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Protein

Alpha-N-acetylgalactosaminidase

Gene

Naga

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei154SubstrateBy similarity1
Active sitei156NucleophileBy similarity1
Binding sitei188SubstrateBy similarity1
Binding sitei213SubstrateBy similarity1
Active sitei217Proton donorBy similarity1
Binding sitei217SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi1306025 Naga

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17By similarityAdd BLAST17
ChainiPRO_000000102018 – 415Alpha-N-acetylgalactosaminidaseAdd BLAST398

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi38 ↔ 80By similarity
Disulfide bondi42 ↔ 49By similarity
Disulfide bondi127 ↔ 158By similarity
Glycosylationi177N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi187 ↔ 209By similarity
Glycosylationi201N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei322PhosphoserineBy similarity1
Glycosylationi330N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei332PhosphoserineBy similarity1
Glycosylationi385N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi391N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ66H12
PRIDEiQ66H12

Expressioni

Gene expression databases

BgeeiENSRNOG00000008064
GenevisibleiQ66H12 RN

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ66H12, 1 interactor
STRINGi10116.ENSRNOP00000060590

Structurei

3D structure databases

ProteinModelPortaliQ66H12
SMRiQ66H12
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni78 – 79Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 27 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2366 Eukaryota
ENOG410XPF1 LUCA
GeneTreeiENSGT00390000008751
HOGENOMiHOG000161224
HOVERGENiHBG001989
InParanoidiQ66H12
KOiK01204
OMAiDDLWDRW
OrthoDBiEOG091G0BGV
PhylomeDBiQ66H12
TreeFamiTF312909

Family and domain databases

CDDicd14792 GH27, 1 hit
Gene3Di2.60.40.1180, 1 hit
3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR002241 Glyco_hydro_27
IPR000111 Glyco_hydro_27/36_CS
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR035373 Melibiase/NAGA_C
PfamiView protein in Pfam
PF16499 Melibiase_2, 1 hit
PF17450 Melibiase_2_C, 1 hit
PRINTSiPR00740 GLHYDRLASE27
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00512 ALPHA_GALACTOSIDASE, 1 hit

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_006242087.3
XP_006242150.1, XM_006242088.3
UniGeneiRn.55746

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiNAGAB_RAT
AccessioniPrimary (citable) accession number: Q66H12
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 11, 2004
Last modified: May 23, 2018
This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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