ID PMGT1_HUMAN Reviewed; 660 AA. AC Q8WZA1; D3DQ16; Q5VST2; Q5VST3; Q9BV55; Q9H9L8; Q9NXF9; Q9NYF7; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 2. DT 27-MAR-2024, entry version 181. DE RecName: Full=Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1; DE Short=POMGnT1; DE EC=2.4.1.- {ECO:0000269|PubMed:11709191, ECO:0000269|PubMed:11742540, ECO:0000269|PubMed:26908613, ECO:0000269|PubMed:27391550, ECO:0000269|PubMed:27493216, ECO:0000269|PubMed:28512129}; DE AltName: Full=UDP-GlcNAc:alpha-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I.2; DE Short=GnT I.2; GN Name=POMGNT1; Synonyms=MGAT1.2; ORFNames=UNQ746/PRO1475; 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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, RP PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY, BIOPHYSICOCHEMICAL PROPERTIES, RP TISSUE SPECIFICITY, VARIANTS MDDGA3 ARG-493 AND ASN-550, VARIANT VAL-623, RP AND MUTAGENESIS OF 1-MET--ILE-65. RC TISSUE=Brain; RX PubMed=11709191; DOI=10.1016/s1534-5807(01)00070-3; RA Yoshida A., Kobayashi K., Manya H., Taniguchi K., Kano H., Mizuno M., RA Inazu T., Mitsuhashi H., Takahashi S., Takeuchi M., Herrmann R., Straub V., RA Talim B., Voit T., Topaloglu H., Toda T., Endo T.; RT "Muscular dystrophy and neuronal migration disorder caused by mutations in RT a glycosyltransferase, POMGnT1."; RL Dev. Cell 1:717-724(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MDDGA3 LYS-223 AND RP TYR-269, AND VARIANT VAL-623. RC TISSUE=Brain; RX PubMed=12588800; DOI=10.1093/hmg/ddg043; RA Taniguchi K., Kobayashi K., Saito K., Yamanouchi H., Ohnuma A., RA Hayashi Y.K., Manya H., Jin D.K., Lee M., Parano E., Falsaperla R., RA Pavone P., Coster R.V., Talim B., Steinbrecher A., Straub V., Nishino I., RA Topaloglu H., Voit T., Endo T., Toda T.; RT "Worldwide distribution and broader clinical spectrum of muscle-eye-brain RT disease."; RL Hum. Mol. Genet. 12:527-534(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-623. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP VAL-623. 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-623. 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-250 RP AND VAL-623. RC TISSUE=Placenta; 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 84-660 (ISOFORM 1), FUNCTION, CATALYTIC RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY, AND RP VARIANT VAL-623. RC TISSUE=Brain; RX PubMed=11742540; DOI=10.1042/0264-6021:3610153; RA Zhang W., Betel D., Schachter H.; RT "Cloning and expression of a novel UDP-GlcNAc:alpha-D-mannoside beta-1,2-N- RT acetylglucosaminyltransferase homologous to UDP-GlcNAc:alpha-3-D-mannoside RT beta-1,2-N-acetylglucosaminyltransferase I."; RL Biochem. J. 361:153-162(2002). RN [9] RP SUBCELLULAR LOCATION, AND INTERACTION WITH FKTN. RX PubMed=17034757; DOI=10.1016/j.bbrc.2006.09.129; RA Xiong H., Kobayashi K., Tachikawa M., Manya H., Takeda S., Chiyonobu T., RA Fujikake N., Wang F., Nishimoto A., Morris G.E., Nagai Y., Kanagawa M., RA Endo T., Toda T.; RT "Molecular interaction between fukutin and POMGnT1 in the glycosylation RT pathway of alpha-dystroglycan."; RL Biochem. Biophys. Res. Commun. 350:935-941(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=28512129; DOI=10.1074/jbc.m117.794487; RA Larsen I.S.B., Narimatsu Y., Joshi H.J., Yang Z., Harrison O.J., Brasch J., RA Shapiro L., Honig B., Vakhrushev S.Y., Clausen H., Halim A.; RT "Mammalian O-mannosylation of cadherins and plexins is independent of RT protein O-mannosyltransferases 1 and 2."; RL J. Biol. Chem. 292:11586-11598(2017). RN [13] RP CHARACTERIZATION OF VARIANTS MDDGA3 LYS-223; TYR-269 AND ARG-493, CATALYTIC RP ACTIVITY, AND COFACTOR. RX PubMed=12788071; DOI=10.1016/s0006-291x(03)00924-0; RA Manya H., Sakai K., Kobayashi K., Taniguchi K., Kawakita M., Toda T., RA Endo T.; RT "Loss-of-function of an N-acetylglucosaminyltransferase, POMGnT1, in RT muscle-eye-brain disease."; RL Biochem. Biophys. Res. Commun. 306:93-97(2003). RN [14] RP IDENTIFICATION OF CATALYTIC DOMAIN, AND CHARACTERIZATION OF VARIANTS MDDGA3 RP LYS-223 AND TYR-269. RX PubMed=15207699; DOI=10.1016/j.bbrc.2004.05.129; RA Akasaka-Manya K., Manya H., Kobayashi K., Toda T., Endo T.; RT "Structure-function analysis of human protein O-linked mannose beta1,2-N- RT acetylglucosaminyltransferase 1, POMGnT1."; RL Biochem. Biophys. Res. Commun. 320:39-44(2004). RN [15] {ECO:0007744|PDB:5GGF, ECO:0007744|PDB:5GGG, ECO:0007744|PDB:5GGI, ECO:0007744|PDB:5GGJ, ECO:0007744|PDB:5GGK, ECO:0007744|PDB:5GGL, ECO:0007744|PDB:5GGN, ECO:0007744|PDB:5GGO, ECO:0007744|PDB:5GGP} RP X-RAY CRYSTALLOGRAPHY (1.21 ANGSTROMS) OF 92-250 IN COMPLEXES WITH RP CARBOHYDRATE; DAG1 PEPTIDE; MANGANESE; MANNOSE AND UDP, DISULFIDE BONDS, RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, DOMAIN, AND MUTAGENESIS OF RP ARG-129; ASP-179; ARG-207; ASP-474; MET-481; ASN-507 AND TRP-600. RX PubMed=27493216; DOI=10.1073/pnas.1525545113; RA Kuwabara N., Manya H., Yamada T., Tateno H., Kanagawa M., Kobayashi K., RA Akasaka-Manya K., Hirose Y., Mizuno M., Ikeguchi M., Toda T., RA Hirabayashi J., Senda T., Endo T., Kato R.; RT "Carbohydrate-binding domain of the POMGnT1 stem region modulates O- RT mannosylation sites of alpha-dystroglycan."; RL Proc. Natl. Acad. Sci. U.S.A. 113:9280-9285(2016). RN [16] RP VARIANTS MDDGA3 HIS-265; GLN-311 AND CYS-442. RX PubMed=15236414; DOI=10.1002/ana.20172; RA Vervoort V.S., Holden K.R., Ukadike K.C., Collins J.S., Saul R.A., RA Srivastava A.K.; RT "POMGnT1 gene alterations in a family with neurological abnormalities."; RL Ann. Neurol. 56:143-148(2004). RN [17] RP VARIANTS MDDGA3 SER-425 AND TYR-490. RX PubMed=15466003; DOI=10.1136/jmg.2004.020701; RA Diesen C., Saarinen A., Pihko H., Rosenlew C., Cormand B., Dobyns W.B., RA Dieguez J., Valanne L., Joensuu T., Lehesjoki A.-E.; RT "POMGnT1 mutation and phenotypic spectrum in muscle-eye-brain disease."; RL J. Med. Genet. 41:E115-E115(2004). RN [18] RP VARIANTS MDDGA3 ARG-198 AND TYR-490, AND VARIANT MDDGB3 GLN-311. RX PubMed=17030669; DOI=10.1001/archneur.63.10.1491; RA Biancheri R., Bertini E., Falace A., Pedemonte M., Rossi A., D'Amico A., RA Scapolan S., Bergamino L., Petrini S., Cassandrini D., Broda P., RA Manfredi M., Zara F., Santorelli F.M., Minetti C., Bruno C.; RT "POMGnT1 mutations in congenital muscular dystrophy: genotype-phenotype RT correlation and expanded clinical spectrum."; RL Arch. Neurol. 63:1491-1495(2006). RN [19] RP VARIANTS MDDGA3 PRO-176; HIS-367 AND HIS-427, AND VARIANT MDDGB3 TYR-490. RX PubMed=19067344; DOI=10.1002/ana.21482; RA Clement E., Mercuri E., Godfrey C., Smith J., Robb S., Kinali M., RA Straub V., Bushby K., Manzur A., Talim B., Cowan F., Quinlivan R., RA Klein A., Longman C., McWilliam R., Topaloglu H., Mein R., Abbs S., RA North K., Barkovich A.J., Rutherford M., Muntoni F.; RT "Brain involvement in muscular dystrophies with defective dystroglycan RT glycosylation."; RL Ann. Neurol. 64:573-582(2008). RN [20] RP VARIANT MDDGC3 ASN-556, AND CHARACTERIZATION OF VARIANT MDDGC3 ASN-556. RX PubMed=18195152; DOI=10.1001/archneurol.2007.2; RA Clement E.M., Godfrey C., Tan J., Brockington M., Torelli S., Feng L., RA Brown S.C., Jimenez-Mallebrera C., Sewry C.A., Longman C., Mein R., RA Abbs S., Vajsar J., Schachter H., Muntoni F.; RT "Mild POMGnT1 mutations underlie a novel limb-girdle muscular dystrophy RT variant."; RL Arch. Neurol. 65:137-141(2008). RN [21] RP VARIANT MDDGB3 PRO-605. RX PubMed=19299310; DOI=10.1212/01.wnl.0000346518.68110.60; RA Mercuri E., Messina S., Bruno C., Mora M., Pegoraro E., Comi G.P., RA D'Amico A., Aiello C., Biancheri R., Berardinelli A., Boffi P., RA Cassandrini D., Laverda A., Moggio M., Morandi L., Moroni I., Pane M., RA Pezzani R., Pichiecchio A., Pini A., Minetti C., Mongini T., Mottarelli E., RA Ricci E., Ruggieri A., Saredi S., Scuderi C., Tessa A., Toscano A., RA Tortorella G., Trevisan C.P., Uggetti C., Vasco G., Santorelli F.M., RA Bertini E.; RT "Congenital muscular dystrophies with defective glycosylation of RT dystroglycan: a population study."; RL Neurology 72:1802-1809(2009). RN [22] RP INVOLVEMENT IN RP76, VARIANTS RP76 LYS-156; SER-287 AND ALA-502, RP CHARACTERIZATION OF VARIANTS RP76 LYS-156 AND SER-287, FUNCTION, CATALYTIC RP ACTIVITY, AND PATHWAY. RX PubMed=26908613; DOI=10.1093/hmg/ddw022; RA Xu M., Yamada T., Sun Z., Eblimit A., Lopez I., Wang F., Manya H., Xu S., RA Zhao L., Li Y., Kimchi A., Sharon D., Sui R., Endo T., Koenekoop R.K., RA Chen R.; RT "Mutations in POMGNT1 cause non-syndromic retinitis pigmentosa."; RL Hum. Mol. Genet. 