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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]

 GNPTA_HUMAN             Reviewed;        1256 AA.
Q3T906; A2RRQ9; Q3ZQK2; Q6IPW5; Q86TQ2; Q96N13; Q9ULL2;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
10-OCT-2018, entry version 128.
RecName: Full=N-acetylglucosamine-1-phosphotransferase subunits alpha/beta;
EC=2.7.8.17 {ECO:0000269|PubMed:19955174};
AltName: Full=GlcNAc-1-phosphotransferase subunits alpha/beta;
AltName: Full=Stealth protein GNPTAB;
AltName: Full=UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta;
Contains:
RecName: Full=N-acetylglucosamine-1-phosphotransferase subunit alpha;
Contains:
RecName: Full=N-acetylglucosamine-1-phosphotransferase subunit beta;
Flags: Precursor;
Name=GNPTAB; Synonyms=GNPTA, KIAA1208;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
INVOLVEMENT IN MLII.
PubMed=16200072; DOI=10.1038/nm1305;
Tiede S., Storch S., Luebke T., Henrissat B., Bargal R.,
Raas-Rothschild A., Braulke T.;
"Mucolipidosis II is caused by mutations in GNPTA encoding the
alpha/beta GlcNAc-1-phosphotransferase.";
Nat. Med. 11:1109-1112(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=16120602; DOI=10.1074/jbc.M509008200;
Kudo M., Bao M., D'Souza A., Ying F., Pan H., Roe B.A., Canfield W.M.;
"The alpha- and beta-subunits of the human UDP-N-
acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-
phosphotransferase are encoded by a single cDNA.";
J. Biol. Chem. 280:36141-36149(2005).
[3]
ERRATUM.
Kudo M., Bao M., D'Souza A., Ying F., Pan H., Roe B.A., Canfield W.M.;
J. Biol. Chem. 280:42476-42476(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-847 (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 307-1256 (ISOFORM 1).
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:337-345(1999).
[7]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[8]
IDENTIFICATION AS A STEALTH PROTEIN, AND PUTATIVE FUNCTION.
PubMed=16299590; DOI=10.1371/journal.pcbi.0010063;
Sperisen P., Schmid C.D., Bucher P., Zilian O.;
"Stealth proteins: in silico identification of a novel protein family
rendering bacterial pathogens invisible to host immune defense.";
PLoS Comput. Biol. 1:492-499(2005).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-699.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=19955174; DOI=10.1074/jbc.M109.068650;
Qian Y., Lee I., Lee W.S., Qian M., Kudo M., Canfield W.M., Lobel P.,
Kornfeld S.;
"Functions of the alpha, beta, and gamma subunits of UDP-
GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase.";
J. Biol. Chem. 285:3360-3370(2010).
[11]
PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, GLYCOSYLATION, AND
MUTAGENESIS OF ARG-925; LEU-927 AND LYS-928.
PubMed=21719679; DOI=10.1126/science.1205677;
Marschner K., Kollmann K., Schweizer M., Braulke T., Pohl S.;
"A key enzyme in the biogenesis of lysosomes is a protease that
regulates cholesterol metabolism.";
Science 333:87-90(2011).
[12]
INVOLVEMENT IN MLII.
PubMed=23773965; DOI=10.1016/j.ygeno.2013.06.001;
Yang Y., Wu J., Liu H., Chen X., Wang Y., Zhao M., He X.;
"Two homozygous nonsense mutations of GNPTAB gene in two Chinese
families with mucolipidosis II alpha/beta using targeted next-
generation sequencing.";
Genomics 102:169-173(2013).
[13]
CHARACTERIZATION OF VARIANTS MLIIIA GLN-4 AND TYR-15.
PubMed=24550498; DOI=10.1073/pnas.1401417111;
van Meel E., Qian Y., Kornfeld S.A.;
"Mislocalization of phosphotransferase as a cause of mucolipidosis III
alphabeta.";
Proc. Natl. Acad. Sci. U.S.A. 111:3532-3537(2014).
[14]
CHARACTERIZATION OF VARIANTS MLII LEU-81; ASP-182; PRO-205; LEU-334;
LEU-348; LEU-374; ASN-732; ARG-928; VAL-955; CYS-986; PRO-1001;
VAL-1054 AND MET-1236, CHARACTERIZATION OF VARIANTS MLIIIA GLN-4;
TYR-15; VAL-190; GLN-334; PHE-399; THR-403; ALA-407; TYR-442; GLY-461;
SER-468; TYR-505; PRO-587; PRO-926; TYR-956; GLY-1018 AND SER-1153,
AND CHARACTERIZATION OF VARIANTS ARG-523; THR-592 AND TRP-785.
PubMed=25505245; DOI=10.1074/jbc.M114.612507;
Qian Y., van Meel E., Flanagan-Steet H., Yox A., Steet R.,
Kornfeld S.;
"Analysis of mucolipidosis II/III GNPTAB missense mutations identifies
domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase
involved in catalytic function and lysosomal enzyme recognition.";
J. Biol. Chem. 290:3045-3056(2015).
[15]
VARIANT MLIIIA ALA-407, AND VARIANT GLY-662.
PubMed=16094673; DOI=10.1002/ajmg.a.30868;
Tiede S., Muschol N., Reutter G., Cantz M., Ullrich K., Braulke T.;
"Missense mutations in N-acetylglucosamine-1-phosphotransferase
alpha/beta subunit gene in a patient with mucolipidosis III and a mild
clinical phenotype.";
Am. J. Med. Genet. A 137:235-240(2005).
[16]
VARIANT MLIIIA GLN-4.
PubMed=16465621; DOI=10.1086/500849;
Kudo M., Brem M.S., Canfield W.M.;
"Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical
pseudo-Hurler polydystrophy) are caused by mutations in the GlcNAc-
phosphotransferase alpha/beta-subunits precursor gene.";
Am. J. Hum. Genet. 78:451-463(2006).
