| IED ID | IndEnz0002002638 |
| Enzyme Type ID | protease002638 |
| Protein Name |
N-acetylglucosamine-1-phosphotransferase subunits alpha/beta EC 2.7.8.17 GlcNAc-1-phosphotransferase subunits alpha/beta Stealth protein GNPTAB UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta Cleaved into: N-acetylglucosamine-1-phosphotransferase subunit alpha; N-acetylglucosamine-1-phosphotransferase subunit beta |
| Gene Name | GNPTAB GNPTA KIAA1208 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MLFKLLQRQTYTCLSHRYGLYVCFLGVVVTIVSAFQFGEVVLEWSRDQYHVLFDSYRDNIAGKSFQNRLCLPMPIDVVYTWVNGTDLELLKELQQVREQMEEEQKAMREILGKNTTEPTKKSEKQLECLLTHCIKVPMLVLDPALPANITLKDLPSLYPSFHSASDIFNVAKPKNPSTNVSVVVFDSTKDVEDAHSGLLKGNSRQTVWRGYLTTDKEVPGLVLMQDLAFLSGFPPTFKETNQLKTKLPENLSSKVKLLQLYSEASVALLKLNNPKDFQELNKQTKKNMTIDGKELTISPAYLLWDLSAISQSKQDEDISASRFEDNEELRYSLRSIERHAPWVRNIFIVTNGQIPSWLNLDNPRVTIVTHQDVFRNLSHLPTFSSPAIESHIHRIEGLSQKFIYLNDDVMFGKDVWPDDFYSHSKGQKVYLTWPVPNCAEGCPGSWIKDGYCDKACNNSACDWDGGDCSGNSGGSRYIAGGGGTGSIGVGQPWQFGGGINSVSYCNQGCANSWLADKFCDQACNVLSCGFDAGDCGQDHFHELYKVILLPNQTHYIIPKGECLPYFSFAEVAKRGVEGAYSDNPIIRHASIANKWKTIHLIMHSGMNATTIHFNLTFQNTNDEEFKMQITVEVDTREGPKLNSTAQKGYENLVSPITLLPEAEILFEDIPKEKRFPKFKRHDVNSTRRAQEEVKIPLVNISLLPKDAQLSLNTLDLQLEHGDITLKGYNLSKSALLRSFLMNSQHAKIKNQAIITDETNDSLVAPQEKQVHKSILPNSLGVSERLQRLTFPAVSVKVNGHDQGQNPPLDLETTARFRVETHTQKTIGGNVTKEKPPSLIVPLESQMTKEKKITGKEKENSRMEENAENHIGVTEVLLGRKLQHYTDSYLGFLPWEKKKYFQDLLDEEESLKTQLAYFTDSKNTGRQLKDTFADSLRYVNKILNSKFGFTSRKVPAHMPHMIDRIVMQELQDMFPEEFDKTSFHKVRHSEDMQFAFSYFYYLMSAVQPLNISQVFDEVDTDQSGVLSDREIRTLATRIHELPLSLQDLTGLEHMLINCSKMLPADITQLNNIPPTQESYYDPNLPPVTKSLVTNCKPVTDKIHKAYKDKNKYRFEIMGEEEIAFKMIRTNVSHVVGQLDDIRKNPRKFVCLNDNIDHNHKDAQTVKAVLRDFYESMFPIPSQFELPREYRNRFLHMHELQEWRAYRDKLKFWTHCVLATLIMFTIFSFFAEQLIALKRKIFPRRRIHKEASPNRIRV |
| Enzyme Length | 1256 |
| Uniprot Accession Number | Q3T906 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | CA_BIND 1018..1029; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448 |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=N(4)-[alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-[6-(N-acetyl-alpha-D-glucosaminyl-1-phospho)-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] + UMP; Xref=Rhea:RHEA:13581, Rhea:RHEA-COMP:14507, Rhea:RHEA-COMP:14508, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:140357, ChEBI:CHEBI:140369; EC=2.7.8.17; Evidence={ECO:0000269|PubMed:19955174}; |
| DNA Binding | |
| EC Number | 2.7.8.17 |
| Enzyme Function | FUNCTION: Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment. {ECO:0000269|PubMed:19955174, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:28918368}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (8); Calcium binding (1); Chain (2); Disulfide bond (4); Domain (2); Glycosylation (11); Helix (5); Metal binding (6); Mutagenesis (5); Natural variant (45); Repeat (2); Sequence conflict (2); Site (1); Transmembrane (2); Turn (2) |
| Keywords | 3D-structure;Alternative splicing;Calcium;Disease variant;Disulfide bond;Glycoprotein;Golgi apparatus;Membrane;Metal-binding;Mucolipidosis;Reference proteome;Repeat;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
| Interact With | Q8WTP8; Q86YD7; Q9UJJ9; P25786; Q96FJ0; P15622-3 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [N-acetylglucosamine-1-phosphotransferase subunit alpha]: Golgi apparatus membrane {ECO:0000269|PubMed:16120602, ECO:0000269|PubMed:16200072, ECO:0000269|PubMed:21719679, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:25788519, ECO:0000269|PubMed:28918368}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [N-acetylglucosamine-1-phosphotransferase subunit beta]: Golgi apparatus membrane {ECO:0000269|PubMed:16120602, ECO:0000269|PubMed:16200072, ECO:0000269|PubMed:21719679, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:28918368}; Single-pass type II membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: The alpha- and beta-subunits are generated by a proteolytic cleavage by MBTPS1 protease at the Lys-928-Asp-929 bond. {ECO:0000269|PubMed:21719679, ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:25788519, ECO:0000269|PubMed:28918368}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 2N6D; |
| Mapped Pubmed ID | 17043677; 18190596; 19659762; 20379614; 20489197; 20880125; 20944643; 21549105; 21988832; 22884963; 23192343; 25416956; 25643770; 26130485; 26385638; 26496610; 26749367; 26833567; 27180337; 27710913; 29289611; 30204966; 30655525; 30882951; 31003007; 31405983; 31579991; 32199982; 32220096; 32560373; |
| Motif | |
| Gene Encoded By | |
| Mass | 143,622 |
| Kinetics | |
| Metal Binding | METAL 449; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00525; METAL 464; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00525; METAL 467; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00525; METAL 516; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00525; METAL 531; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00525; METAL 534; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00525 |
| Rhea ID | RHEA:13581 |
| Cross Reference Brenda | 2.7.8.17; |