25:1479-1488(2016). RN [23] RP INVOLVEMENT IN RP76, VARIANT RP76 ARG-120, CHARACTERIZATION OF VARIANT RP76 RP ARG-120, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=27391550; DOI=10.1167/iovs.16-19463; RA Wang N.H., Chen S.J., Yang C.F., Chen H.W., Chuang H.P., Lu Y.H., RA Chen C.H., Wu J.Y., Niu D.M., Chen Y.T.; RT "Homozygosity Mapping and Whole-Genome Sequencing Links a Missense Mutation RT in POMGNT1 to Autosomal Recessive Retinitis Pigmentosa."; RL Invest. Ophthalmol. Vis. Sci. 57:3601-3609(2016). CC -!- FUNCTION: Participates in O-mannosyl glycosylation by catalyzing the CC addition of N-acetylglucosamine to O-linked mannose on glycoproteins CC (PubMed:11709191, PubMed:27493216, PubMed:28512129). Catalyzes the CC synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha- CC dystroglycan and other O-mannosylated proteins, providing the necessary CC basis for the addition of further carbohydrate moieties CC (PubMed:11709191, PubMed:27493216). Is specific for alpha linked CC terminal mannose and does not have MGAT3, MGAT4, MGAT5, MGAT7 or MGAT8 CC activity. {ECO:0000269|PubMed:11709191, ECO:0000269|PubMed:11742540, CC ECO:0000269|PubMed:26908613, ECO:0000269|PubMed:27391550, CC ECO:0000269|PubMed:27493216, ECO:0000269|PubMed:28512129}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + UDP-N-acetyl- CC alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha- CC D-mannosyl)-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54128, CC Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:13802, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137323, CC ChEBI:CHEBI:138067; Evidence={ECO:0000269|PubMed:11709191, CC ECO:0000269|PubMed:11742540, ECO:0000269|PubMed:12788071, CC ECO:0000269|PubMed:26908613, ECO:0000269|PubMed:27391550, CC ECO:0000269|PubMed:27493216, ECO:0000269|PubMed:28512129}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:27493216, ECO:0000305|PubMed:12788071}; CC Note=The manganese ion interacts primarily with the substrate UDP-N- CC acetylglucosamine. {ECO:0000269|PubMed:27493216}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.85 mM for mannosylpeptide {ECO:0000269|PubMed:11709191, CC ECO:0000269|PubMed:11742540}; CC KM=0.73 mM for UDP-GlcNAc {ECO:0000269|PubMed:11709191, CC ECO:0000269|PubMed:11742540}; CC KM=30 mM for Man(alpha1-)O-benzyl {ECO:0000269|PubMed:11709191, CC ECO:0000269|PubMed:11742540}; CC KM=12 mM for CYA[Man(alpha1-)O-T]AV {ECO:0000269|PubMed:11709191, CC ECO:0000269|PubMed:11742540}; CC pH dependence: CC Optimum pH is 6.0. {ECO:0000269|PubMed:11709191, CC ECO:0000269|PubMed:11742540}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:11709191, ECO:0000269|PubMed:11742540, CC ECO:0000269|PubMed:26908613, ECO:0000269|PubMed:27391550, CC ECO:0000269|PubMed:27493216}. CC -!- SUBUNIT: Interacts with DAG1 (via O-linked mannose moiety) CC (PubMed:27493216). Interacts (via transmembrane domain) with FKTN; the CC interaction is direct and is required for normal location in Golgi CC membranes (PubMed:17034757). {ECO:0000269|PubMed:17034757, CC ECO:0000269|PubMed:27493216}. CC -!- INTERACTION: CC Q8WZA1; P04233-2: CD74; NbExp=3; IntAct=EBI-3912424, EBI-12222807; CC Q8WZA1; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-3912424, EBI-1045797; CC Q8WZA1; Q5JRM2: CXorf66; NbExp=3; IntAct=EBI-3912424, EBI-12823659; CC Q8WZA1; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-3912424, EBI-781551; CC Q8WZA1; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-3912424, EBI-739832; CC Q8WZA1; Q9H5K3: POMK; NbExp=2; IntAct=EBI-3912424, EBI-11337900; CC Q8WZA1; Q9Y2B1: RXYLT1; NbExp=4; IntAct=EBI-3912424, EBI-3914763; CC Q8WZA1; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-3912424, EBI-10982110; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:17034757, ECO:0000303|PubMed:11709191}; Single-pass CC type II membrane protein {ECO:0000305|PubMed:11709191}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8WZA1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WZA1-2; Sequence=VSP_054029; CC -!- TISSUE SPECIFICITY: Constitutively expressed. An additional weaker band CC is also detected in spinal cord, lymph node, and trachea. Expressed CC especially in astrocytes. Also expressed in immature and mature CC neurons. {ECO:0000269|PubMed:11709191, ECO:0000269|PubMed:11742540}. CC -!