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Q9QWR8 (NAGAB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-N-acetylgalactosaminidase
EC=3.2.1.49
Alternative name(s):
Alpha-galactosidase B
Gene names
Name:Naga
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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.

Subunit structure

Homodimer By similarity.

Subcellular location

Lysosome By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 27 family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 By similarity
Chain18 – 415398Alpha-N-acetylgalactosaminidase
PRO_0000001019

Regions

Region78 – 792Substrate binding By similarity

Sites

Active site1561Nucleophile By similarity
Active site2171Proton donor By similarity
Binding site1541Substrate By similarity
Binding site1881Substrate By similarity
Binding site2131Substrate By similarity
Binding site2171Substrate By similarity

Amino acid modifications

Modified residue3221Phosphoserine By similarity
Modified residue3321Phosphoserine By similarity
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation2011N-linked (GlcNAc...) Potential
Glycosylation3851N-linked (GlcNAc...) Potential
Disulfide bond38 ↔ 80 By similarity
Disulfide bond42 ↔ 49 By similarity
Disulfide bond127 ↔ 158 By similarity
Disulfide bond187 ↔ 209 By similarity

Experimental info

Sequence conflict52 – 532ER → DG in CAA11703. Ref.2
Sequence conflict2391L → P in AAH21631. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9QWR8 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: 8BBA9BE03E1350C8

FASTA41547,235
        10         20         30         40         50         60 
MLQKTVLLLA LVAQVLMLEN GLLRTPPMGW LAWERFRCNI DCVEDPKNCI SERLFMEMAD 

        70         80         90        100        110        120 
RLAQDGWRDL GYVYLNIDDC WIGGRDASGR LIPDPKRFPH GIAFLADYAH SLGLKLGIYE 

       130        140        150        160        170        180 
DMGKMTCMGY PGTTLDKVEL DAETFAEWKV DMLKLDGCFS SSRERAEGYP KMAAALNATG 

       190        200        210        220        230        240 
RPIAFSCSWP AYEGGLPPKV NYTEVSRVCN LWRNYKDIQD SWKSVLSILD WFVRHQDVLQ 

       250        260        270        280        290        300 
PVAGPGHWND PDMLLIGNFG LSFDESRAQM ALWTVLAAPL LMSTDLRTIS PQNMDILQNP 

       310        320        330        340        350        360 
LMIKINQDPL GIQGRRILKS KSHIEVFKRY LSNQASALVF FSRRTDMPFR FHCSLLELNY 

       370        380        390        400        410 
PKGRVYEGQN VFTGDIFSGL QTEVNFTVII NPSGVVMWYL YPIKDLGIST MMSHW

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00315593.
RefSeqNP_032695.3. NM_008669.4.
UniGeneMm.20325.

3D structure databases

ProteinModelPortalQ9QWR8.
SMRQ9QWR8. Positions 18-404.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000023088.

Protein family/group databases

CAZyGH27. Glycoside Hydrolase Family 27.

PTM databases

PhosphoSiteQ9QWR8.

Proteomic databases

PaxDbQ9QWR8.
PRIDEQ9QWR8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023088; ENSMUSP00000023088; ENSMUSG00000022453.
GeneID17939.
KEGGmmu:17939.
UCSCuc007wyw.2. mouse.

Organism-specific databases

CTD4668.
MGIMGI:1261422. Naga.

Phylogenomic databases

eggNOGNOG68897.
GeneTreeENSGT00390000008751.
HOGENOMHOG000161224.
HOVERGENHBG001989.
InParanoidQ9QWR8.
KOK01204.
OMAEAQNVYT.
OrthoDBEOG4S1T77.

Gene expression databases

BgeeQ9QWR8.
CleanExMM_NAGA.
GenevestigatorQ9QWR8.
GermOnlineENSMUSG00000022453. Mus musculus.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02065. Melibiase. 1 hit.
[Graphical view]
PRINTSPR00740. GLHYDRLASE27.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio292845.
SOURCESearch...

Entry information

Entry nameNAGAB_MOUSE
AccessionPrimary (citable) accession number: Q9QWR8
Secondary accession number(s): O88620, Q8R437, Q8VDK2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 1, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents