NAGPA_BOVIN
ID NAGPA_BOVIN Reviewed; 527 AA.
AC P68827;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 110.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP PROTEIN SEQUENCE OF 50-83, SUBCELLULAR LOCATION, AND HOMOTETRAMERIZATION.
RC TISSUE=Liver;
RX PubMed=9722550; DOI=10.1074/jbc.273.36.23203;
RA Kornfeld R.H., Bao M., Brewer K., Noll C., Canfield W.M.;
RT "Purification and multimeric structure of bovine N-acetylglucosamine-1-
RT phosphodiester alpha-N-acetylglucosaminidase.";
RL J. Biol. Chem. 273:23203-23210(1998).
RN [3]
RP CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=8294420; DOI=10.1016/s0021-9258(17)42087-4;
RA Mullis K.G., Huynh M., Kornfeld R.H.;
RT "Purification and kinetic parameters of bovine liver N-acetylglucosamine-1-
RT phosphodiester alpha-N-acetylglucosaminidase.";
RL J. Biol. Chem. 269:1718-1726(1994).
RN [4]
RP CHARACTERIZATION, SUBUNIT, SIALIC ACID, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=8294421; DOI=10.1016/s0021-9258(17)42088-6;
RA Mullis K.G., Kornfeld R.H.;
RT "Characterization and immunolocalization of bovine N-acetylglucosamine-1-
RT phosphodiester alpha-N-acetylglucosaminidase.";
RL J. Biol. Chem. 269:1727-1733(1994).
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:Q9UK23,
CC ECO:0000269|PubMed:8294421}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi
CC apparatus, trans-Golgi network {ECO:0000250}. Note=Cis/medial Golgi.
CC {ECO:0000250}.
CC -!- PTM: Glycosylated. Contains complex N-linked oligosaccharides with
CC appreciable amounts of sialic acid.
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 AlphaFoldDB; P68827; -.
DR SMR; P68827; -.
DR STRING; 9913.ENSBTAP00000010385; -.
DR PaxDb; P68827; -.
DR PRIDE; P68827; -.
DR Ensembl; ENSBTAT00000076777; ENSBTAP00000057755; ENSBTAG00000007896.
DR VEuPathDB; HostDB:ENSBTAG00000007896; -.
DR VGNC; VGNC:31870; NAGPA.
DR eggNOG; ENOG502QRY5; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR HOGENOM; CLU_031673_1_0_1; -.
DR InParanoid; P68827; -.
DR OrthoDB; 18592at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000007896; Expressed in monocyte and 103 other tissues.
DR ExpressionAtlas; P68827; baseline and differential.
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; IBA:GO_Central.
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 Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Golgi apparatus; Hydrolase; Membrane; Reference proteome; Sialic acid;
KW Signal; Transmembrane; Transmembrane helix; 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_0000424658"
FT CHAIN 50..527
FT /note="N-acetylglucosamine-1-phosphodiester alpha-N-
FT acetylglucosaminidase"
FT /id="PRO_0000096699"
FT TOPO_DOM 50..463
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 359..391
FT /note="EGF-like"
FT REGION 498..505
FT /note="Mediates the interaction with AP4M1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK23"
FT MOTIF 500..503
FT /note="Tyrosine-based internalization motif"
FT MOTIF 523..527
FT /note="NPF internalization motif"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 62
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 57223 MW; 33FEC4FE9DF72D9E CRC64;
MASSMGRFLL FFIALRGFLL EASGDFGSGA SRDDDVLLPY SRARARLARD CTRVHAGRLE
HHESWPPAAQ TAGAHRPSVR TFVSYFADRA VPGHLTRAPE PLRTFSVLEP GGPGGCASKR
RATVEETARP SGCTVAQNGG FFRMETGECL GNVVSGGRRV SSAGGLQNAQ FGIRRDGTLV
TGYLSEEEVL DTENPFVQLL SGVVWLIRNG SIYINESQAA ECEETQETGS FNRFVNVISA
RTAVGHDRKG QLVLLHVDGQ TEQRGINLWE MAEFLLKQDV VNAINLDGGG SATFVLNGTL
ASYPSDHCQD NMWRCPRRVS TVVCVHEPRC QPPDCSGHGT CMEGRCQCTG HFWRGAACDK
LDCGPANCSQ HGLCTETGCR CEAGWTGSNC SEECPLGWYG PGCQSPCKCE HQCPCDPQTG
NCSVNWSPTL SSLFSRVKEC FPPPEVTVQA EELSLLTRTT WLAITLALAF LLLISTAANV
SLFLGSRAAR RRHLDGAYVY HPLQEVNGEH PAAEKEQLGD SSNPFKD