- DOMAIN: Amino acid residues between 299-311 are important for both CC protein expression and enzymatic activity. The minimal catalytic domain CC is located between positions 299-651. Single amino acid substitutions CC in the stem domain from MEB patients abolished the activity of the CC membrane-bound form but not the soluble form. This suggests that the CC stem domain of the soluble form is unnecessary for activity, but that CC some amino acids play a crucial role in the membrane-bound form. CC {ECO:0000269|PubMed:15207699}. CC -!- DOMAIN: The GG-type lectin domain is known as the stem domain in CC POMGnT1. It mediates specific interaction with beta-linked N- CC acetylglucosamine moieties of O-glycosylated proteins. It also CC interacts with its product, N-acetyl-beta-D-glucosaminyl-(1->2)-O- CC alpha-D-mannosylprotein. {ECO:0000269|PubMed:27493216}. CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain CC and eye anomalies A3 (MDDGA3) [MIM:253280]: An autosomal recessive CC disorder characterized by congenital muscular dystrophy, ocular CC abnormalities, cobblestone lissencephaly, and cerebellar and pontine CC hypoplasia. Patients present severe congenital myopia, congenital CC glaucoma, pallor of the optic disks, retinal hypoplasia, intellectual CC disability, hydrocephalus, abnormal electroencephalograms, generalized CC muscle weakness and myoclonic jerks. Included diseases are the more CC severe Walker-Warburg syndrome and the slightly less severe muscle-eye- CC brain disease. {ECO:0000269|PubMed:11709191, CC ECO:0000269|PubMed:12588800, ECO:0000269|PubMed:12788071, CC ECO:0000269|PubMed:15207699, ECO:0000269|PubMed:15236414, CC ECO:0000269|PubMed:15466003, ECO:0000269|PubMed:17030669, CC ECO:0000269|PubMed:19067344}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with impaired CC intellectual development B3 (MDDGB3) [MIM:613151]: An autosomal CC recessive disorder characterized by congenital muscular dystrophy CC associated with intellectual disability and mild structural brain CC abnormalities. Clinical features include intellectual disability, white CC matter changes, cerebellar cysts, pontine hypoplasia, myopia, optic CC atrophy, decreased alpha-dystroglycan on muscle biopsy and increased CC serum creatine kinase. {ECO:0000269|PubMed:17030669, CC ECO:0000269|PubMed:19067344, ECO:0000269|PubMed:19299310}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C3 (MDDGC3) CC [MIM:613157]: A rare form of limb-girdle muscular dystrophy with normal CC cognition. Muscle biopsy shows dystrophic changes with variable CC staining for glycosylated alpha-dystroglycan. CC {ECO:0000269|PubMed:18195152}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Retinitis pigmentosa 76 (RP76) [MIM:617123]: A form of CC retinitis pigmentosa, a retinal dystrophy belonging to the group of CC pigmentary retinopathies. Retinitis pigmentosa is characterized by CC retinal pigment deposits visible on fundus examination and primary loss CC of rod photoreceptor cells followed by secondary loss of cone CC photoreceptors. Patients typically have night vision blindness and loss CC of midperipheral visual field. As their condition progresses, they lose CC their far peripheral visual field and eventually central vision as CC well. RP76 inheritance is autosomal recessive. CC {ECO:0000269|PubMed:26908613, ECO:0000269|PubMed:27391550}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the glycosyltransferase 13 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB14207.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Protein CC O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_559"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB057356; BAB71960.1; -; mRNA. DR EMBL; AY358592; AAQ88955.1; -; mRNA. DR EMBL; AK000284; BAA91053.1; -; mRNA. DR EMBL; AK022727; BAB14207.1; ALT_INIT; mRNA. DR EMBL; AK056186; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL672043; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX06932.1; -; Genomic_DNA. DR EMBL; CH471059; EAX06933.1; -; Genomic_DNA. DR EMBL; CH471059; EAX06935.1; -; Genomic_DNA. DR EMBL; BC001471; AAH01471.1; -; mRNA. DR EMBL; AF250859; AAF71270.2; -; mRNA. DR CCDS; CCDS531.1; -. [Q8WZA1-1] DR CCDS; CCDS57995.1; -. [Q8WZA1-2] DR RefSeq; NP_060209.3; NM_017739.3. [Q8WZA1-1] DR RefSeq; XP_006710819.1; XM_006710756.1. [Q8WZA1-2] DR