GNPTG_HUMAN
ID GNPTG_HUMAN Reviewed; 305 AA.
AC Q9UJJ9; B2R556; Q6XYD7; Q96L13;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=N-acetylglucosamine-1-phosphotransferase subunit gamma;
DE AltName: Full=GlcNAc-1-phosphotransferase subunit gamma;
DE AltName: Full=UDP-N-acetylglucosamine-1-phosphotransferase subunit gamma;
DE Flags: Precursor;
GN Name=GNPTG; Synonyms=C16orf27, GNPTAG; ORFNames=CAB56184, LP2537;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND
RP INVOLVEMENT IN MLIIIC.
RC TISSUE=Brain;
RX PubMed=10712439; DOI=10.1172/jci5826;
RA Raas-Rothschild A., Cormier-Daire V., Bao M., Genin E., Salomon R.,
RA Brewer K., Zeigler M., Mandel H., Toth S., Roe B., Munnich A.,
RA Canfield W.M.;
RT "Molecular basis of variant pseudo-Hurler polydystrophy (mucolipidosis
RT IIIC).";
RL J. Clin. Invest. 105:673-681(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RA Fitzgerald P., Amarante-Mendes G.P., Li W., Green D.R.;
RT "cDNA from human fetal brain.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-305.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [8]
RP INVOLVEMENT IN MLIIIC, AND VARIANT MLIIIC SER-106.
RX PubMed=15060128; DOI=10.1136/jmg.2003.015222;
RA Raas-Rothschild A., Bargal R., Goldman O., Ben-Asher E., Groener J.E.,
RA Toutain A., Stemmer E., Ben-Neriah Z., Flusser H., Beemer F.A.,
RA Penttinen M., Olender T., Rein A.J., Bach G., Zeigler M.;
RT "Genomic organisation of the UDP-N-acetylglucosamine-1-phosphotransferase
RT gamma subunit (GNPTAG) and its mutations in mucolipidosis III.";
RL J. Med. Genet. 41:E52-E52(2004).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19955174; DOI=10.1074/jbc.m109.068650;
RA Qian Y., Lee I., Lee W.S., Qian M., Kudo M., Canfield W.M., Lobel P.,
RA Kornfeld S.;
RT "Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal
RT enzyme N-acetylglucosamine-1-phosphotransferase.";
RL J. Biol. Chem. 285:3360-3370(2010).
RN [10]
RP POSSIBLE INVOLVEMENT IN PERSISTENT STUTTERING, AND VARIANTS ALA-ARG-LEU-5
RP INS; GLU-25 AND VAL-230.
RX PubMed=20147709; DOI=10.1056/nejmoa0902630;
RA Kang C., Riazuddin S., Mundorff J., Krasnewich D., Friedman P.,
RA Mullikin J.C., Drayna D.;
RT "Mutations in the lysosomal enzyme-targeting pathway and persistent
RT stuttering.";
RL N. Engl. J. Med. 362:677-685(2010).
RN [11]
RP GLYCOSYLATION.
RX PubMed=21173149; DOI=10.1074/jbc.m110.202382;
RA Encarnacao M., Kollmann K., Trusch M., Braulke T., Pohl S.;
RT "Post-translational modifications of the gamma-subunit affect intracellular
RT trafficking and complex assembly of GlcNAc-1-phosphotransferase.";
RL J. Biol. Chem. 286:5311-5318(2011).
RN [12]
RP VARIANT MLIIIC ASN-115 DEL, HOMODIMERIZATION, GLYCOSYLATION AT ASN-115, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15532026; DOI=10.1002/humu.9293;
RA Tiede S., Cantz M., Raas-Rothschild A., Muschol N., Buerger F., Ullrich K.,
RA Braulke T.;
RT "A novel mutation in UDP-N-acetylglucosamine-1-phosphotransferase gamma
RT subunit (GNPTAG) in two siblings with mucolipidosis type III alters a used
RT glycosylation site.";
RL Hum. Mutat. 24:535-535(2004).
RN [13]
RP VARIANTS MLIIIC SER-106 AND ASN-115 DEL, AND VARIANT MET-286.
RX PubMed=19370764; DOI=10.1002/humu.20959;
RA Persichetti E., Chuzhanova N.A., Dardis A., Tappino B., Pohl S.,
RA Thomas N.S., Rosano C., Balducci C., Paciotti S., Dominissini S.,
RA Montalvo A.L., Sibilio M., Parini R., Rigoldi M., Di Rocco M., Parenti G.,
RA Orlacchio A., Bembi B., Cooper D.N., Filocamo M., Beccari T.;
RT "Identification and molecular characterization of six novel mutations in
RT the UDP-N-acetylglucosamine-1-phosphotransferase gamma subunit (GNPTG) gene
RT in patients with mucolipidosis III gamma.";
RL Hum. Mutat. 30:978-984(2009).
RN [14]
RP VARIANT MLIIIC TYR-142.
RX PubMed=24316125; DOI=10.1016/j.gene.2013.11.010;
RA Liu S., Zhang W., Shi H., Meng Y., Qiu Z.;
RT "Three novel homozygous mutations in the GNPTG gene that cause
RT mucolipidosis type III gamma.";
RL Gene 535:294-298(2014).
RN [15]
RP VARIANT MLIIIC SER-126, CHARACTERIZATION OF VARIANT MLIIIC SER-126, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26108976; DOI=10.1002/ajmg.a.37213;
RA Barea J.J., van Meel E., Kornfeld S., Bird L.M.;
RT "Tuberous sclerosis, polycystic kidney disease and mucolipidosis III gamma
RT caused by a microdeletion unmasking a recessive mutation.";
RL Am. J. Med. Genet. A 167A:2844-2846(2015).
RN [16]
RP CHARACTERIZATION OF VARIANT MLIIIC SER-106 AND TYR-142, CHARACTERIZATION OF
RP VARIANT MET-286, AND SUBCELLULAR LOCATION.
RX PubMed=27038293; DOI=10.1002/humu.22993;
RA van Meel E., Kornfeld S.;
RT "Mucolipidosis III GNPTG missense mutations cause misfolding of the gamma
RT subunit of GlcNAc-1-phosphotransferase.";
RL Hum. Mutat. 37:623-626(2016).
CC -!- FUNCTION: Non-catalytic subunit of the N-acetylglucosamine-1-
CC phosphotransferase complex, an enzyme that catalyzes the formation of
CC mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides
CC in the Golgi apparatus. Binds and presents the high mannose glycans of
CC the acceptor to the catalytic alpha and beta subunits (GNPTAB).
CC Enhances the rate of N-acetylglucosamine-1-phosphate transfer to the
CC oligosaccharides of acid hydrolase acceptors.
CC {ECO:0000269|PubMed:10712439, ECO:0000269|PubMed:19955174}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Hexamer of two alpha (GNPTAB),
CC two beta (GNPTAB) and two gamma (GNPTG) subunits; disulfide-linked. The
CC alpha and/or the beta subunits of the enzyme constitute the catalytic
CC subunits. {ECO:0000269|PubMed:10712439, ECO:0000269|PubMed:19955174}.
CC -!- INTERACTION:
CC Q9UJJ9; Q3T906: GNPTAB; NbExp=5; IntAct=EBI-372067, EBI-1104907;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15532026}. Golgi
CC apparatus {ECO:0000269|PubMed:15532026, ECO:0000269|PubMed:26108976,
CC ECO:0000269|PubMed:27038293}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10712439}.
CC -!- PTM: Cys-245 mediates the formation of the interchain disulfide bond
CC for formation of the homodimer. Cys-142, Cys-157 and Cys-169 are
CC involved in intramolecular disulfide bonds formation (By similarity).
CC {ECO:0000250}.
CC -!- DISEASE: Mucolipidosis type III complementation group C (MLIIIC)
CC [MIM:252605]: Autosomal recessive disease of lysosomal hydrolase
CC trafficking. Unlike the related diseases, mucolipidosis II and IIIA,
CC the enzyme affected in mucolipidosis IIIC (GlcNAc-phosphotransferase)
CC retains full transferase activity on synthetic substrates but lacks
CC activity on lysosomal hydrolases. Typical clinical findings include
CC stiffness of the hands and shoulders, claw-hand deformity, scoliosis,
CC short stature, coarse facies, and mild intellectual disability.
CC Radiographically, severe dysostosis multiplex of the hip is
CC characteristic and frequently disabling. The clinical diagnosis can be
CC confirmed by finding elevated serum lysosomal enzyme levels and/or
CC decreased lysosomal enzyme levels in cultured fibroblasts.
