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Protein

Alpha-N-acetylgalactosaminidase

Gene

Naga

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides. Required for the breakdown of glycolipids (By similarity).By similarity

Catalytic activityi

Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei154 – 1541SubstrateBy similarity
Active sitei156 – 1561NucleophileBy similarity
Binding sitei188 – 1881SubstrateBy similarity
Binding sitei213 – 2131SubstrateBy similarity
Active sitei217 – 2171Proton donorBy similarity
Binding sitei217 – 2171SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-N-acetylgalactosaminidase (EC:3.2.1.49)
Alternative name(s):
Alpha-galactosidase B
Gene namesi
Name:Naga
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi1306025. Naga.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717By similarityAdd
BLAST
Chaini18 – 415398Alpha-N-acetylgalactosaminidasePRO_0000001020Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi38 ↔ 80By similarity
Disulfide bondi42 ↔ 49By similarity
Disulfide bondi127 ↔ 158By similarity
Glycosylationi177 – 1771N-linked (GlcNAc...)By similarity
Disulfide bondi187 ↔ 209By similarity
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
Modified residuei322 – 3221PhosphoserineBy similarity
Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence Analysis
Modified residuei332 – 3321PhosphoserineBy similarity
Glycosylationi385 – 3851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ66H12.
PRIDEiQ66H12.

Expressioni

Gene expression databases

GenevisibleiQ66H12. RN.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ66H12. 1 interaction.
STRINGi10116.ENSRNOP00000060590.

Structurei

3D structure databases

ProteinModelPortaliQ66H12.
SMRiQ66H12. Positions 18-402.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni78 – 792Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 27 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG68897.
GeneTreeiENSGT00390000008751.
HOGENOMiHOG000161224.
HOVERGENiHBG001989.
InParanoidiQ66H12.
KOiK01204.
OMAiFMEMADH.
OrthoDBiEOG7F24SV.
PhylomeDBiQ66H12.
TreeFamiTF312909.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02065. Melibiase. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q66H12-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQKTVLLLA LVAQVLMLEN GLLRTPPMGW LAWERFRCNI NCEEDPKNCI
60 70 80 90 100
SERLFMEMAD RLAQDGWRDL GYVYLNIDDC WIGGRDATGR LIPDPKRFPH
110 120 130 140 150
GIAFLADYAH SLGLKLGIYE DMGKMTCMGY PGTTLDKVEL DAATFAEWKV
160 170 180 190 200
DMLKLDGCYS TPKERAEGYP KMAAALNATG RPIAFSCSWP AYEGGLPPKV
210 220 230 240 250
NYTEVAGTCN LWRNYKDIQD SWKSVLSILD WFVKHQDILQ PVSGPGHWND
260 270 280 290 300
PDMLLIGNFG LSFDESRAQM ALWTVLAAPL FMSTDLRTIS PQNIDILQNP
310 320 330 340 350
LLIKINQDPL GIQGRLIFKS KSHIEVFKRN LSDDASALVF FSRRTDMPYH
360 370 380 390 400
FHCSLLELNY PKGSVYEGQN VFTGDIISGL HPETNFTVII NPSGVVMWYL
410
YPVKGLGIYT MMSQL
Length:415
Mass (Da):46,871
Last modified:October 11, 2004 - v1
Checksum:i57605634B3F74C6E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC082084 mRNA. Translation: AAH82084.1.
RefSeqiNP_001012120.1. NM_001012120.1.
XP_006242149.1. XM_006242087.2.
XP_006242150.1. XM_006242088.2.
UniGeneiRn.55746.

Genome annotation databases

EnsembliENSRNOT00000068020; ENSRNOP00000060590; ENSRNOG00000008064.
GeneIDi315165.
KEGGirno:315165.
UCSCiRGD:1306025. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC082084 mRNA. Translation: AAH82084.1.
RefSeqiNP_001012120.1. NM_001012120.1.
XP_006242149.1. XM_006242087.2.
XP_006242150.1. XM_006242088.2.
UniGeneiRn.55746.

3D structure databases

ProteinModelPortaliQ66H12.
SMRiQ66H12. Positions 18-402.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ66H12. 1 interaction.
STRINGi10116.ENSRNOP00000060590.

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.

Proteomic databases

PaxDbiQ66H12.
PRIDEiQ66H12.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000068020; ENSRNOP00000060590; ENSRNOG00000008064.
GeneIDi315165.
KEGGirno:315165.
UCSCiRGD:1306025. rat.

Organism-specific databases

CTDi4668.
RGDi1306025. Naga.

Phylogenomic databases

eggNOGiNOG68897.
GeneTreeiENSGT00390000008751.
HOGENOMiHOG000161224.
HOVERGENiHBG001989.
InParanoidiQ66H12.
KOiK01204.
OMAiFMEMADH.
OrthoDBiEOG7F24SV.
PhylomeDBiQ66H12.
TreeFamiTF312909.

Miscellaneous databases

NextBioi668806.
PROiQ66H12.

Gene expression databases

GenevisibleiQ66H12. RN.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02065. Melibiase. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiNAGAB_RAT
AccessioniPrimary (citable) accession number: Q66H12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 11, 2004
Last modified: June 24, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.