RefSeq; XP_016857179.1; XM_017001690.1. [Q8WZA1-1] DR PDB; 5GGF; X-ray; 2.49 A; A/B/C=92-660. DR PDB; 5GGG; X-ray; 3.00 A; A=92-660. DR PDB; 5GGI; X-ray; 2.60 A; A/B=92-660. DR PDB; 5GGJ; X-ray; 1.42 A; A/B=92-250. DR PDB; 5GGK; X-ray; 1.30 A; A/B=92-250. DR PDB; 5GGL; X-ray; 1.27 A; A/B=92-250. DR PDB; 5GGN; X-ray; 1.21 A; A/B=92-250. DR PDB; 5GGO; X-ray; 1.50 A; A/B=92-250. DR PDB; 5GGP; X-ray; 1.60 A; A/B=92-250. DR PDB; 5XFC; X-ray; 1.40 A; A/B=92-250. DR PDBsum; 5GGF; -. DR PDBsum; 5GGG; -. DR PDBsum; 5GGI; -. DR PDBsum; 5GGJ; -. DR PDBsum; 5GGK; -. DR PDBsum; 5GGL; -. DR PDBsum; 5GGN; -. DR PDBsum; 5GGO; -. DR PDBsum; 5GGP; -. DR PDBsum; 5XFC; -. DR AlphaFoldDB; Q8WZA1; -. DR SMR; Q8WZA1; -. DR BioGRID; 120763; 115. DR IntAct; Q8WZA1; 27. DR MINT; Q8WZA1; -. DR STRING; 9606.ENSP00000361060; -. DR ChEMBL; CHEMBL2321629; -. DR CAZy; GT13; Glycosyltransferase Family 13. DR iPTMnet; Q8WZA1; -. DR PhosphoSitePlus; Q8WZA1; -. DR SwissPalm; Q8WZA1; -. DR BioMuta; POMGNT1; -. DR DMDM; 311033411; -. DR EPD; Q8WZA1; -. DR jPOST; Q8WZA1; -. DR MassIVE; Q8WZA1; -. DR MaxQB; Q8WZA1; -. DR PaxDb; 9606-ENSP00000361060; -. DR PeptideAtlas; Q8WZA1; -. DR ProteomicsDB; 65277; -. DR ProteomicsDB; 75242; -. [Q8WZA1-1] DR Pumba; Q8WZA1; -. DR Antibodypedia; 32757; 117 antibodies from 24 providers. DR DNASU; 55624; -. DR Ensembl; ENST00000371984.8; ENSP00000361052.3; ENSG00000085998.15. [Q8WZA1-1] DR Ensembl; ENST00000371992.1; ENSP00000361060.1; ENSG00000085998.15. [Q8WZA1-2] DR Ensembl; ENST00000396420.8; ENSP00000379698.4; ENSG00000085998.15. [Q8WZA1-1] DR Ensembl; ENST00000686737.1; ENSP00000508736.1; ENSG00000085998.15. [Q8WZA1-1] DR Ensembl; ENST00000687683.1; ENSP00000508522.1; ENSG00000085998.15. [Q8WZA1-1] DR Ensembl; ENST00000690678.1; ENSP00000508703.1; ENSG00000085998.15. [Q8WZA1-1] DR GeneID; 55624; -. DR KEGG; hsa:55624; -. DR MANE-Select; ENST00000371984.8; ENSP00000361052.3; NM_017739.4; NP_060209.4. DR UCSC; uc001cpe.4; human. [Q8WZA1-1] DR AGR; HGNC:19139; -. DR CTD; 55624; -. DR DisGeNET; 55624; -. DR GeneCards; POMGNT1; -. DR HGNC; HGNC:19139; POMGNT1. DR HPA; ENSG00000085998; Low tissue specificity. DR MalaCards; POMGNT1; -. DR MIM; 253280; phenotype. DR MIM; 606822; gene. DR MIM; 613151; phenotype. DR MIM; 613157; phenotype. DR MIM; 617123; phenotype. DR neXtProt; NX_Q8WZA1; -. DR OpenTargets; ENSG00000085998; -. DR Orphanet; 370959; Congenital muscular dystrophy with cerebellar involvement. DR Orphanet; 588; Muscle-eye-brain disease. DR Orphanet; 206564; POMGNT1-related limb-girdle muscular dystrophy R15. DR Orphanet; 791; Retinitis pigmentosa. DR Orphanet; 899; Walker-Warburg syndrome. DR PharmGKB; PA142671161; -. DR VEuPathDB; HostDB:ENSG00000085998; -. DR eggNOG; ENOG502QSG3; Eukaryota. DR GeneTree; ENSGT00530000063632; -. DR HOGENOM; CLU_024847_0_0_1; -. DR InParanoid; Q8WZA1; -. DR OMA; NYETEIH; -. DR OrthoDB; 5382840at2759; -. DR PhylomeDB; Q8WZA1; -. DR TreeFam; TF320555; -. DR BioCyc; MetaCyc:ENSG00000085998-MONOMER; -. DR BRENDA; 2.4.1.312; 2681. DR PathwayCommons; Q8WZA1; -. DR Reactome; R-HSA-5083628; Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3. DR Reactome; R-HSA-5173105; O-linked glycosylation. DR SignaLink; Q8WZA1; -. DR SIGNOR; Q8WZA1; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 55624; 10 hits in 1153 CRISPR screens. DR ChiTaRS; POMGNT1; human. DR GeneWiki; POMGNT1; -. DR GenomeRNAi; 55624; -. DR Pharos; Q8WZA1; Tbio. DR PRO; PR:Q8WZA1; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8WZA1; Protein. DR Bgee; ENSG00000085998; Expressed in apex of heart and 187 other cell types or tissues. DR ExpressionAtlas; Q8WZA1; baseline and differential. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IMP:UniProtKB. DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:UniProtKB. DR GO; GO:0047223; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; IDA:MGI. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl. DR GO; GO:0021542; P:dentate gyrus development; IEA:Ensembl. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0051674; P:localization of cell; IEA:Ensembl. DR GO; GO:0042552; P:myelination; IEA:Ensembl. DR GO; GO:0016266; P:O-glycan processing; IDA:UniProtKB. DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI. DR GO; GO:0035269; P:protein O-linked mannosylation; IEA:Ensembl. DR GO; GO:0150103; P:reactive gliosis; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl. DR CDD; cd02514; GT13_GLCNAC-TI; 1. DR CDD; cd13937; PANDER_GnT-1_2_like; 1. DR InterPro; IPR004139; Glyco_trans_13. DR InterPro; IPR039477; ILEI/PANDER_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR039474; POMGNT1_PANDER-like. DR PANTHER; PTHR46396; PROTEIN O-LINKED-MANNOSE BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE 1; 1. DR PANTHER; PTHR46396:SF1; PROTEIN O-LINKED-MANNOSE BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE 1; 1. DR Pfam; PF03071; GNT-I; 1. DR Pfam; PF15711; ILEI; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR PROSITE; PS52031; GG_LECTIN; 1. DR Genevisible; Q8WZA1; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Congenital muscular dystrophy; KW Disease variant; Disulfide bond; Dystroglycanopathy; Glycosyltransferase; KW Golgi apparatus; Lectin; Limb-girdle muscular dystrophy; Lissencephaly; KW Manganese; Membrane; Metal-binding; Phosphoprotein; Reference proteome; KW Retinitis pigmentosa; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..660 FT /note="Protein O-linked-mannose beta-1,2-N- FT acetylglucosaminyltransferase 1" FT /id="PRO_0000191390" FT TOPO_DOM 1..37 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 38..58 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 59..660 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:11709191" FT DOMAIN 97..258 FT /note="GG-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01375" FT REGION 68..96 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 300..646 FT /note="Catalytic" FT /evidence="ECO:0000269|PubMed:15207699, FT ECO:0000269|PubMed:27493216" FT REGION 473..481 FT /note="Interaction with O-glycosylated substrate FT glycoprotein" FT /evidence="ECO:0000269|PubMed:27493216" FT REGION 506..512 FT /note="Interaction with O-glycosylated substrate FT glycoprotein" FT /evidence="ECO:0000269|PubMed:27493216" FT REGION 600..605 FT /note="Interaction with O-glycosylated substrate FT glycoprotein" FT /evidence="ECO:0000269|PubMed:27493216" FT REGION 637..660 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 78..96 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 129 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000269|PubMed:27493216" FT BINDING 179 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000269|PubMed:27493216" FT BINDING 207 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000269|PubMed:27493216" FT BINDING 307..311 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000305|PubMed:27493216, FT ECO:0007744|PDB:5GGI" FT BINDING 338 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000305|PubMed:27493216, FT ECO:0007744|PDB:5GGI" FT BINDING 371 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000305|PubMed:27493216, FT ECO:0007744|PDB:5GGI" FT BINDING 394..395 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000305|PubMed:27493216, FT ECO:0007744|PDB:5GGI" FT BINDING 395 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:27493216, FT ECO:0007744|PDB:5GGI" FT BINDING 500 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:27493216, FT ECO:0007744|PDB:5GGI" FT BINDING 506..507 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000305|PubMed:27493216, FT ECO:0007744|PDB:5GGI" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT DISULFID 254..281 FT /evidence="ECO:0000269|PubMed:27493216, FT ECO:0007744|PDB:5GGF, ECO:0007744|PDB:5GGG, FT ECO:0007744|PDB:5GGI" FT DISULFID 269..279 FT /evidence="ECO:0000269|PubMed:27493216, FT ECO:0007744|PDB:5GGF, ECO:0007744|PDB:5GGG, FT ECO:0007744|PDB:5GGI" FT DISULFID 421..490 FT /evidence="ECO:0000269|PubMed:27493216, FT ECO:0007744|PDB:5GGF, ECO:0007744|PDB:5GGG, FT ECO:0007744|PDB:5GGI" FT DISULFID 562..596 FT /evidence="ECO:0000269|PubMed:27493216, FT ECO:0007744|PDB:5GGF, ECO:0007744|PDB:5GGG, FT ECO:0007744|PDB:5GGI" FT VAR_SEQ 624..660 FT /note="VGVPASPYSVKKPPSVTPIFLEPPPKEEGAPGAPEQT -> SEEATLSHPNF FT PGATPKGGGSPRSPRTDMRPPPGPCGAGPGSESNLFIDCPEGLENRPNLEGLDFFLGWN FT AALRVGLALTQETAVPNPWTGPAGAHMLTQTHSETLRHWTRPPLSLLFVQISKAG (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054029" FT VARIANT 120 FT /note="L -> R (in RP76; no effect on protein abundance; FT reduced acetylglucosaminyltransferase