CC {ECO:0000269|PubMed:10712439, ECO:0000269|PubMed:15060128,
CC ECO:0000269|PubMed:15532026, ECO:0000269|PubMed:19370764,
CC ECO:0000269|PubMed:24316125, ECO:0000269|PubMed:26108976,
CC ECO:0000269|PubMed:27038293}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Defects in GNPTG have been suggested to play a role in
CC susceptibility to persistent stuttering. Stuttering is a common speech
CC disorder characterized by repetitions, prolongations, and interruptions
CC in the flow of speech. {ECO:0000269|PubMed:20147709}.
CC -!- CAUTION: The MLIIIC 'Tyr-142' variant is reported as a 'Val-142'
CC variant due to a typo. {ECO:0000305|PubMed:24316125}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP34456.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF302786; AAG27706.1; -; mRNA.
DR EMBL; AL031709; CAB56184.1; -; Genomic_DNA.
DR EMBL; AK312067; BAG35003.1; -; mRNA.
DR EMBL; CH471112; EAW85668.1; -; Genomic_DNA.
DR EMBL; BC014592; AAH14592.1; -; mRNA.
DR EMBL; AY203933; AAP34456.1; ALT_INIT; mRNA.
DR CCDS; CCDS10436.1; -.
DR PIR; T45062; T45062.
DR RefSeq; NP_115909.1; NM_032520.4.
DR AlphaFoldDB; Q9UJJ9; -.
DR BioGRID; 124144; 92.
DR ComplexPortal; CPX-6841; N-acetylglucosamine-1-phosphotransferase complex.
DR IntAct; Q9UJJ9; 15.
DR MINT; Q9UJJ9; -.
DR STRING; 9606.ENSP00000204679; -.
DR GlyConnect; 2942; 3 N-Linked glycans (1 site).
DR GlyGen; Q9UJJ9; 4 sites, 4 N-linked glycans (1 site), 3 O-linked glycans (2 sites).
DR iPTMnet; Q9UJJ9; -.
DR PhosphoSitePlus; Q9UJJ9; -.
DR BioMuta; GNPTG; -.
DR CPTAC; CPTAC-2710; -.
DR EPD; Q9UJJ9; -.
DR jPOST; Q9UJJ9; -.
DR MassIVE; Q9UJJ9; -.
DR MaxQB; Q9UJJ9; -.
DR PaxDb; Q9UJJ9; -.
DR PeptideAtlas; Q9UJJ9; -.
DR PRIDE; Q9UJJ9; -.
DR ProteomicsDB; 84628; -.
DR Antibodypedia; 1360; 103 antibodies from 16 providers.
DR DNASU; 84572; -.
DR Ensembl; ENST00000204679.9; ENSP00000204679.4; ENSG00000090581.11.
DR GeneID; 84572; -.
DR KEGG; hsa:84572; -.
DR MANE-Select; ENST00000204679.9; ENSP00000204679.4; NM_032520.5; NP_115909.1.
DR UCSC; uc002clm.4; human.
DR CTD; 84572; -.
DR DisGeNET; 84572; -.
DR GeneCards; GNPTG; -.
DR GeneReviews; GNPTG; -.
DR HGNC; HGNC:23026; GNPTG.
DR HPA; ENSG00000090581; Low tissue specificity.
DR MalaCards; GNPTG; -.
DR MIM; 252605; phenotype.
DR MIM; 607838; gene.
DR neXtProt; NX_Q9UJJ9; -.
DR OpenTargets; ENSG00000090581; -.
DR Orphanet; 423470; Mucolipidosis type III gamma.
DR PharmGKB; PA134990433; -.
DR VEuPathDB; HostDB:ENSG00000090581; -.
DR eggNOG; KOG2397; Eukaryota.
DR GeneTree; ENSGT00510000048359; -.
DR HOGENOM; CLU_075705_0_0_1; -.
DR InParanoid; Q9UJJ9; -.
DR OMA; TFGLNNH; -.
DR OrthoDB; 632472at2759; -.
DR PhylomeDB; Q9UJJ9; -.
DR TreeFam; TF329550; -.
DR BRENDA; 2.7.8.17; 2681.
DR PathwayCommons; Q9UJJ9; -.
DR SignaLink; Q9UJJ9; -.
DR BioGRID-ORCS; 84572; 17 hits in 1075 CRISPR screens.
DR ChiTaRS; GNPTG; human.
DR GenomeRNAi; 84572; -.
