NAGAB_MOUSE
ID NAGAB_MOUSE Reviewed; 415 AA.
AC Q9QWR8; O88620; Q8R437; Q8VDK2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Alpha-N-acetylgalactosaminidase;
DE EC=3.2.1.49;
DE AltName: Full=Alpha-galactosidase B;
DE Flags: Precursor;
GN Name=Naga;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9787108; DOI=10.1006/mgme.1998.2750;
RA Wang A.M., Ioannou Y.A., Zeidner K.M., Desnick R.J.;
RT "Murine alpha-N-acetylgalactosaminidase: isolation and expression of a
RT full-length cDNA and genomic organization: further evidence of an alpha-
RT galactosidase gene family.";
RL Mol. Genet. Metab. 65:165-173(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=9602128; DOI=10.1016/s0378-1119(98)00103-6;
RA Herrmann T., Schindler D., Tabe H., Onodera O., Igarashi S., Polack A.,
RA Zehnpfennig D., Tsuji S.;
RT "Molecular cloning, structural organization, sequence, chromosomal
RT assignment, and expression of the mouse alpha-N-acetylgalactosaminidase
RT gene.";
RL Gene 211:205-214(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Removes terminal alpha-N-acetylgalactosamine residues from
CC glycolipids and glycopeptides. Required for the breakdown of
CC glycolipids. {ECO:0000250|UniProtKB:P17050}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine
CC residues from human blood group A and AB mucin glycoproteins,
CC Forssman hapten and blood group A lacto series glycolipids.;
CC EC=3.2.1.49;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-alpha-GalNAc,IV(2)-alpha-Fuc-
CC nLc4Cer(d18:1(4E)) + H2O = a neolactoside IV(2)-alpha-Fuc-
CC nLc4Cer(d18:1(4E)) + N-acetyl-alpha-D-galactosamine;
CC Xref=Rhea:RHEA:48212, ChEBI:CHEBI:15377, ChEBI:CHEBI:28471,
CC ChEBI:CHEBI:28691, ChEBI:CHEBI:40356;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48213;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-alpha-GalNAc,IV(2)-alpha-Fuc-
CC nLc4Cer(d18:0) + H2O = a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:0)
CC + N-acetyl-alpha-D-galactosamine; Xref=Rhea:RHEA:49304,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:40356, ChEBI:CHEBI:91118,
CC ChEBI:CHEBI:91119; Evidence={ECO:0000250|UniProtKB:P17050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49305;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside IV3GalNAc-Gb4Cer + H2O = globoside Gb4Cer + N-
CC acetyl-alpha-D-galactosamine; Xref=Rhea:RHEA:48412,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:40356, ChEBI:CHEBI:88167,
CC ChEBI:CHEBI:90400; Evidence={ECO:0000250|UniProtKB:P17050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48413;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P17050}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P17050}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL87527.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF079458; AAC28851.1; -; mRNA.
DR EMBL; AJ223966; CAA11703.1; -; Genomic_DNA.
DR EMBL; AY079439; AAL87527.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY079440; AAL87528.1; -; Genomic_DNA.
DR EMBL; AK077116; BAC36620.1; -; mRNA.
DR EMBL; BC021631; AAH21631.1; -; mRNA.
DR CCDS; CCDS27686.1; -.
DR RefSeq; NP_032695.3; NM_008669.4.
DR AlphaFoldDB; Q9QWR8; -.
DR SMR; Q9QWR8; -.
DR BioGRID; 201683; 1.
DR IntAct; Q9QWR8; 1.
DR MINT; Q9QWR8; -.
DR STRING; 10090.ENSMUSP00000023088; -.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR GlyConnect; 2123; 1 N-Linked glycan (1 site).
DR GlyGen; Q9QWR8; 3 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q9QWR8; -.
DR SwissPalm; Q9QWR8; -.
DR EPD; Q9QWR8; -.
DR jPOST; Q9QWR8; -.
DR MaxQB; Q9QWR8; -.
DR PaxDb; Q9QWR8; -.
DR PRIDE; Q9QWR8; -.
DR ProteomicsDB; 252760; -.
DR Antibodypedia; 275; 184 antibodies from 23 providers.
DR DNASU; 17939; -.
DR Ensembl; ENSMUST00000023088; ENSMUSP00000023088; ENSMUSG00000022453.
DR GeneID; 17939; -.
DR KEGG; mmu:17939; -.
DR UCSC; uc007wyw.2; mouse.
DR CTD; 4668; -.
DR MGI; MGI:1261422; Naga.
DR VEuPathDB; HostDB:ENSMUSG00000022453; -.
DR eggNOG; KOG2366; Eukaryota.
DR GeneTree; ENSGT00390000008751; -.
DR HOGENOM; CLU_013093_0_0_1; -.
DR InParanoid; Q9QWR8; -.
DR OMA; NAFGCDI; -.
DR OrthoDB; 964130at2759; -.
DR PhylomeDB; Q9QWR8; -.
DR TreeFam; TF312909; -.
DR BRENDA; 3.2.1.49; 3474.
DR BioGRID-ORCS; 17939; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Naga; mouse.
DR PRO; PR:Q9QWR8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9QWR8; protein.
DR Bgee; ENSMUSG00000022453; Expressed in islet of Langerhans and 241 other tissues.
DR ExpressionAtlas; Q9QWR8; baseline and differential.
DR Genevisible; Q9QWR8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004557; F:alpha-galactosidase activity; IBA:GO_Central.
DR GO; GO:0008456; F:alpha-N-acetylgalactosaminidase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0016052; P:carbohydrate catabolic process; ISS:UniProtKB.
DR GO; GO:0019377; P:glycolipid catabolic process; ISS:UniProtKB.
DR GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR GO; GO:0046477; P:glycosylceramide catabolic process; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035373; Melibiase/NAGA_C.
DR PANTHER; PTHR11452; PTHR11452; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17450; Melibiase_2_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism;
KW Lysosome; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..415
FT /note="Alpha-N-acetylgalactosaminidase"
FT /id="PRO_0000001019"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 217
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 78..79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..80
FT /evidence="ECO:0000250"
FT DISULFID 42..49
FT /evidence="ECO:0000250"
FT DISULFID 127..158
FT /evidence="ECO:0000250"
FT DISULFID 187..209
FT /evidence="ECO:0000250"
FT CONFLICT 52..53
FT /note="ER -> DG (in Ref. 2; CAA11703)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="L -> P (in Ref. 5; AAH21631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47235 MW; 8BBA9BE03E1350C8 CRC64;
MLQKTVLLLA LVAQVLMLEN GLLRTPPMGW LAWERFRCNI DCVEDPKNCI SERLFMEMAD
RLAQDGWRDL GYVYLNIDDC WIGGRDASGR LIPDPKRFPH GIAFLADYAH SLGLKLGIYE
DMGKMTCMGY PGTTLDKVEL DAETFAEWKV DMLKLDGCFS SSRERAEGYP KMAAALNATG
RPIAFSCSWP AYEGGLPPKV NYTEVSRVCN LWRNYKDIQD SWKSVLSILD WFVRHQDVLQ
PVAGPGHWND PDMLLIGNFG LSFDESRAQM ALWTVLAAPL LMSTDLRTIS PQNMDILQNP
LMIKINQDPL GIQGRRILKS KSHIEVFKRY LSNQASALVF FSRRTDMPFR FHCSLLELNY
PKGRVYEGQN VFTGDIFSGL QTEVNFTVII NPSGVVMWYL YPIKDLGIST MMSHW
