GenomeNet

Database: UniProt
Entry: Q8BJ48
LinkDB: Q8BJ48
Original site: Q8BJ48 
ID   NAGPA_MOUSE             Reviewed;         517 AA.
AC   Q8BJ48; Q3UUT5; Q8CHQ8; Q9QZE6;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   10-APR-2019, entry version 133.
DE   RecName: Full=N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase;
DE            EC=3.1.4.45;
DE   AltName: Full=Mannose 6-phosphate-uncovering enzyme;
DE   AltName: Full=Phosphodiester alpha-GlcNAcase;
DE   Flags: Precursor;
GN   Name=Nagpa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Thymus;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-517.
RX   PubMed=10551838; DOI=10.1074/jbc.274.46.32778;
RA   Kornfeld R.H., Bao M., Brewer K., Noll C., Canfield W.M.;
RT   "Molecular cloning and functional expression of two splice forms of
RT   human N-acetylglucosamine-1-phosphodiester alpha-N-
RT   acetylglucosaminidase.";
RL   J. Biol. Chem. 274:32778-32785(1999).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart;
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the second step in the formation of the
CC       mannose 6-phosphate targeting signal on lysosomal enzyme
CC       oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-
CC       mannose moieties, which are formed in the first step. Also
CC       hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-
CC       acetylglucosaminyltransferases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(4)-[6-(N-acetyl-alpha-D-glucosaminyl-1-phospho)-
CC         alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-
CC         asparaginyl-[protein] = H(+) + N(4)-[6-phospho-alpha-D-mannosyl-
CC         (1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] + N-
CC         acetyl-D-glucosamine; Xref=Rhea:RHEA:24372, Rhea:RHEA-
CC         COMP:14508, Rhea:RHEA-COMP:14509, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:140369, ChEBI:CHEBI:140371,
CC         ChEBI:CHEBI:506227; EC=3.1.4.45;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Homotetramer arranged as two disulfide-linked homodimers.
CC       Interacts with AP4M1. {ECO:0000250|UniProtKB:P68827,
CC       ECO:0000250|UniProtKB:Q9UK23}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane;
CC       Single-pass type I membrane protein. Golgi apparatus, trans-Golgi
CC       network {ECO:0000250}. Note=Cis/medial Golgi.
CC   -!- DOMAIN: The tyrosine-based internalization signal may be essential
CC       for its retrieval from the plasma membrane to the TGN.
CC   -!- DOMAIN: The C-terminal NPFKD sequence is an attractive candidate
CC       for either an endocytosis signal acting at the plasma membrane or
CC       a retrieval signal acting at the TGN to return the enzyme to the
CC       cis/medial-Golgi.
CC   -!- PTM: The precursor is cleaved and activated in the trans-Golgi
CC       network by a furin endopeptidase. {ECO:0000250}.
DR   EMBL; AK032158; BAC27731.1; -; mRNA.
DR   EMBL; AK138035; BAE23539.1; -; mRNA.
DR   EMBL; BC039790; AAH39790.1; -; mRNA.
DR   EMBL; AF187073; AAF08274.1; -; Genomic_DNA.
DR   CCDS; CCDS27933.1; -.
DR   RefSeq; NP_038824.2; NM_013796.3.
DR   UniGene; Mm.215641; -.
DR   ProteinModelPortal; Q8BJ48; -.
DR   SMR; Q8BJ48; -.
DR   IntAct; Q8BJ48; 1.
DR   MINT; Q8BJ48; -.
DR   STRING; 10090.ENSMUSP00000023911; -.
DR   PhosphoSitePlus; Q8BJ48; -.
DR   SwissPalm; Q8BJ48; -.
DR   EPD; Q8BJ48; -.
DR   MaxQB; Q8BJ48; -.
DR   PaxDb; Q8BJ48; -.
DR   PRIDE; Q8BJ48; -.
DR   Ensembl; ENSMUST00000023911; ENSMUSP00000023911; ENSMUSG00000023143.
DR   GeneID; 27426; -.
DR   KEGG; mmu:27426; -.
DR   UCSC; uc007ybv.2; mouse.
DR   CTD; 51172; -.
DR   MGI; MGI:1351598; Nagpa.
DR   eggNOG; ENOG410IF19; Eukaryota.
DR   eggNOG; ENOG410ZT6Y; LUCA.
DR   GeneTree; ENSGT00950000182725; -.
DR   HOGENOM; HOG000059612; -.