[17]
VARIANT MLII MET-1236.
PubMed=16835905; DOI=10.1002/humu.9443;
Tiede S., Cantz M., Spranger J., Braulke T.;
"Missense mutation in the N-acetylglucosamine-1-phosphotransferase
gene (GNPTA) in a patient with mucolipidosis II induces changes in the
size and cellular distribution of GNPTG.";
Hum. Mutat. 27:830-831(2006).
[18]
VARIANT MLIIIA PHE-399.
PubMed=16630736; DOI=10.1016/j.ymgme.2006.03.003;
Bargal R., Zeigler M., Abu-Libdeh B., Zuri V., Mandel H.,
Ben Neriah Z., Stewart F., Elcioglu N., Hindi T., Le Merrer M.,
Bach G., Raas-Rothschild A.;
"When Mucolipidosis III meets Mucolipidosis II: GNPTA gene mutations
in 24 patients.";
Mol. Genet. Metab. 88:359-363(2006).
[19]
VARIANT MLIIIA PRO-587.
PubMed=17034777; DOI=10.1016/j.cca.2006.09.004;
Lam C.W., Yan M.S., Li C.K., Lau K.C., Tong S.F., Tang H.Y.;
"DNA-based diagnosis of mucolipidosis type IIIA and
mucopolysacchariodisis type VI in a Chinese family: a chance of 1 in
7.6 trillion.";
Clin. Chim. Acta 376:250-252(2007).
[20]
VARIANTS MLII ASP-182; PRO-205; ASN-732; ARG-928; VAL-955 AND
VAL-1054, VARIANT MLIIIA GLN-4, AND CHARACTERIZATION OF VARIANT MLIIIA
GLN-4.
PubMed=19938078; DOI=10.1002/ajmg.a.33134;
Zarghooni M., Dittakavi S.S.;
"Molecular analysis of cell lines from patients with mucolipidosis II
and mucolipidosis III.";
Am. J. Med. Genet. A 149A:2753-2761(2009).
[21]
VARIANTS MLIIIA THR-403; TYR-442; GLY-461 AND PRO-926, AND VARIANT
MLII PRO-1001.
PubMed=19634183; DOI=10.1002/humu.21099;
Tappino B., Chuzhanova N.A., Regis S., Dardis A., Corsolini F.,
Stroppiano M., Tonoli E., Beccari T., Rosano C., Mucha J., Blanco M.,
Szlago M., Di Rocco M., Cooper D.N., Filocamo M.;
"Molecular characterization of 22 novel UDP-N-acetylglucosamine-1-
phosphate transferase alpha- and beta-subunit (GNPTAB) gene mutations
causing mucolipidosis types IIalpha/beta and IIIalpha/beta in 46
patients.";
Hum. Mutat. 30:E956-E973(2009).
[22]
VARIANTS MLII LEU-334 AND LEU-374, AND VARIANTS MLIIIA LEU-374;
TYR-956 AND SER-1153.
PubMed=19197337; DOI=10.1038/jhg.2009.3;
Otomo T., Muramatsu T., Yorifuji T., Okuyama T., Nakabayashi H.,
Fukao T., Ohura T., Yoshino M., Tanaka A., Okamoto N., Inui K.,
Ozono K., Sakai N.;
"Mucolipidosis II and III alpha/beta: mutation analysis of 40 Japanese
patients showed genotype-phenotype correlation.";
J. Hum. Genet. 54:145-151(2009).
[23]
VARIANTS MLIIIA GLN-4; TYR-15; VAL-190; GLN-334; PHE-399; SER-468;
TYR-505; ARG-956 AND GLY-1018, AND VARIANT MLII LEU-348.
PubMed=19617216; DOI=10.1136/jmg.2009.067736;
Cathey S.S., Leroy J.G., Wood T., Eaves K., Simensen R.J., Kudo M.,
Stevenson R.E., Friez M.J.;
"Phenotype and genotype in mucolipidoses II and III alpha/beta: a
study of 61 probands.";
J. Med. Genet. 47:38-48(2010).
[24]
VARIANTS SER-455; LEU-625 AND LYS-1200, AND POSSIBLE INVOLVEMENT IN
PERSISTENT STUTTERING.
PubMed=20147709; DOI=10.1056/NEJMoa0902630;
Kang C., Riazuddin S., Mundorff J., Krasnewich D., Friedman P.,
Mullikin J.C., Drayna D.;
"Mutations in the lysosomal enzyme-targeting pathway and persistent
stuttering.";
N. Engl. J. Med. 362:677-685(2010).
[25]
VARIANT MLII CYS-986.
PubMed=22495880; DOI=10.1002/ajmg.a.35295;
Coutinho M.F., Santos L.S., Girisha K.M., Satyamoorthy K., Lacerda L.,
Prata M.J., Alves S.;
"Mucolipidosis type II alpha/beta with a homozygous missense mutation
in the GNPTAB gene.";
Am. J. Med. Genet. A 158A:1225-1228(2012).
[26]
VARIANT MLIIIA GLN-4, AND CHARACTERIZATION OF VARIANT MLIIIA GLN-4.
PubMed=24045841; DOI=10.1038/ejhg.2013.207;
Leroy J.G., Sillence D., Wood T., Barnes J., Lebel R.R., Friez M.J.,
Stevenson R.E., Steet R., Cathey S.S.;
"A novel intermediate mucolipidosis II/IIIalphabeta caused by GNPTAB
mutation in the cytosolic N-terminal domain.";
Eur. J. Hum. Genet. 22:594-601(2014).
[27]
VARIANT MLII LEU-81, AND VARIANTS MLIIIA PHE-399; THR-403 AND TYR-505.