activity; FT dbSNP:rs886037949)" FT /evidence="ECO:0000269|PubMed:27391550" FT /id="VAR_077054" FT VARIANT 156 FT /note="E -> K (in RP76; reduced FT acetylglucosaminyltransferase activity; dbSNP:rs886037947)" FT /evidence="ECO:0000269|PubMed:26908613" FT /id="VAR_076524" FT VARIANT 176 FT /note="T -> P (in MDDGA3; dbSNP:rs386834030)" FT /evidence="ECO:0000269|PubMed:19067344" FT /id="VAR_065021" FT VARIANT 198 FT /note="S -> R (in MDDGA3; dbSNP:rs386834032)" FT /evidence="ECO:0000269|PubMed:17030669" FT /id="VAR_065022" FT VARIANT 223 FT /note="E -> K (in MDDGA3; specific activity abolished in FT the membrane bound form but not the soluble form; FT dbSNP:rs386834036)" FT /evidence="ECO:0000269|PubMed:12588800, FT ECO:0000269|PubMed:12788071, ECO:0000269|PubMed:15207699" FT /id="VAR_023101" FT VARIANT 250 FT /note="E -> V (in dbSNP:rs17855359)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_030645" FT VARIANT 265 FT /note="R -> H (in MDDGA3; uncertain significance; FT dbSNP:rs386834010)" FT /evidence="ECO:0000269|PubMed:15236414" FT /id="VAR_023102" FT VARIANT 269 FT /note="C -> Y (in MDDGA3; specific activity abolished of FT the membrane bound form but not the soluble form; FT dbSNP:rs386834037)" FT /evidence="ECO:0000269|PubMed:12588800, FT ECO:0000269|PubMed:12788071, ECO:0000269|PubMed:15207699" FT /id="VAR_023103" FT VARIANT 287 FT /note="I -> S (in RP76; reduced FT acetylglucosaminyltransferase activity; dbSNP:rs200863680)" FT /evidence="ECO:0000269|PubMed:26908613" FT /id="VAR_076525" FT VARIANT 311 FT /note="R -> Q (in MDDGA3 and MDDGB3; dbSNP:rs193919336)" FT /evidence="ECO:0000269|PubMed:15236414, FT ECO:0000269|PubMed:17030669" FT /id="VAR_023104" FT VARIANT 367 FT /note="R -> H (in MDDGA3; dbSNP:rs762972459)" FT /evidence="ECO:0000269|PubMed:19067344" FT /id="VAR_065023" FT VARIANT 425 FT /note="W -> S (in MDDGA3; dbSNP:rs386834011)" FT /evidence="ECO:0000269|PubMed:15466003" FT /id="VAR_023105" FT VARIANT 427 FT /note="D -> H (in MDDGA3)" FT /evidence="ECO:0000269|PubMed:19067344" FT /id="VAR_065024" FT VARIANT 442 FT /note="R -> C (in MDDGA3; dbSNP:rs28940869)" FT /evidence="ECO:0000269|PubMed:15236414" FT /id="VAR_023106" FT VARIANT 490 FT /note="C -> Y (in MDDGA3 and MDDGB3; dbSNP:rs267606960)" FT /evidence="ECO:0000269|PubMed:15466003, FT ECO:0000269|PubMed:17030669, ECO:0000269|PubMed:19067344" FT /id="VAR_023107" FT VARIANT 493 FT /note="P -> R (in MDDGA3; specific activity abolished; FT dbSNP:rs28942068)" FT /evidence="ECO:0000269|PubMed:11709191, FT ECO:0000269|PubMed:12788071" FT /id="VAR_023108" FT VARIANT 502 FT /note="G -> A (in RP76; dbSNP:rs886037948)" FT /evidence="ECO:0000269|PubMed:26908613" FT /id="VAR_076526" FT VARIANT 504 FT /note="V -> I (in dbSNP:rs17102066)" FT /id="VAR_030646" FT VARIANT 550 FT /note="S -> N (in MDDGA3; dbSNP:rs193919335)" FT /evidence="ECO:0000269|PubMed:11709191" FT /id="VAR_023109" FT VARIANT 556 FT /note="D -> N (in MDDGC3; normal enzyme activity but FT altered kinetic properties; dbSNP:rs74374973)" FT /evidence="ECO:0000269|PubMed:18195152" FT /id="VAR_065025" FT VARIANT 605 FT /note="R -> P (in MDDGB3; dbSNP:rs267606962)" FT /evidence="ECO:0000269|PubMed:19299310" FT /id="VAR_065026" FT VARIANT 623 FT /note="M -> V (in dbSNP:rs6659553)" FT /evidence="ECO:0000269|PubMed:11709191, FT ECO:0000269|PubMed:11742540, ECO:0000269|PubMed:12588800, FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6" FT /id="VAR_023110" FT MUTAGEN 1..65 FT /note="Missing: Gives rise to a soluble form." FT /evidence="ECO:0000269|PubMed:11709191" FT MUTAGEN 129 FT /note="R->A: Decreased protein stability. Decreased enzyme FT activity." FT /evidence="ECO:0000269|PubMed:27493216" FT MUTAGEN 179 FT /note="D->A: Moderately increased enzyme activity. FT Decreased affinity for N-acetylglucosamine." FT /evidence="ECO:0000269|PubMed:27493216" FT MUTAGEN 207 FT /note="R->A: Decreased enzyme activity. Impairs protein FT stability." FT /evidence="ECO:0000269|PubMed:27493216" FT MUTAGEN 473 FT /note="W->A: Abolishes in vitro enzyme activity; when FT associated with A-477." FT /evidence="ECO:0000269|PubMed:27493216" FT MUTAGEN 474 FT /note="D->A: Nearly abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:27493216" FT MUTAGEN 477 FT /note="M->A: Abolishes in vitro enzyme activity; when