DR   HOVERGEN; HBG052571; -.
DR   InParanoid; Q8BJ48; -.
DR   KO; K01125; -.
DR   OMA; CPCDPKT; -.
DR   OrthoDB; 18592at2759; -.
DR   PhylomeDB; Q8BJ48; -.
DR   TreeFam; TF331920; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q8BJ48; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000023143; Expressed in 170 organ(s), highest expression level in lymph node.
DR   ExpressionAtlas; Q8BJ48; baseline and differential.
DR   Genevisible; Q8BJ48; MM.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003944; F:N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0033299; P:secretion of lysosomal enzymes; IMP:MGI.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR018711; NAGPA.
DR   Pfam; PF09992; NAGPA; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Golgi apparatus; Hydrolase; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Zymogen.
FT   SIGNAL        1     25       {ECO:0000250}.
FT   PROPEP       26     49       Removed in mature form. {ECO:0000250}.
FT                                /FTId=PRO_0000424660.
FT   CHAIN        50    517       N-acetylglucosamine-1-phosphodiester
FT                                alpha-N-acetylglucosaminidase.
FT                                /FTId=PRO_0000021789.
FT   TOPO_DOM     50    453       Lumenal. {ECO:0000255}.
FT   TRANSMEM    454    474       Helical. {ECO:0000255}.
FT   TOPO_DOM    475    517       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      359    391       EGF-like.
FT   REGION      488    495       Mediates the interaction with AP4M1.
FT                                {ECO:0000250|UniProtKB:Q9UK23}.
FT   MOTIF       488    491       Tyrosine-based internalization motif.
FT   MOTIF       511    515       NPF internalization motif.
FT   CARBOHYD    215    215       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    297    297       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    367    367       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    389    389       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    421    421       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    116    149       {ECO:0000250}.
FT   DISULFID    133    324       {ECO:0000250}.
FT   DISULFID    308    315       {ECO:0000250}.
FT   DISULFID    363    374       {ECO:0000250}.
FT   DISULFID    381    390       {ECO:0000250}.
FT   CONFLICT     69     73       TNPGA -> LATHEPRAP (in Ref. 3; AAF08274).
FT                                {ECO:0000305}.
FT   CONFLICT    117    121       AQKRR -> GGRSAA (in Ref. 3; AAF08274).
FT                                {ECO:0000305}.
FT   CONFLICT    130    130       P -> R (in Ref. 3; AAF08274).
FT                                {ECO:0000305}.
FT   CONFLICT    183    185       YLS -> SCL (in Ref. 3; AAF08274).
FT                                {ECO:0000305}.
FT   CONFLICT    265    265       G -> GD (in Ref. 3; AAF08274).
FT                                {ECO:0000305}.
FT   CONFLICT    349    349       T -> N (in Ref. 1; BAC27731).
FT                                {ECO:0000305}.
FT   CONFLICT    414    414       S -> F (in Ref. 3; AAF08274).
FT                                {ECO:0000305}.
FT   CONFLICT    508    508       M -> T (in Ref. 2; AAH39790).
FT                                {ECO:0000305}.
SQ   SEQUENCE   517 AA;  56044 MW;  80E9D4AFB3873177 CRC64;
     MAAPRGPGLF LIPALLGLLG VAWCSLSFGV SRDDDLLLPY PLARRRPSRD CARVRSGSPE
     QESWPPPPTN PGASHHAAVR TFVSHFEGRA VAGHLTRVAD PLRTFSVLEP GGAGGCAQKR
     RATVEDTAVP AGCRIAQNGG FFRMSTGECL GNVVSDGRLV SSSGGLQNAQ FGIRRDGTIV
     TGYLSEEEVL DPVNPFVQLL SGVVWLIRNG NIYINESQAI ECDETQETGS FSKFVNVMSA
     RTAVGHDREG QLILFHADGQ TEQRGLNLWE MAEFLRQQDV VNAINLDGGG SATFVLNGTL
     ASYPSDHCQD NMWRCPRQVS TVVCVHEPRC QPPDCSGHGT CVDGHCECTS HFWRGEACSE
     LDCGPSNCSQ HGLCTETGCH CDAGWTGSNC SEECPLGWYG PGCQRPCQCE HQCSCDPQTG
     NCSISQVRQC LQPTEATPRA GELASFTRTT WLALTLTLIF LLLISTGVNV SLFLGSRAER
     NRHLDGDYVY HPLQEVNGEA LTAEKEHMEE TSNPFKD
//
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