PubMed=23566849; DOI=10.1016/j.gene.2013.03.105;
Cury G.K., Matte U., Artigalas O., Alegra T., Velho R.V., Sperb F.,
Burin M.G., Ribeiro E.M., Lourenco C.M., Kim C.A., Valadares E.R.,
Galera M.F., Acosta A.X., Schwartz I.V.;
"Mucolipidosis II and III alpha/beta in Brazil: analysis of the GNPTAB
gene.";
Gene 524:59-64(2013).
[28]
VARIANTS MLII LEU-81; CYS-986 AND MET-1236, VARIANT MLIIIA PHE-399,
CHARACTERIZATION OF VARIANTS MLII LEU-81; CYS-986 AND MET-1236,
CHARACTERIZATION OF VARIANT MLIIIA PHE-399, SUBCELLULAR LOCATION,
PROTEOLYTIC PROCESSING, AND GLYCOSYLATION.
PubMed=24375680; DOI=10.1002/humu.22502;
De Pace R., Coutinho M.F., Koch-Nolte F., Haag F., Prata M.J.,
Alves S., Braulke T., Pohl S.;
"Mucolipidosis II-related mutations inhibit the exit from the
endoplasmic reticulum and proteolytic cleavage of GlcNAc-1-
phosphotransferase precursor protein (GNPTAB).";
Hum. Mutat. 35:368-376(2014).
[29]
VARIANT MLII ASN-732, CHARACTERIZATION OF VARIANT MLII ASN-732,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23733939; DOI=10.1073/pnas.1308453110;
Qian Y., Flanagan-Steet H., van Meel E., Steet R., Kornfeld S.A.;
"The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-
acetylglucosamine-1-phosphotransferase is a substrate recognition
module.";
Proc. Natl. Acad. Sci. U.S.A. 110:10246-10251(2013).
[30]
VARIANTS THR-592 AND TRP-785.
PubMed=24767253; DOI=10.1186/1750-1172-9-59;
Fernandez-Marmiesse A., Morey M., Pineda M., Eiris J., Couce M.L.,
Castro-Gago M., Fraga J.M., Lacerda L., Gouveia S., Perez-Poyato M.S.,
Armstrong J., Castineiras D., Cocho J.A.;
"Assessment of a targeted resequencing assay as a support tool in the
diagnosis of lysosomal storage disorders.";
Orphanet J. Rare Dis. 9:59-59(2014).
[31]
VARIANTS MLIIIA MET-644 AND THR-1223 DEL, CHARACTERIZATION OF VARIANTS
MLIIIA PHE-399; THR-403; TYR-505; ARG-575; MET-644 AND THR-1223 DEL,
CHARACTERIZATION OF VARIANT MLII 937-TYR--MET-972 DEL, MUTAGENESIS OF
ILE-346 AND TRP-357, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
PubMed=25788519; DOI=10.1093/hmg/ddv100;
Velho R.V., De Pace R., Kluender S., Sperb-Ludwig F., Lourenco C.M.,
Schwartz I.V., Braulke T., Pohl S.;
"Analyses of disease-related GNPTAB mutations define a novel GlcNAc-1-
phosphotransferase interaction domain and an alternative site-1
protease cleavage site.";
Hum. Mol. Genet. 24:3497-3505(2015).
[32]
VARIANT MLII CYS-986, AND VARIANT ARG-523.
PubMed=24798265; DOI=10.1007/8904_2014_308;
Cobos P.N., Steglich C., Santer R., Lukacs Z., Gal A.;
"Dried blood spots allow targeted screening to diagnose
mucopolysaccharidosis and mucolipidosis.";
JIMD Rep. 15:123-132(2015).
[33]
VARIANT LYS-1200.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
[34]
VARIANTS MLII GLY-76; LEU-81; LEU-385 AND 1111-TYR--VAL-1256 DEL,
CHARACTERIZATION OF VARIANTS MLII GLY-76 AND LEU-385, VARIANTS MLIIIA
LEU-81; 278-GLN--VAL-1256 DEL; THR-403 AND TYR-505, FUNCTION,
SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
PubMed=28918368; DOI=10.1016/j.biocel.2017.09.006;
Ludwig N.F., Velho R.V., Sperb-Ludwig F., Acosta A.X., Ribeiro E.M.,
Kim C.A., Gandelman Horovitz D.D., Boy R., Rodovalho-Doriqui M.J.,
Lourenco C.M., Santos E.S., Braulke T., Pohl S., Schwartz I.V.D.;
"GNPTAB missense mutations cause loss of GlcNAc-1-phosphotransferase
activity in mucolipidosis type II through distinct mechanisms.";
Int. J. Biochem. Cell Biol. 92:90-94(2017).
-!- 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}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + lysosomal-enzyme
D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-
phospho-D-mannose. {ECO:0000269|PubMed:19955174}.
-!- SUBUNIT: Hexamer of two alpha, two beta and two gamma (GNPTG)
subunits; disulfide-linked. The alpha and/or the beta subunits of
the enzyme constitute the catalytic subunits.
{ECO:0000269|PubMed:19955174}.
-!- INTERACTION:
Q8WTP8:AEN; NbExp=3; IntAct=EBI-1104907, EBI-8637627;
Q86YD7:FAM90A1; NbExp=3; IntAct=EBI-1104907, EBI-6658203;
P25786:PSMA1; NbExp=3; IntAct=EBI-1104907, EBI-359352;
Q96FJ0:STAMBPL1; NbExp=3; IntAct=EBI-1104907, EBI-745021;
P15622-3:ZNF250; NbExp=3; IntAct=EBI-1104907, EBI-10177272;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q3T906-1; Sequence=Displayed;
Name=2;
IsoId=Q3T906-2; Sequence=VSP_017338, VSP_017339;
-!- TISSUE SPECIFICITY: Expressed in the heart, whole brain, placenta,
lung, liver, skeletal muscle, kidney and pancreas.
