PMGT1_HUMAN
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 03-AUG-2022, entry version 173.
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 stem domain mediates specific interaction with beta-linked
CC N-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 ---------------------------------------------------------------------------
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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; 108.
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; Q8WZA1; -.
DR PeptideAtlas; Q8WZA1; -.
DR PRIDE; Q8WZA1; -.
DR ProteomicsDB; 65277; -.
DR ProteomicsDB; 75242; -. [Q8WZA1-1]
DR Antibodypedia; 32757; 109 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 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; HKKRSWY; -.
DR OrthoDB; 1324622at2759; -.
DR PhylomeDB; Q8WZA1; -.
DR TreeFam; TF320555; -.
DR BioCyc; MetaCyc:ENSG00000085998-MON; -.
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; 9 hits in 1077 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 185 other tissues.
DR ExpressionAtlas; Q8WZA1; baseline and differential.
DR Genevisible; Q8WZA1; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of 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:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; IDA:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI.
DR CDD; cd13937; PANDER_GnT-1_2_like; 1.
DR Gene3D; 3.90.550.10; -; 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 Pfam; PF03071; GNT-I; 1.
DR Pfam; PF15711; ILEI; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Congenital muscular dystrophy;
KW Disease variant; Disulfide bond; Dystroglycanopathy; Glycosyltransferase;
KW Golgi apparatus; Limb-girdle muscular dystrophy; Lissencephaly; Manganese;
KW 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 REGION 68..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..288
FT /note="Carbohydrate-binding stem domain"
FT /evidence="ECO:0000269|PubMed:27493216"
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; found on the same allele as Q-
FT 311; unknown pathological significance; 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
