PMID- 10551838
OWN - NLM
STAT- MEDLINE
DCOM- 20000103
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 46
DP  - 1999 Nov 12
TI  - Molecular cloning and functional expression of two splice forms of human
      N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase.
PG  - 32778-85
AB  - We have isolated and sequenced human cDNA and mouse genomic DNA clones encoding
      N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
      (phosphodiester alpha-GlcNAcase) which catalyzes the second step in the synthesis
      of the mannose 6-phosphate recognition signal on lysosomal enzymes. The gene is
      organized into 10 exons. The protein sequence encoded by the clones shows 80%
      identity between human and mouse phosphodiester alpha-GlcNAcase and no homology
      to other known proteins. It predicts a type I membrane-spanning glycoprotein of
      514 amino acids containing a 24-amino acid signal sequence, a luminal domain of
      422 residues with six potential N-linked glycosylation sites, a single 27-residue
      transmembrane region, and a 41-residue cytoplasmic tail that contains both a
      tyrosine-based and an NPF internalization motif. Human brain expressed sequence
      tags lack a 102-base pair region present in human liver cDNA that corresponds to 
      exon 8 in the genomic DNA and probably arises via alternative splicing. COS cells
      transfected with the human cDNA expressed 50-100-fold increases in phosphodiester
      alpha-GlcNAcase activity proving that the cDNA encodes the subunits of the
      tetrameric enzyme. Transfection with cDNA lacking the 102-base pair region also
      gave active enzyme. The complete genomic sequence of human phosphodiester
      alpha-GlcNAcase was recently deposited in the data base. It showed that our cDNA 
      clone was missing only the 5'-untranslated region and initiator methionine and
      revealed that the human genomic DNA has the same exon organization as the mouse
      gene.
FAU - Kornfeld, R
AU  - Kornfeld R
AD  - Department of Medicine, Washington University School of Medicine, St. Louis,
      Missouri 63110, USA.
FAU - Bao, M
AU  - Bao M
FAU - Brewer, K
AU  - Brewer K
FAU - Noll, C
AU  - Noll C
FAU - Canfield, W
AU  - Canfield W
LA  - eng
SI  - GENBANK/AF187072
SI  - GENBANK/AF187073
GR  - CA08759/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (RNA, Messenger)
RN  - EC 3.1.4.- (Phosphoric Diester Hydrolases)
RN  - EC 3.1.4.45 (N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase)
SB  - IM
MH  - Alternative Splicing/*genetics
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - COS Cells
MH  - Cloning, Molecular
MH  - Exons
MH  - Gene Expression Regulation, Enzymologic
MH  - Glycosylation
MH  - Humans
MH  - Introns
MH  - Membrane Glycoproteins/chemistry/genetics
MH  - Molecular Sequence Data
MH  - Phosphoric Diester Hydrolases/*genetics
MH  - RNA, Messenger/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Transfection
EDAT- 1999/11/07 00:00
MHDA- 1999/11/07 00:01
CRDT- 1999/11/07 00:00
PHST- 1999/11/07 00:00 [pubmed]
PHST- 1999/11/07 00:01 [medline]
PHST- 1999/11/07 00:00 [entrez]
AID - 10.1074/jbc.274.46.32778 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Nov 12;274(46):32778-85. doi: 10.1074/jbc.274.46.32778.