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Protein

Alpha-N-acetylgalactosaminidase

Gene

Naga

Organism
Mus musculus (Mouse)
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

Enzyme and pathway databases

BRENDAi3.2.1.49. 3474.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1261422. 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_0000001019Add
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...)Sequence Analysis
Disulfide bondi187 ↔ 209By similarity
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
Modified residuei322 – 3221PhosphoserineBy similarity
Modified residuei332 – 3321PhosphoserineBy similarity
Glycosylationi385 – 3851N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9QWR8.
PaxDbiQ9QWR8.
PRIDEiQ9QWR8.

PTM databases

PhosphoSiteiQ9QWR8.

Expressioni

Gene expression databases

BgeeiQ9QWR8.
CleanExiMM_NAGA.
GenevisibleiQ9QWR8. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9QWR8. 1 interaction.
MINTiMINT-1849631.
STRINGi10090.ENSMUSP00000023088.

Structurei

3D structure databases

ProteinModelPortaliQ9QWR8.
SMRiQ9QWR8. Positions 18-404.
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.
InParanoidiQ9QWR8.
KOiK01204.
OMAiALWTIFA.
OrthoDBiEOG7F24SV.
PhylomeDBiQ9QWR8.
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.

Q9QWR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQKTVLLLA LVAQVLMLEN GLLRTPPMGW LAWERFRCNI DCVEDPKNCI
60 70 80 90 100
SERLFMEMAD RLAQDGWRDL GYVYLNIDDC WIGGRDASGR LIPDPKRFPH
110 120 130 140 150
GIAFLADYAH SLGLKLGIYE DMGKMTCMGY PGTTLDKVEL DAETFAEWKV
160 170 180 190 200
DMLKLDGCFS SSRERAEGYP KMAAALNATG RPIAFSCSWP AYEGGLPPKV
210 220 230 240 250
NYTEVSRVCN LWRNYKDIQD SWKSVLSILD WFVRHQDVLQ PVAGPGHWND
260 270 280 290 300
PDMLLIGNFG LSFDESRAQM ALWTVLAAPL LMSTDLRTIS PQNMDILQNP
310 320 330 340 350
LMIKINQDPL GIQGRRILKS KSHIEVFKRY LSNQASALVF FSRRTDMPFR
360 370 380 390 400
FHCSLLELNY PKGRVYEGQN VFTGDIFSGL QTEVNFTVII NPSGVVMWYL
410
YPIKDLGIST MMSHW
Length:415
Mass (Da):47,235
Last modified:June 7, 2005 - v2
Checksum:i8BBA9BE03E1350C8
GO

Sequence cautioni

The sequence AAL87527.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 532ER → DG in CAA11703 (PubMed:9602128).Curated
Sequence conflicti239 – 2391L → P in AAH21631 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079458 mRNA. Translation: AAC28851.1.
AJ223966 Genomic DNA. Translation: CAA11703.1.
AY079439 Genomic DNA. Translation: AAL87527.1. Different initiation.
AY079440 Genomic DNA. Translation: AAL87528.1.
AK077116 mRNA. Translation: BAC36620.1.
BC021631 mRNA. Translation: AAH21631.1.
CCDSiCCDS27686.1.
RefSeqiNP_032695.3. NM_008669.4.
UniGeneiMm.20325.

Genome annotation databases

EnsembliENSMUST00000023088; ENSMUSP00000023088; ENSMUSG00000022453.
GeneIDi17939.
KEGGimmu:17939.
UCSCiuc007wyw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079458 mRNA. Translation: AAC28851.1.
AJ223966 Genomic DNA. Translation: CAA11703.1.
AY079439 Genomic DNA. Translation: AAL87527.1. Different initiation.
AY079440 Genomic DNA. Translation: AAL87528.1.
AK077116 mRNA. Translation: BAC36620.1.
BC021631 mRNA. Translation: AAH21631.1.
CCDSiCCDS27686.1.
RefSeqiNP_032695.3. NM_008669.4.
UniGeneiMm.20325.

3D structure databases

ProteinModelPortaliQ9QWR8.
SMRiQ9QWR8. Positions 18-404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QWR8. 1 interaction.
MINTiMINT-1849631.
STRINGi10090.ENSMUSP00000023088.

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.

PTM databases

PhosphoSiteiQ9QWR8.

Proteomic databases

MaxQBiQ9QWR8.
PaxDbiQ9QWR8.
PRIDEiQ9QWR8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023088; ENSMUSP00000023088; ENSMUSG00000022453.
GeneIDi17939.
KEGGimmu:17939.
UCSCiuc007wyw.2. mouse.

Organism-specific databases

CTDi4668.
MGIiMGI:1261422. Naga.

Phylogenomic databases

eggNOGiNOG68897.
GeneTreeiENSGT00390000008751.
HOGENOMiHOG000161224.
HOVERGENiHBG001989.
InParanoidiQ9QWR8.
KOiK01204.
OMAiALWTIFA.
OrthoDBiEOG7F24SV.
PhylomeDBiQ9QWR8.
TreeFamiTF312909.

Enzyme and pathway databases

BRENDAi3.2.1.49. 3474.

Miscellaneous databases

NextBioi292845.
PROiQ9QWR8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QWR8.
CleanExiMM_NAGA.
GenevisibleiQ9QWR8. MM.

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

« Hide 'large scale' publications
  1. "Murine alpha-N-acetylgalactosaminidase: isolation and expression of a full-length cDNA and genomic organization: further evidence of an alpha-galactosidase gene family."
    Wang A.M., Ioannou Y.A., Zeidner K.M., Desnick R.J.
    Mol. Genet. Metab. 65:165-173(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning, structural organization, sequence, chromosomal assignment, and expression of the mouse alpha-N-acetylgalactosaminidase gene."
    Herrmann T., Schindler D., Tabe H., Onodera O., Igarashi S., Polack A., Zehnpfennig D., Tsuji S.
    Gene 211:205-214(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
    Tissue: Liver.
  3. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ILS and ISS.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  5. "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].
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiNAGAB_MOUSE
AccessioniPrimary (citable) accession number: Q9QWR8
Secondary accession number(s): O88620, Q8R437, Q8VDK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 22, 2015
This is version 106 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.