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Q9QWR8

- NAGAB_MOUSE

UniProt

Q9QWR8 - NAGAB_MOUSE

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Protein

Alpha-N-acetylgalactosaminidase

Gene
Naga
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

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 – 1541Substrate By similarity
Active sitei156 – 1561Nucleophile By similarity
Binding sitei188 – 1881Substrate By similarity
Binding sitei213 – 2131Substrate By similarity
Active sitei217 – 2171Proton donor By similarity
Binding sitei217 – 2171Substrate By similarity

GO - Molecular functioni

  1. alpha-galactosidase activity Source: RefGenome
  2. alpha-N-acetylgalactosaminidase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate catabolic process Source: UniProtKB
  2. glycolipid catabolic process Source: UniProtKB
  3. glycoside catabolic process Source: RefGenome
  4. glycosylceramide catabolic process Source: RefGenome
  5. oligosaccharide metabolic process Source: RefGenome
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1261422. Naga.

Subcellular locationi

Lysosome By similarity

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 By similarityAdd
BLAST
Chaini18 – 415398Alpha-N-acetylgalactosaminidasePRO_0000001019Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi38 ↔ 80 By similarity
Disulfide bondi42 ↔ 49 By similarity
Disulfide bondi127 ↔ 158 By similarity
Glycosylationi177 – 1771N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi187 ↔ 209 By similarity
Glycosylationi201 – 2011N-linked (GlcNAc...) Reviewed prediction
Modified residuei322 – 3221Phosphoserine By similarity
Modified residuei332 – 3321Phosphoserine By similarity
Glycosylationi385 – 3851N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9QWR8.
PaxDbiQ9QWR8.
PRIDEiQ9QWR8.

PTM databases

PhosphoSiteiQ9QWR8.

Expressioni

Gene expression databases

BgeeiQ9QWR8.
CleanExiMM_NAGA.
GenevestigatoriQ9QWR8.

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.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG68897.
GeneTreeiENSGT00390000008751.
HOGENOMiHOG000161224.
HOVERGENiHBG001989.
InParanoidiQ9QWR8.
KOiK01204.
OMAiTNFTVVI.
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

MLQKTVLLLA LVAQVLMLEN GLLRTPPMGW LAWERFRCNI DCVEDPKNCI    50
SERLFMEMAD RLAQDGWRDL GYVYLNIDDC WIGGRDASGR LIPDPKRFPH 100
GIAFLADYAH SLGLKLGIYE DMGKMTCMGY PGTTLDKVEL DAETFAEWKV 150
DMLKLDGCFS SSRERAEGYP KMAAALNATG RPIAFSCSWP AYEGGLPPKV 200
NYTEVSRVCN LWRNYKDIQD SWKSVLSILD WFVRHQDVLQ PVAGPGHWND 250
PDMLLIGNFG LSFDESRAQM ALWTVLAAPL LMSTDLRTIS PQNMDILQNP 300
LMIKINQDPL GIQGRRILKS KSHIEVFKRY LSNQASALVF FSRRTDMPFR 350
FHCSLLELNY PKGRVYEGQN VFTGDIFSGL QTEVNFTVII NPSGVVMWYL 400
YPIKDLGIST MMSHW 415
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 532ER → DG in CAA11703. 1 Publication
Sequence conflicti239 – 2391L → P in AAH21631. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS27686.1.
RefSeqi NP_032695.3. NM_008669.4.
UniGenei Mm.20325.

3D structure databases

ProteinModelPortali Q9QWR8.
SMRi Q9QWR8. Positions 18-404.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9QWR8. 1 interaction.
MINTi MINT-1849631.
STRINGi 10090.ENSMUSP00000023088.

Protein family/group databases

CAZyi GH27. Glycoside Hydrolase Family 27.

PTM databases

PhosphoSitei Q9QWR8.

Proteomic databases

MaxQBi Q9QWR8.
PaxDbi Q9QWR8.
PRIDEi Q9QWR8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023088 ; ENSMUSP00000023088 ; ENSMUSG00000022453 .
GeneIDi 17939.
KEGGi mmu:17939.
UCSCi uc007wyw.2. mouse.

Organism-specific databases

CTDi 4668.
MGIi MGI:1261422. Naga.

Phylogenomic databases

eggNOGi NOG68897.
GeneTreei ENSGT00390000008751.
HOGENOMi HOG000161224.
HOVERGENi HBG001989.
InParanoidi Q9QWR8.
KOi K01204.
OMAi TNFTVVI.
OrthoDBi EOG7F24SV.
PhylomeDBi Q9QWR8.
TreeFami TF312909.

Miscellaneous databases

NextBioi 292845.
PROi Q9QWR8.
SOURCEi Search...

Gene expression databases

Bgeei Q9QWR8.
CleanExi MM_NAGA.
Genevestigatori Q9QWR8.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF02065. Melibiase. 1 hit.
[Graphical view ]
PRINTSi PR00740. GLHYDRLASE27.
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 9, 2014
This is version 97 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