{ECO:0000269|PubMed:16120602}.
-!- DOMAIN: The DMAP-interaction domain mediates substrate
recognition. It specifically recognizes a conformation-dependent
protein determinant present in acid hydrolases (PubMed:23733939).
{ECO:0000269|PubMed:23733939}.
-!- 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}.
-!- DISEASE: Mucolipidosis type II (MLII) [MIM:252500]: Fatal,
autosomal recessive, lysosomal storage disorder characterized by
severe clinical and radiologic features, peculiar fibroblast
inclusions, and no excessive mucopolysacchariduria. Congenital
dislocation of the hip, thoracic deformities, hernia, and
hyperplastic gums are evident soon after birth.
{ECO:0000269|PubMed:16200072, ECO:0000269|PubMed:16835905,
ECO:0000269|PubMed:19197337, ECO:0000269|PubMed:19617216,
ECO:0000269|PubMed:19634183, ECO:0000269|PubMed:19938078,
ECO:0000269|PubMed:22495880, ECO:0000269|PubMed:23566849,
ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:23773965,
ECO:0000269|PubMed:24375680, ECO:0000269|PubMed:24798265,
ECO:0000269|PubMed:25505245, ECO:0000269|PubMed:25788519,
ECO:0000269|PubMed:28918368}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Mucolipidosis type III complementation group A (MLIIIA)
[MIM:252600]: Autosomal recessive disease of lysosomal enzyme
targeting. Clinically MLIII is characterized by restricted joint
mobility, skeletal dysplasia, and short stature. Mildly coarsened
facial features and thickening of the skin have been described.
Cardiac valvular disease and corneal clouding may also occur. Half
of the reported patients show learning disabilities or mental
retardation. {ECO:0000269|PubMed:16094673,
ECO:0000269|PubMed:16465621, ECO:0000269|PubMed:16630736,
ECO:0000269|PubMed:17034777, ECO:0000269|PubMed:19197337,
ECO:0000269|PubMed:19617216, ECO:0000269|PubMed:19634183,
ECO:0000269|PubMed:19938078, ECO:0000269|PubMed:23566849,
ECO:0000269|PubMed:24045841, ECO:0000269|PubMed:24375680,
ECO:0000269|PubMed:24550498, ECO:0000269|PubMed:25505245,
ECO:0000269|PubMed:25788519, ECO:0000269|PubMed:28918368}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=Genetic variations in GNPTAB have been suggested to
play a role in susceptibility to persistent stuttering. Stuttering
is a common speech disorder characterized by repetitions,
prolongations, and interruptions in the flow of speech.
{ECO:0000269|PubMed:20147709}.
-!- MISCELLANEOUS: Due to the low pH in the endosomal/prelysosomal
compartment, the lysosomal enzyme-MPR complex dissociates and then
the enzyme is delivered to the lysosome. Between 5% and 20% of
newly synthesized lysosomal enzymes escape the binding to the MPR
in the Golgi apparatus and are secreted.
-!- MISCELLANEOUS: Stealth proteins are part of a protein family that
is conserved from bacteria to higher eukaryotes. Family members
were first identified in microbes as proteins that help pathogens
to elude the host innate immune system. Microbial stealth proteins
are most likely involved in the biosynthesis of
exopolysaccharides. Stealth proteins are predicted to function as
hexose-1-phosphoryltransferases.
-!- SIMILARITY: Belongs to the stealth family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AM085438; CAJ30014.1; -; mRNA.
EMBL; AY687932; AAV98624.1; -; mRNA.
EMBL; BC071687; AAH71687.1; -; mRNA.
EMBL; BC042615; AAH42615.1; -; mRNA.
EMBL; BC131787; AAI31788.1; -; mRNA.
EMBL; AK056137; BAB71102.1; -; mRNA.
EMBL; AB033034; BAA86522.2; -; mRNA.
CCDS; CCDS9088.1; -. [Q3T906-1]
RefSeq; NP_077288.2; NM_024312.4. [Q3T906-1]
UniGene; Hs.46850; -.
PDB; 2N6D; NMR; -; A=135-305.
PDBsum; 2N6D; -.
ProteinModelPortal; Q3T906; -.
SMR; Q3T906; -.
BioGrid; 122576; 26.
CORUM; Q3T906; -.
IntAct; Q3T906; 14.
MINT; Q3T906; -.
STRING; 9606.ENSP00000299314; -.
CarbonylDB; Q3T906; -.
GlyConnect; 1532; -.
iPTMnet; Q3T906; -.
PhosphoSitePlus; Q3T906; -.
BioMuta; GNPTAB; -.
DMDM; 90185244; -.
EPD; Q3T906; -.
MaxQB; Q3T906; -.
PaxDb; Q3T906; -.
PeptideAtlas; Q3T906; -.
PRIDE; Q3T906; -.
ProteomicsDB; 61878; -.
ProteomicsDB; 61879; -. [Q3T906-2]
Ensembl; ENST00000299314; ENSP00000299314; ENSG00000111670. [Q3T906-1]
Ensembl; ENST00000549940; ENSP00000449150; ENSG00000111670. [Q3T906-2]
GeneID; 79158; -.
KEGG; hsa:79158; -.
UCSC; uc001tit.4; human. [Q3T906-1]
CTD; 79158; -.
DisGeNET; 79158; -.
EuPathDB; HostDB:ENSG00000111670.14; -.
GeneCards; GNPTAB; -.
GeneReviews; GNPTAB; -.
HGNC; HGNC:29670; GNPTAB.
HPA; HPA014558; -.
HPA; HPA042343; -.
MalaCards; GNPTAB; -.
MIM; 252500; phenotype.
MIM; 252600; phenotype.
MIM; 607840; gene.
neXtProt; NX_Q3T906; -.
