P17050 · NAGAB_HUMAN
- ProteinAlpha-N-acetylgalactosaminidase
- GeneNAGA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids411 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides. Required for the breakdown of glycolipids.
Miscellaneous
Alpha-galactosidase B was first found to be an isoenzyme of alpha-galactosidases, but apparently it differs from alpha-galactosidase A in substrate specificity and is alpha-N-acetylgalactosaminidase.
Catalytic activity
- a neolactoside IV3-alpha-GalNAc,IV2-alpha-Fuc-nLc4Cer(d18:1(4E)) + H2O = a neolactoside IV2-alpha-Fuc-nLc4Cer(d18:1(4E)) + N-acetyl-alpha-D-galactosamineThis reaction proceeds in the forward direction.
- a neolactoside IV3-alpha-GalNAc,IV2-alpha-Fuc-nLc4Cer(d18:0) + H2O = a neolactoside IV2-alpha-Fuc-nLc4Cer(d18:0) + N-acetyl-alpha-D-galactosamineThis reaction proceeds in the forward direction.
- a globoside IV3GalNAc-Gb4Cer + H2O = a globoside Gb4Cer + N-acetyl-alpha-D-galactosamineThis reaction proceeds in the forward direction.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 78-79 | substrate | ||||
Sequence: DD | ||||||
Binding site | 154 | substrate | ||||
Sequence: K | ||||||
Active site | 156 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 188 | substrate | ||||
Sequence: S | ||||||
Binding site | 213 | substrate | ||||
Sequence: R | ||||||
Active site | 217 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 217 | substrate | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular exosome | |
Cellular Component | lysosome | |
Molecular Function | alpha-galactosidase activity | |
Molecular Function | alpha-N-acetylgalactosaminidase activity | |
Molecular Function | protein homodimerization activity | |
Biological Process | carbohydrate catabolic process | |
Biological Process | glycolipid catabolic process | |
Biological Process | glycoside catabolic process | |
Biological Process | oligosaccharide metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameAlpha-N-acetylgalactosaminidase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP17050
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Schindler disease (SCHIND)
- Note
- DescriptionForm of NAGA deficiency characterized by early-onset neuroaxonal dystrophy and neurological signs (convulsion during fever, epilepsy, psychomotor retardation and hypotonia). NAGA deficiency is typically classified in three main phenotypes: NAGA deficiency type I (Schindler disease or Schindler disease type I) with severe manifestations; NAGA deficiency type II (Kanzazi disease or Schindler disease type II) which is mild; NAGA deficiency type III (Schindler disease type III) characterized by mild-to-moderate neurologic manifestations. NAGA deficiency results in the increased urinary excretion of glycopeptides and oligosaccharides containing alpha-N-acetylgalactosaminyl moieties. Inheritance is autosomal recessive.
- See alsoMIM:609241
Natural variants in SCHIND
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_000496 | 160 | S>C | in SCHIND; type III; dbSNP:rs121434532 | |
VAR_000497 | 325 | E>K | in SCHIND; type I and type III; dbSNP:rs121434529 |
Kanzaki disease (KANZD)
- Note
- DescriptionAutosomal recessive disorder characterized by late-onset, angiokeratoma corporis diffusum and mild intellectual impairment.
- See alsoMIM:609242
Natural variants in KANZD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_022525 | 329 | R>Q | in KANZD; dbSNP:rs121434533 | |
VAR_000498 | 329 | R>W | in KANZD; loss of activity; dbSNP:rs121434530 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_000496 | 160 | in SCHIND; type III; dbSNP:rs121434532 | |||
Sequence: S → C | ||||||
Mutagenesis | 201 | Loss of glycosylation site; no effect on enzyme activity and stability. | ||||
Sequence: N → Q | ||||||
Natural variant | VAR_000497 | 325 | in SCHIND; type I and type III; dbSNP:rs121434529 | |||
Sequence: E → K | ||||||
Natural variant | VAR_022525 | 329 | in KANZD; dbSNP:rs121434533 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_000498 | 329 | in KANZD; loss of activity; dbSNP:rs121434530 | |||
Sequence: R → W |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 538 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MLLKTVLLLGHVAQVLM | ||||||
Chain | PRO_0000001018 | 18-411 | Alpha-N-acetylgalactosaminidase | |||
Sequence: LDNGLLQTPPMGWLAWERFRCNINCDEDPKNCISEQLFMEMADRMAQDGWRDMGYTYLNIDDCWIGGRDASGRLMPDPKRFPHGIPFLADYVHSLGLKLGIYADMGNFTCMGYPGTTLDKVVQDAQTFAEWKVDMLKLDGCFSTPEERAQGYPKMAAALNATGRPIAFSCSWPAYEGGLPPRVNYSLLADICNLWRNYDDIQDSWWSVLSILNWFVEHQDILQPVAGPGHWNDPDMLLIGNFGLSLEQSRAQMALWTVLAAPLLMSTDLRTISAQNMDILQNPLMIKINQDPLGIQGRRIHKEKSLIEVYMRPLSNKASALVFFSCRTDMPYRYHSSLGQLNFTGSVIYEAQDVYSGDIISGLRDETNFTVIINPSGVVMWYLYPIKNLEMSQQ | ||||||
Disulfide bond | 38↔80 | |||||
Sequence: CNINCDEDPKNCISEQLFMEMADRMAQDGWRDMGYTYLNIDDC | ||||||
Disulfide bond | 42↔49 | |||||
Sequence: CDEDPKNC | ||||||
Glycosylation | 124 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 127↔158 | |||||
Sequence: CMGYPGTTLDKVVQDAQTFAEWKVDMLKLDGC | ||||||
Glycosylation | 177 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 187↔209 | |||||
Sequence: CSWPAYEGGLPPRVNYSLLADIC | ||||||
Glycosylation | 201 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 322 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 332 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 359 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 385 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length411
- Mass (Da)46,565
- Last updated1992-03-01 v2
- Checksum781A0728C0B29CD9
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 24 | in Ref. 8; AA sequence | ||||
Sequence: Q → N | ||||||
Sequence conflict | 165 | in Ref. 2; AAA59902 | ||||
Sequence: R → A | ||||||
Sequence conflict | 175 | in Ref. 2; AAA59902 | ||||
Sequence: A → G | ||||||
Sequence conflict | 205 | in Ref. 2; AAA59902 | ||||
Sequence: L → Q |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M62783 EMBL· GenBank· DDBJ | AAA51677.1 EMBL· GenBank· DDBJ | mRNA | ||
M59199 EMBL· GenBank· DDBJ | AAB06718.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M29276 EMBL· GenBank· DDBJ | AAA59902.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
M38083 EMBL· GenBank· DDBJ | AAA36351.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456527 EMBL· GenBank· DDBJ | CAG30413.1 EMBL· GenBank· DDBJ | mRNA | ||
Z99716 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC000095 EMBL· GenBank· DDBJ | AAH00095.1 EMBL· GenBank· DDBJ | mRNA |