DR Pharos; Q9UJJ9; Tbio.
DR PRO; PR:Q9UJJ9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9UJJ9; protein.
DR Bgee; ENSG00000090581; Expressed in right adrenal gland cortex and 180 other tissues.
DR ExpressionAtlas; Q9UJJ9; baseline and differential.
DR Genevisible; Q9UJJ9; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0070622; C:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase complex; IPI:ComplexPortal.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0003976; F:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; IEA:Ensembl.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:UniProtKB.
DR GO; GO:0016256; P:N-glycan processing to lysosome; IC:ComplexPortal.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR010506; DMAP1-bd.
DR InterPro; IPR039792; GNPTG.
DR InterPro; IPR039794; Gtb1-like.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR036607; PRKCSH.
DR PANTHER; PTHR12630; PTHR12630; 1.
DR PANTHER; PTHR12630:SF6; PTHR12630:SF6; 1.
DR Pfam; PF13015; PRKCSH_1; 1.
DR SMART; SM01137; DMAP_binding; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
DR PROSITE; PS51914; MRH; 1.
PE 1: Evidence at protein level;
KW Disease variant; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Mucolipidosis; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..305
FT /note="N-acetylglucosamine-1-phosphotransferase subunit
FT gamma"
FT /id="PRO_0000019577"
FT DOMAIN 69..171
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 176..279
FT /note="DMAP1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT REGION 267..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:15532026"
FT DISULFID 71..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 129..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 142..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 245
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VARIANT 5
FT /note="L -> LARL (rare variant; found in individuals
FT suffering from stuttering; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:20147709"
FT /id="VAR_073222"
FT VARIANT 25
FT /note="A -> E (rare variant; found in individuals suffering
FT from stuttering; unknown pathological significance;
FT dbSNP:rs137853826)"
FT /evidence="ECO:0000269|PubMed:20147709"
FT /id="VAR_073223"
FT VARIANT 106
FT /note="G -> S (in MLIIIC; decreased localization to Golgi
FT apparatus; dbSNP:rs137852885)"
FT /evidence="ECO:0000269|PubMed:15060128,
FT ECO:0000269|PubMed:19370764, ECO:0000269|PubMed:27038293"
FT /id="VAR_077164"
FT VARIANT 115
FT /note="Missing (in MLIIIC)"
FT /evidence="ECO:0000269|PubMed:15532026,
FT ECO:0000269|PubMed:19370764"
FT /id="VAR_070815"
FT VARIANT 126
FT /note="G -> S (in MLIIIC; loss of localization to Golgi
FT apparatus; dbSNP:rs775359476)"
FT /evidence="ECO:0000269|PubMed:26108976"
FT /id="VAR_077165"
FT VARIANT 142
FT /note="C -> Y (in MLIIIC; decreased localization to Golgi
FT apparatus)"
FT /evidence="ECO:0000269|PubMed:24316125,
FT ECO:0000269|PubMed:27038293"
FT /id="VAR_070816"
FT VARIANT 230
FT /note="L -> V (rare variant; found in individuals suffering
FT from stuttering; unknown pathological significance;
FT dbSNP:rs137853827)"
FT /evidence="ECO:0000269|PubMed:20147709"
FT /id="VAR_073224"
FT VARIANT 286
FT /note="T -> M (does not affect localization to Golgi
FT apparatus; dbSNP:rs193302860)"
FT /evidence="ECO:0000269|PubMed:19370764,
FT ECO:0000269|PubMed:27038293"
FT /id="VAR_077166"
FT CONFLICT 223
FT /note="Missing (in Ref. 6; AAH14592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 33974 MW; 7774BBC0911DA1C2 CRC64;
MAAGLARLLL LLGLSAGGPA PAGAAKMKVV EEPNAFGVNN PFLPQASRLQ AKRDPSPVSG
PVHLFRLSGK CFSLVESTYK YEFCPFHNVT QHEQTFRWNA YSGILGIWHE WEIANNTFTG
MWMRDGDACR SRSRQSKVEL ACGKSNRLAH VSEPSTCVYA LTFETPLVCH PHALLVYPTL
PEALQRQWDQ VEQDLADELI TPQGHEKLLR TLFEDAGYLK TPEENEPTQL EGGPDSLGFE
TLENCRKAHK ELSKEIKRLK GLLTQHGIPY TRPTETSNLE HLGHETPRAK SPEQLRGDPG
LRGSL