OpenTargets; ENSG00000111670; -.
Orphanet; 576; Mucolipidosis type 2.
Orphanet; 577; Mucolipidosis type 3.
PharmGKB; PA128394710; -.
eggNOG; ENOG410IEF9; Eukaryota.
eggNOG; ENOG410XYNB; LUCA.
GeneTree; ENSGT00390000006747; -.
HOVERGEN; HBG057712; -.
InParanoid; Q3T906; -.
KO; K08239; -.
OMA; QELQDMF; -.
OrthoDB; EOG091G0C78; -.
PhylomeDB; Q3T906; -.
TreeFam; TF324175; -.
BRENDA; 2.7.8.17; 2681.
ChiTaRS; GNPTAB; human.
GenomeRNAi; 79158; -.
PRO; PR:Q3T906; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111670; Expressed in 229 organ(s), highest expression level in tibia.
CleanEx; HS_GNPTAB; -.
ExpressionAtlas; Q3T906; baseline and differential.
Genevisible; Q3T906; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0003976; F:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; IDA:UniProtKB.
GO; GO:0046835; P:carbohydrate phosphorylation; IDA:UniProtKB.
GO; GO:0007040; P:lysosome organization; IMP:UniProtKB.
GO; GO:0016256; P:N-glycan processing to lysosome; IMP:UniProtKB.
GO; GO:0033299; P:secretion of lysosomal enzymes; IEA:Ensembl.
InterPro; IPR010506; DMAP1-bd.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR035993; Notch-like_dom_sf.
InterPro; IPR000800; Notch_dom.
InterPro; IPR031358; Stealth_CR1.
InterPro; IPR021520; Stealth_CR2.
InterPro; IPR031357; Stealth_CR3.
InterPro; IPR031356; Stealth_CR4.
Pfam; PF06464; DMAP_binding; 1.
Pfam; PF00066; Notch; 2.
Pfam; PF17101; Stealth_CR1; 1.
Pfam; PF11380; Stealth_CR2; 1.
Pfam; PF17102; Stealth_CR3; 1.
Pfam; PF17103; Stealth_CR4; 1.
SMART; SM01137; DMAP_binding; 1.
SMART; SM00004; NL; 2.
SUPFAM; SSF90193; SSF90193; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 1.
PROSITE; PS50258; LNR; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein; Golgi apparatus;
Membrane; Metal-binding; Mucolipidosis; Polymorphism;
Reference proteome; Repeat; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 928 N-acetylglucosamine-1-phosphotransferase
subunit alpha.
/FTId=PRO_0000225008.
CHAIN 929 1256 N-acetylglucosamine-1-phosphotransferase
subunit beta.
/FTId=PRO_0000225009.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TRANSMEM 1215 1235 Helical. {ECO:0000255}.
REPEAT 438 473 LNR 1.
REPEAT 505 545 LNR 2.
DOMAIN 700 813 DMAP-interaction.
DOMAIN 1005 1040 EF-hand. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 1018 1029 {ECO:0000255|PROSITE-ProRule:PRU00448}.
COMPBIAS 465 498 Gly-rich.
METAL 449 449 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
METAL 464 464 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
METAL 467 467 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
METAL 516 516 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
METAL 531 531 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
METAL 534 534 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00525}.
SITE 928 929 Cleavage; by MBTPS1.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 614 614 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 699 699 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 729 729 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 829 829 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1009 1009 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1129 1129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 438 461 {ECO:0000255|PROSITE-ProRule:PRU00525}.
DISULFID 452 468 {ECO:0000255|PROSITE-ProRule:PRU00525}.
DISULFID 505 528 {ECO:0000255|PROSITE-ProRule:PRU00525}.
DISULFID 519 535 {ECO:0000255|PROSITE-ProRule:PRU00525}.
VAR_SEQ 471 490 NSGGSRYIAGGGGTGSIGVG -> KDVLNCNSFIFMEYFLL
NHY (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017338.
VAR_SEQ 491 1256 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017339.
VARIANT 4 4 K -> Q (in MLIIIA; also found in patients
with intermediate phenotype between MLII
and MLIIIA; no effect on protein
abundance; decreased retention in the
Golgi; mistargeted to lysosomes and
plasma membrane; decreased UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs34159654).
{ECO:0000269|PubMed:16465621,
ECO:0000269|PubMed:19617216,
ECO:0000269|PubMed:19938078,
ECO:0000269|PubMed:24045841,
ECO:0000269|PubMed:24550498,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_027509.
VARIANT 15 15 S -> Y (in MLIIIA; unknown pathological
significance; no effect on protein
abundance; decreased protein cleavage
into alpha and beta subunits; decreased
retention in the Golgi; mistargeted to
lysosomes and plasma membrane; decreased
UDP-N-acetylglucosamine-lysosomal-enzyme
N-acetylglucosaminephosphotransferase
activity; dbSNP:rs281864947).
{ECO:0000269|PubMed:19617216,
ECO:0000269|PubMed:24550498,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073124.
VARIANT 76 76 D -> G (in MLII; loss of Golgi
localization; defects in protein cleavage
into alpha and beta subunits; loss of
UDP-N-acetylglucosamine-lysosomal-enzyme
N-acetylglucosaminephosphotransferase
activity). {ECO:0000269|PubMed:28918368}.
/FTId=VAR_079713.
VARIANT 81 81 W -> L (in MLII and MLIIIA; no effect on
protein abundance; decreased localization
to the Golgi; defects in protein cleavage
into alpha and beta subunits; loss of
UDP-N-acetylglucosamine-lysosomal-enzyme
N-acetylglucosaminephosphotransferase
activity; dbSNP:rs281864953).
{ECO:0000269|PubMed:23566849,
ECO:0000269|PubMed:24375680,
ECO:0000269|PubMed:25505245,
ECO:0000269|PubMed:28918368}.
