By similarity)
D-glucosyl-N-acylsphingosine glucohydrolase
<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:GBABy similarity
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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

<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

Keywords - Cellular componenti

Lysosome, 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
CHEMBL1275219

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 39By similarityAdd BLAST39
<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_000027864840 – 536Lysosomal acid glucosylceramidaseAdd BLAST497

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 bondi43 ↔ 55By similarity
Disulfide bondi57 ↔ 62By 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>Glycosylationi58N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi98N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi185N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi208N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi309N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi501N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q2KHZ8

PRoteomics IDEntifications database

More...
PRIDEi
Q2KHZ8

<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

Interacts with saposin-C. Interacts with SCARB2. Interacts with TCP1. Interacts with GRN; this interaction prevents aggregation of GBA-SCARB2 complex via interaction with HSPA1A upon stress (By similarity).By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000019765

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q2KHZ8

<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
Q2KHZ8

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

More...
SMRi
Q2KHZ8

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

<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 glycosyl hydrolase 30 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2566 Eukaryota
COG5520 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000270031

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG002285

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q2KHZ8

KEGG Orthology (KO)

More...
KOi
K01201

Database of Orthologous Groups

More...
OrthoDBi
644299at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1180, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR033452 GH30_C
IPR001139 Glyco_hydro_30
IPR033453 Glyco_hydro_30_TIM-barrel
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF

The PANTHER Classification System

More...
PANTHERi
PTHR11069 PTHR11069, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02055 Glyco_hydro_30, 1 hit
PF17189 Glyco_hydro_30C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00843 GLHYDRLASE30

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445 SSF51445, 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>Sequencei

<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.

Q2KHZ8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELSSPSREE YPMPRGRVGI MAASLMGLLL LHTVSWVSGA RPCSPKSFGY
60 70 80 90 100
SSVVCVCNGT YCDSLDPLTL PDPGTFSRFE STRSGRRMEL SLGTIQANRT
110 120 130 140 150
GTGLLLTLQP DQKFQKVKGF GGAMTDAAAL NILALSPAAR NLLLKSYFSE
160 170 180 190 200
EGIEYNIIRV PMASCDFSIR TYTYDDSPDD FQLLNFSLPE EDVKLKIPLI
210 220 230 240 250
HQALELANRS VSLFASPWTS PTWLKTNGAV NGKGTLKGQA GDLYHKTWAR
260 270 280 290 300
YFVKFLDAYA EHKLRFWAVT AENEPTAGLL TGYPFQCLGF TPEHQRDFIA
310 320 330 340 350
RDLGPILANS THRDVRLLML DDQRLLLPRW AQVVLADPEA AKYVHGIAVH
360 370 380 390 400
WYLDFLAPAK ATLGETHRLF PNTMLFASEA CVGSKFWEQS VRLGSWDRGM
410 420 430 440 450
RYSHSIITNL LYHVVGWTDW NLALNPEGGP NWVRNFVDSP IIVDIAKDTF
460 470 480 490 500
YKQPMFYHLG HFSKFIPEGS QRVGLVASKK SDLDTVALLR PDGSAVAVVL
510 520 530
NRSSKDVPLT IKDPAVGFME TVSPGYSIHT YLWRRQ
Length:536
Mass (Da):59,855
Last modified:March 7, 2006 - v1
<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:i1260A9C428E5D3FE
GO

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
BC112823 mRNA Translation: AAI12824.1

NCBI Reference Sequences

More...
RefSeqi
NP_001039886.1, NM_001046421.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Bt.5413

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
537087

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:537087

<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
BC112823 mRNA Translation: AAI12824.1
RefSeqiNP_001039886.1, NM_001046421.2
UniGeneiBt.5413

3D structure databases

ProteinModelPortaliQ2KHZ8
SMRiQ2KHZ8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019765

Chemistry databases

BindingDBiQ2KHZ8
ChEMBLiCHEMBL1275219

Protein family/group databases

CAZyiGH30 Glycoside Hydrolase Family 30

Proteomic databases

PaxDbiQ2KHZ8
PRIDEiQ2KHZ8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi537087
KEGGibta:537087

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2629

Phylogenomic databases

eggNOGiKOG2566 Eukaryota
COG5520 LUCA
HOGENOMiHOG000270031
HOVERGENiHBG002285
InParanoidiQ2KHZ8
KOiK01201
OrthoDBi644299at2759

Enzyme and pathway databases

UniPathwayi
UPA00296

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q2KHZ8

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR033452 GH30_C
IPR001139 Glyco_hydro_30
IPR033453 Glyco_hydro_30_TIM-barrel
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
PANTHERiPTHR11069 PTHR11069, 1 hit
PfamiView protein in Pfam
PF02055 Glyco_hydro_30, 1 hit
PF17189 Glyco_hydro_30C, 1 hit
PRINTSiPR00843 GLHYDRLASE30
SUPFAMiSSF51445 SSF51445, 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 nameiGLCM_BOVIN
<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: Q2KHZ8
<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: February 20, 2007
Last sequence update: March 7, 2006
Last modified: February 13, 2019
This is version 82 of the entry and version 1 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, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again