NAGPA_MOUSE
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 03-AUG-2022, entry version 149.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., 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 [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 project:
RT 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 human
RT N-acetylglucosamine-1-phosphodiester alpha-N-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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the second step in the formation of the mannose 6-
CC phosphate targeting signal on lysosomal enzyme oligosaccharides by
CC removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which
CC are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor
CC for Golgi N-acetylglucosaminyltransferases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-[6-(N-acetyl-alpha-D-glucosaminyl-1-phospho)-alpha-
CC D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein]
CC = H(+) + N(4)-[6-phospho-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-
CC (glycan)]-L-asparaginyl-[protein] + N-acetyl-D-glucosamine;
CC Xref=Rhea:RHEA:24372, Rhea:RHEA-COMP:14508, Rhea:RHEA-COMP:14509,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:140369,
CC ChEBI:CHEBI:140371, 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; Single-
CC pass type I membrane protein. Golgi apparatus, trans-Golgi network
CC {ECO:0000250}. Note=Cis/medial Golgi.
CC -!- DOMAIN: The tyrosine-based internalization signal may be essential for
CC its retrieval from the plasma membrane to the TGN.
CC -!- DOMAIN: The C-terminal NPFKD sequence is an attractive candidate for
CC either an endocytosis signal acting at the plasma membrane or a
CC 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 network
CC by a furin endopeptidase. {ECO:0000250}.
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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 AlphaFoldDB; Q8BJ48; -.
DR SMR; Q8BJ48; -.
DR STRING; 10090.ENSMUSP00000023911; -.
DR GlyGen; Q8BJ48; 5 sites.
DR PhosphoSitePlus; Q8BJ48; -.
DR SwissPalm; Q8BJ48; -.
DR EPD; Q8BJ48; -.
DR MaxQB; Q8BJ48; -.
DR PaxDb; Q8BJ48; -.
DR PRIDE; Q8BJ48; -.
DR ProteomicsDB; 252761; -.
DR Antibodypedia; 24469; 40 antibodies from 14 providers.
DR DNASU; 27426; -.
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 VEuPathDB; HostDB:ENSMUSG00000023143; -.
DR eggNOG; ENOG502QRY5; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR HOGENOM; CLU_031673_1_0_1; -.
DR InParanoid; Q8BJ48; -.
DR OMA; RPCKCEH; -.
DR OrthoDB; 18592at2759; -.
DR PhylomeDB; Q8BJ48; -.
DR TreeFam; TF331920; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 27426; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q8BJ48; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BJ48; protein.
DR Bgee; ENSMUSG00000023143; Expressed in interventricular septum and 164 other tissues.
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; IPR000742; EGF-like_dom.
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 Disulfide bond; EGF-like domain; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT PROPEP 26..49
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000424660"
FT CHAIN 50..517
FT /note="N-acetylglucosamine-1-phosphodiester alpha-N-
FT acetylglucosaminidase"
FT /id="PRO_0000021789"
FT TOPO_DOM 50..453
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 359..391
FT /note="EGF-like"
FT REGION 49..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..495
FT /note="Mediates the interaction with AP4M1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK23"
FT MOTIF 488..491
FT /note="Tyrosine-based internalization motif"
FT MOTIF 511..515
FT /note="NPF internalization motif"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..149
FT /evidence="ECO:0000250"
FT DISULFID 133..324
FT /evidence="ECO:0000250"
FT DISULFID 308..315
FT /evidence="ECO:0000250"
FT DISULFID 363..374
FT /evidence="ECO:0000250"
FT DISULFID 381..390
FT /evidence="ECO:0000250"
FT CONFLICT 69..73
FT /note="TNPGA -> LATHEPRAP (in Ref. 3; AAF08274)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..121
FT /note="AQKRR -> GGRSAA (in Ref. 3; AAF08274)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="P -> R (in Ref. 3; AAF08274)"
FT /evidence="ECO:0000305"
FT CONFLICT 183..185
FT /note="YLS -> SCL (in Ref. 3; AAF08274)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="G -> GD (in Ref. 3; AAF08274)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="T -> N (in Ref. 1; BAC27731)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="S -> F (in Ref. 3; AAF08274)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="M -> T (in Ref. 2; AAH39790)"
FT /evidence="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