/FTId=VAR_070831.
VARIANT 182 182 V -> D (in MLII; unknown pathological
significance; decreased localization to
the Golgi; decreased UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs281864958).
{ECO:0000269|PubMed:19938078,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073125.
VARIANT 190 190 D -> V (in MLIIIA; also found in patients
with intermediate phenotype between MLII
and MLIIIA; unknown pathological
significance; no effect on protein
abundance; no effect on localization to
the Golgi; no effect on protein cleavage
into alpha and beta subunits; decreased
UDP-N-acetylglucosamine-lysosomal-enzyme
N-acetylglucosaminephosphotransferase
activity; dbSNP:rs34946266).
{ECO:0000269|PubMed:19617216}.
/FTId=VAR_053545.
VARIANT 205 205 Q -> P (in MLII; unknown pathological
significance; dbSNP:rs281864959).
{ECO:0000269|PubMed:19938078}.
/FTId=VAR_073126.
VARIANT 278 1256 Missing (in MLIIIA).
{ECO:0000269|PubMed:28918368}.
/FTId=VAR_079714.
VARIANT 334 334 R -> L (in MLII; no effect on protein
abundance; loss of localization to the
Golgi; loss of protein cleavage into
alpha and beta subunits; loss of UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs281864970).
{ECO:0000269|PubMed:19197337,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073127.
VARIANT 334 334 R -> Q (in MLIIIA; no effect on protein
abundance; loss of localization to the
Golgi; loss of protein cleavage into
alpha and beta subunits; loss of UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs281864970).
{ECO:0000269|PubMed:19617216,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073128.
VARIANT 348 348 I -> L (in MLII; unknown pathological
significance; no effect on protein
abundance; no effect on localization to
the Golgi; no effect on protein cleavage
into alpha and beta subunits; decreased
UDP-N-acetylglucosamine-lysosomal-enzyme
N-acetylglucosaminephosphotransferase
activity; dbSNP:rs7958709).
{ECO:0000269|PubMed:19617216,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_027510.
VARIANT 374 374 F -> L (in MLII and MLIIIA; no effect on
protein abundance; no effect on
localization to the Golgi; loss of UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs137852900).
{ECO:0000269|PubMed:19197337,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_062807.
VARIANT 385 385 S -> L (in MLII; no loss of Golgi
localization; no defects in protein
cleavage into alpha and beta subunits;
loss of UDP-N-acetylglucosamine-
lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity). {ECO:0000269|PubMed:28918368}.
/FTId=VAR_079715.
VARIANT 399 399 S -> F (in MLIIIA; no effect on protein
abundance; loss of localization to the
Golgi; defects in protein cleavage into
alpha and beta subunits; decreased UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs281865026).
{ECO:0000269|PubMed:16630736,
ECO:0000269|PubMed:19617216,
ECO:0000269|PubMed:23566849,
ECO:0000269|PubMed:24375680,
ECO:0000269|PubMed:25505245,
ECO:0000269|PubMed:25788519}.
/FTId=VAR_062808.
VARIANT 403 403 I -> T (in MLIIIA; loss of localization
to the Golgi; loss of protein cleavage
into alpha and beta subunits; decreased
UDP-N-acetylglucosamine-lysosomal-enzyme
N-acetylglucosaminephosphotransferase
activity; dbSNP:rs281864973).
{ECO:0000269|PubMed:19634183,
ECO:0000269|PubMed:23566849,
ECO:0000269|PubMed:25505245,
ECO:0000269|PubMed:25788519,
ECO:0000269|PubMed:28918368}.
/FTId=VAR_062809.
VARIANT 407 407 D -> A (in MLIIIA; no effect on protein
abundance; no effect on localization to
the Golgi; no effect on protein cleavage
into alpha and beta subunits; decreased
UDP-N-acetylglucosamine-lysosomal-enzyme
N-acetylglucosaminephosphotransferase
activity; dbSNP:rs137852895).
{ECO:0000269|PubMed:16094673,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_025416.
VARIANT 442 442 C -> Y (in MLIIIA; no effect on
localization to the Golgi; no effect on
protein cleavage into alpha and beta
subunits; loss of UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity toward some substrates;
dbSNP:rs281864975).
{ECO:0000269|PubMed:19634183,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_062810.
VARIANT 455 455 A -> S (rare variant; found in
individuals suffering from stuttering;
unknown pathological significance;
dbSNP:rs137853822).
{ECO:0000269|PubMed:20147709}.
/FTId=VAR_073219.
VARIANT 461 461 C -> G (in MLIIIA; no effect on protein
abundance; no effect on localization to
the Golgi; no effect on protein cleavage
into alpha and beta subunits; loss of
UDP-N-acetylglucosamine-lysosomal-enzyme
N-acetylglucosaminephosphotransferase
activity toward some substrates;
dbSNP:rs281864977).
{ECO:0000269|PubMed:19634183,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_062811.
VARIANT 468 468 C -> S (in MLIIIA; patients with
intermediate phenotype between MLII and
MLIIIA; no effect on protein abundance;
no effect on localization to the Golgi;
no effect on protein cleavage into alpha
and beta subunits; loss of UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity toward some substrates;
dbSNP:rs281864979).
{ECO:0000269|PubMed:19617216,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073129.
VARIANT 505 505 C -> Y (in MLIIIA; unknown pathological
significance; decreased localization to
the Golgi; decreased protein cleavage
into alpha and beta subunits; decreased
UDP-N-acetylglucosamine-lysosomal-enzyme
N-acetylglucosaminephosphotransferase
activity; reduces protein abundance;
dbSNP:rs281864980).
{ECO:0000269|PubMed:19617216,
ECO:0000269|PubMed:23566849,
ECO:0000269|PubMed:25505245,
ECO:0000269|PubMed:25788519,
ECO:0000269|PubMed:28918368}.