FT associated with A-473." FT /evidence="ECO:0000269|PubMed:27493216" FT MUTAGEN 481 FT /note="M->A: Decreased enzyme activity." FT /evidence="ECO:0000269|PubMed:27493216" FT MUTAGEN 507 FT /note="N->A: Abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:27493216" FT MUTAGEN 600 FT /note="W->A: Abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:27493216" FT CONFLICT 636 FT /note="P -> L (in Ref. 3; BAA91053)" FT /evidence="ECO:0000305" FT STRAND 98..108 FT /evidence="ECO:0007829|PDB:5GGN" FT STRAND 110..114 FT /evidence="ECO:0007829|PDB:5GGN" FT STRAND 117..122 FT /evidence="ECO:0007829|PDB:5GGN" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:5GGP" FT STRAND 130..136 FT /evidence="ECO:0007829|PDB:5GGN" FT TURN 138..140 FT /evidence="ECO:0007829|PDB:5GGN" FT STRAND 143..149 FT /evidence="ECO:0007829|PDB:5GGN" FT HELIX 156..166 FT /evidence="ECO:0007829|PDB:5GGN" FT STRAND 171..179 FT /evidence="ECO:0007829|PDB:5GGN" FT HELIX 187..195 FT /evidence="ECO:0007829|PDB:5GGN" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:5GGN" FT STRAND 209..215 FT /evidence="ECO:0007829|PDB:5GGN" FT STRAND 220..226 FT /evidence="ECO:0007829|PDB:5GGN" FT STRAND 229..233 FT /evidence="ECO:0007829|PDB:5GGG" FT STRAND 238..245 FT /evidence="ECO:0007829|PDB:5GGN" FT HELIX 249..252 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 261..269 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 276..279 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:5GGF" FT TURN 298..301 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 304..308 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 312..323 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 333..339 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 342..350 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 354..358 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 364..382 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 387..393 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 396..398 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 402..415 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 419..424 FT /evidence="ECO:0007829|PDB:5GGF" FT TURN 431..433 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 440..445 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 449..454 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 455..460 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 463..465 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 475..480 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 482..485 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 489..500 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 504..507 FT /evidence="ECO:0007829|PDB:5GGI" FT HELIX 510..516 FT /evidence="ECO:0007829|PDB:5GGI" FT TURN 517..519 FT /evidence="ECO:0007829|PDB:5GGI" FT HELIX 533..536 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 538..551 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 552..554 FT /evidence="ECO:0007829|PDB:5GGG" FT HELIX 564..566 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 574..583 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 588..596 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 606..608 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 611..616 FT /evidence="ECO:0007829|PDB:5GGF" FT STRAND 619..627 FT /evidence="ECO:0007829|PDB:5GGF" FT HELIX 630..634 FT /evidence="ECO:0007829|PDB:5GGF" FT CONFLICT Q8WZA1-2:636 FT /note="G -> K (in Ref. 4; AK056186)" FT /evidence="ECO:0000305" SQ SEQUENCE 660 AA; 75252 MW; C58D0E543E033F17 CRC64; MDDWKPSPLI KPFGARKKRS WYLTWKYKLT NQRALRRFCQ TGAVLFLLVT VIVNIKLILD TRRAISEANE DPEPEQDYDE ALGRLEPPRR RGSGPRRVLD VEVYSSRSKV YVAVDGTTVL EDEAREQGRG IHVIVLNQAT GHVMAKRVFD TYSPHEDEAM VLFLNMVAPG RVLICTVKDE GSFHLKDTAK ALLRSLGSQA GPALGWRDTW AFVGRKGGPV FGEKHSKSPA LSSWGDPVLL KTDVPLSSAE EAECHWADTE LNRRRRRFCS KVEGYGSVCS CKDPTPIEFS PDPLPDNKVL NVPVAVIAGN RPNYLYRMLR SLLSAQGVSP QMITVFIDGY YEEPMDVVAL FGLRGIQHTP ISIKNARVSQ HYKASLTATF NLFPEAKFAV VLEEDLDIAV DFFSFLSQSI HLLEEDDSLY CISAWNDQGY EHTAEDPALL YRVETMPGLG WVLRRSLYKE ELEPKWPTPE KLWDWDMWMR MPEQRRGREC IIPDVSRSYH FGIVGLNMNG YFHEAYFKKH KFNTVPGVQL RNVDSLKKEA YEVEVHRLLS EAEVLDHSKN PCEDSFLPDT EGHTYVAFIR MEKDDDFTTW TQLAKCLHIW DLDVRGNHRG LWRLFRKKNH FLMVGVPASP YSVKKPPSVT PIFLEPPPKE EGAPGAPEQT //