/FTId=VAR_070832.
VARIANT 523 523 C -> R (found in a patient with
mucolipidosis type II or III; unknown
pathological significance; decreased
localization to the Golgi; decreased
protein cleavage into alpha and beta
subunits; decreased UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity). {ECO:0000269|PubMed:24798265,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073130.
VARIANT 575 575 G -> R (in MLIIIA; significantly reduces
protein cleavage into alpha and beta
subunits; reduces protein abundance;
significantly decreased localization to
the Golgi; significantly reduces UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase).
{ECO:0000269|PubMed:25788519}.
/FTId=VAR_074206.
VARIANT 587 587 R -> P (in MLIIIA; decreased localization
to the Golgi; decreased UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity). {ECO:0000269|PubMed:17034777,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073131.
VARIANT 592 592 A -> T (found in a patient with
mucolipidosis type II or III; unknown
pathological significance; decreased
localization to the Golgi; decreased UDP-
N-acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs149390820).
{ECO:0000269|PubMed:24767253,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073132.
VARIANT 625 625 F -> L (rare variant; found in
individuals suffering from stuttering;
unknown pathological significance;
dbSNP:rs137853823).
{ECO:0000269|PubMed:20147709}.
/FTId=VAR_073220.
VARIANT 644 644 T -> M (in MLIIIA; reduces protein
cleavage into alpha and beta subunits;
reduces protein abundance; no effect on
subcellular location in Golgi apparatus;
mildly affects UDP-N-acetylglucosamine-
lysosomal-enzyme N-
acetylglucosaminephosphotransferase;
dbSNP:rs386765812).
{ECO:0000269|PubMed:25788519}.
/FTId=VAR_074207.
VARIANT 662 662 A -> G (in dbSNP:rs142172397).
{ECO:0000269|PubMed:16094673}.
/FTId=VAR_025417.
VARIANT 732 732 K -> N (in MLII; no effect on
localization to the Golgi; loss of UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity toward some substrates;
dbSNP:rs281864989).
{ECO:0000269|PubMed:19938078,
ECO:0000269|PubMed:23733939,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_070833.
VARIANT 785 785 L -> W (found in a patient with
mucolipidosis type II or III; unknown
pathological significance; no effect on
localization to the Golgi; loss of UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity toward some substrates;
dbSNP:rs144060383).
{ECO:0000269|PubMed:24767253,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073133.
VARIANT 926 926 Q -> P (in MLIIIA; no effect on
localization to the Golgi; loss of
protein cleavage into alpha and beta
subunits; loss of UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs281865002).
{ECO:0000269|PubMed:19634183,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_062812.
VARIANT 928 928 K -> R (in MLII; unknown pathological
significance; dbSNP:rs281865003).
{ECO:0000269|PubMed:19938078}.
/FTId=VAR_073134.
VARIANT 937 972 Missing (in MLII; abnormal protein
cleavage into alpha and beta subunits; no
effect on protein abundance;
significantly decreased localization to
the Golgi; loss of UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase).
{ECO:0000269|PubMed:25788519}.
/FTId=VAR_074208.
VARIANT 955 955 A -> V (in MLII; unknown pathological
significance; no effect on protein
abundance; no effect on localization to
the Golgi; decreased UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs138390866).
{ECO:0000269|PubMed:19938078,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073135.
VARIANT 956 956 H -> R (in MLIIIA; unknown pathological
significance; dbSNP:rs281865005).
{ECO:0000269|PubMed:19617216}.
/FTId=VAR_073136.
VARIANT 956 956 H -> Y (in MLIIIA; no effect on protein
abundance; no effect on localization to
the Golgi; dbSNP:rs281865004).
{ECO:0000269|PubMed:19197337,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_062813.
VARIANT 986 986 R -> C (in MLII; decreased protein
abundance; no effect on localization to
the Golgi; no effect on protein cleavage
into alpha and beta subunits; loss of
UDP-N-acetylglucosamine-lysosomal-enzyme
N-acetylglucosaminephosphotransferase
activity; dbSNP:rs769587233).
{ECO:0000269|PubMed:22495880,
ECO:0000269|PubMed:24375680,
ECO:0000269|PubMed:24798265,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_070834.
VARIANT 1001 1001 L -> P (in MLII; no effect on protein
abundance; decreased localization to the
Golgi; decreased UDP-N-acetylglucosamine-
lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs281865006).
{ECO:0000269|PubMed:19634183,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_062814.
VARIANT 1018 1018 D -> G (in MLIIIA; patients with
intermediate phenotype between MLII and
MLIIIA; unknown pathological
significance; no effect on protein
abundance; decreased localization to the
Golgi; loss of UDP-N-acetylglucosamine-
lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs281865007).
{ECO:0000269|PubMed:19617216,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073137.
VARIANT 1054 1054 L -> V (in MLII; unknown pathological
significance; no effect on localization
to the Golgi; decreased UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs281865010).
{ECO:0000269|PubMed:19938078,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_073138.
VARIANT 1111 1256 Missing (in MLII).
{ECO:0000269|PubMed:28918368}.
/FTId=VAR_079716.
VARIANT 1153 1153 N -> S (in MLIIIA; no effect on protein
abundance; no effect on localization to
the Golgi; loss of UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity; dbSNP:rs281865019).
{ECO:0000269|PubMed:19197337,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_062815.
VARIANT 1200 1200 E -> K (polymorphism; may be a risk
factor for stuttering;
dbSNP:rs137853825).
{ECO:0000269|PubMed:20147709,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_073221.
VARIANT 1223 1223 Missing (in MLIIIA; no effect on protein
cleavage into alpha and beta subunits; no
effect on protein abundance; no effect on
subcellular location in cis-Golgi
apparatus; slightly affects UDP-N-
acetylglucosamine-lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity). {ECO:0000269|PubMed:25788519}.
/FTId=VAR_074209.
VARIANT 1236 1236 K -> M (in MLII; decreased protein
abundance; no effect on localization to
the Golgi; does not suppress protein
cleavage into alpha and beta subunits;
decreased UDP-N-acetylglucosamine-
lysosomal-enzyme N-
acetylglucosaminephosphotransferase
activity). {ECO:0000269|PubMed:16835905,
ECO:0000269|PubMed:24375680,
ECO:0000269|PubMed:25505245}.
/FTId=VAR_027511.
MUTAGEN 346 346 I->A: Partially cleaved by MBTPS1.
{ECO:0000269|PubMed:25788519}.
MUTAGEN 357 357 W->A: Abolishes proteolytic cleavage by
MBTPS1. {ECO:0000269|PubMed:25788519}.
MUTAGEN 925 925 R->A: Abolishes proteolytic cleavage by
MBTPS1. {ECO:0000269|PubMed:21719679}.
MUTAGEN 927 927 L->A: Abolishes proteolytic cleavage by
MBTPS1. {ECO:0000269|PubMed:21719679}.
MUTAGEN 928 928 K->A: Abolishes proteolytic cleavage by
MBTPS1. {ECO:0000269|PubMed:21719679}.
CONFLICT 392 392 I -> V (in Ref. 2; AAV98624).
{ECO:0000305}.
CONFLICT 901 901 Q -> L (in Ref. 2; AAV98624).
{ECO:0000305}.
STRAND 138 141 {ECO:0000244|PDB:2N6D}.
TURN 151 153 {ECO:0000244|PDB:2N6D}.
TURN 155 157 {ECO:0000244|PDB:2N6D}.
HELIX 159 161 {ECO:0000244|PDB:2N6D}.
STRAND 165 172 {ECO:0000244|PDB:2N6D}.
STRAND 175 184 {ECO:0000244|PDB:2N6D}.
HELIX 188 196 {ECO:0000244|PDB:2N6D}.
STRAND 207 210 {ECO:0000244|PDB:2N6D}.
STRAND 225 231 {ECO:0000244|PDB:2N6D}.
HELIX 240 244 {ECO:0000244|PDB:2N6D}.
HELIX 249 251 {ECO:0000244|PDB:2N6D}.
STRAND 252 256 {ECO:0000244|PDB:2N6D}.
STRAND 262 265 {ECO:0000244|PDB:2N6D}.
STRAND 267 272 {ECO:0000244|PDB:2N6D}.
HELIX 274 280 {ECO:0000244|PDB:2N6D}.
SEQUENCE 1256 AA; 143622 MW; 8B861154C516943E CRC64;
MLFKLLQRQT YTCLSHRYGL YVCFLGVVVT IVSAFQFGEV VLEWSRDQYH VLFDSYRDNI
AGKSFQNRLC LPMPIDVVYT WVNGTDLELL KELQQVREQM EEEQKAMREI LGKNTTEPTK
KSEKQLECLL THCIKVPMLV LDPALPANIT LKDLPSLYPS FHSASDIFNV AKPKNPSTNV
SVVVFDSTKD VEDAHSGLLK GNSRQTVWRG YLTTDKEVPG LVLMQDLAFL SGFPPTFKET
NQLKTKLPEN LSSKVKLLQL YSEASVALLK LNNPKDFQEL NKQTKKNMTI DGKELTISPA
YLLWDLSAIS QSKQDEDISA SRFEDNEELR YSLRSIERHA PWVRNIFIVT NGQIPSWLNL
DNPRVTIVTH QDVFRNLSHL PTFSSPAIES HIHRIEGLSQ KFIYLNDDVM FGKDVWPDDF
YSHSKGQKVY LTWPVPNCAE GCPGSWIKDG YCDKACNNSA CDWDGGDCSG NSGGSRYIAG
GGGTGSIGVG QPWQFGGGIN SVSYCNQGCA NSWLADKFCD QACNVLSCGF DAGDCGQDHF
HELYKVILLP NQTHYIIPKG ECLPYFSFAE VAKRGVEGAY SDNPIIRHAS IANKWKTIHL
IMHSGMNATT IHFNLTFQNT NDEEFKMQIT VEVDTREGPK LNSTAQKGYE NLVSPITLLP
EAEILFEDIP KEKRFPKFKR HDVNSTRRAQ EEVKIPLVNI SLLPKDAQLS LNTLDLQLEH
GDITLKGYNL SKSALLRSFL MNSQHAKIKN QAIITDETND SLVAPQEKQV HKSILPNSLG
VSERLQRLTF PAVSVKVNGH DQGQNPPLDL ETTARFRVET HTQKTIGGNV TKEKPPSLIV
PLESQMTKEK KITGKEKENS RMEENAENHI GVTEVLLGRK LQHYTDSYLG FLPWEKKKYF
QDLLDEEESL KTQLAYFTDS KNTGRQLKDT FADSLRYVNK ILNSKFGFTS RKVPAHMPHM
IDRIVMQELQ DMFPEEFDKT SFHKVRHSED MQFAFSYFYY LMSAVQPLNI SQVFDEVDTD
QSGVLSDREI RTLATRIHEL PLSLQDLTGL EHMLINCSKM LPADITQLNN IPPTQESYYD
PNLPPVTKSL VTNCKPVTDK IHKAYKDKNK YRFEIMGEEE IAFKMIRTNV SHVVGQLDDI
RKNPRKFVCL NDNIDHNHKD AQTVKAVLRD FYESMFPIPS QFELPREYRN RFLHMHELQE
WRAYRDKLKF WTHCVLATLI MFTIFSFFAE QLIALKRKIF PRRRIHKEAS PNRIRV


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