PMGT1_MOUSE
ID PMGT1_MOUSE Reviewed; 660 AA.
AC Q91X88; A2A8F8; Q9D2H7; Q9D5D3; Q9DCN3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1;
DE Short=POMGnT1;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q8WZA1};
GN Name=Pomgnt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=129/SvJ;
RA Minowa M.T., Yoshida A., Endo T., Takeuchi M.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=12670716; DOI=10.1016/s0169-328x(03)00055-x;
RA Henion T.R., Qu Q., Smith F.I.;
RT "Expression of dystroglycan, fukutin and POMGnT1 during mouse cerebellar
RT development.";
RL Brain Res. Mol. Brain Res. 112:177-181(2003).
RN [6]
RP TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Participates in O-mannosyl glycosylation by catalyzing the
CC addition of N-acetylglucosamine to O-linked mannose on glycoproteins.
CC Catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr
CC moiety on alpha-dystroglycan and other O-mannosylated proteins,
CC providing the necessary basis for the addition of further carbohydrate
CC moieties. Is specific for alpha linked terminal mannose.
CC {ECO:0000250|UniProtKB:Q8WZA1}.
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:0000250|UniProtKB:Q8WZA1};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8WZA1};
CC Note=The manganese ion interacts primarily with the substrate UDP-N-
CC acetylglucosamine. {ECO:0000250|UniProtKB:Q8WZA1};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8WZA1}.
CC -!- SUBUNIT: Interacts with DAG1 (via O-linked mannose moiety). Interacts
CC (via transmembrane domain) with FKTN; the interaction is direct and is
CC required for normal location in Golgi membranes.
CC {ECO:0000250|UniProtKB:Q8WZA1}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8WZA1}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8WZA1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q91X88-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91X88-2; Sequence=VSP_014972, VSP_014973;
CC Name=3;
CC IsoId=Q91X88-3; Sequence=VSP_014974;
CC -!- TISSUE SPECIFICITY: Expressed at basal body and daughter centriole of
CC photoreceptor cells (at protein level). {ECO:0000269|PubMed:26908613}.
CC -!- DEVELOPMENTAL STAGE: Broadly expressed in late embryonic and early
CC postnatal cerebellar neurons, including premigratory granule neurons of
CC the external granule cell layer. Expression is maintained in neurons of
CC the internal granule cell layer after migration is complete. Expressed
CC in Purkinje cells throughout development. Expressed in Bergmann glial
CC scaffolds used by granule cells during early posnatal radial migration.
CC {ECO:0000269|PubMed:12670716}.
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:0000250|UniProtKB:Q8WZA1}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 13 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=POMGnT1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_594";
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DR EMBL; AB053220; BAC55021.1; -; mRNA.
DR EMBL; AB053221; BAC55022.1; -; Genomic_DNA.
DR EMBL; AK002638; BAB22251.1; -; mRNA.
DR EMBL; AK019640; BAB31822.1; -; mRNA.
DR EMBL; AK015478; BAB29863.1; -; mRNA.
DR EMBL; AL611947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011201; AAH11201.1; -; mRNA.
DR CCDS; CCDS18506.1; -. [Q91X88-1]
DR CCDS; CCDS18507.1; -. [Q91X88-3]
DR CCDS; CCDS71450.1; -. [Q91X88-2]
DR RefSeq; NP_001277587.1; NM_001290658.1. [Q91X88-2]
DR RefSeq; NP_080927.1; NM_026651.2. [Q91X88-1]
DR RefSeq; NP_084062.2; NM_029786.2. [Q91X88-3]
DR AlphaFoldDB; Q91X88; -.
DR SMR; Q91X88; -.
DR BioGRID; 212776; 4.
DR STRING; 10090.ENSMUSP00000102107; -.
DR CAZy; GT13; Glycosyltransferase Family 13.
DR iPTMnet; Q91X88; -.
DR PhosphoSitePlus; Q91X88; -.
DR SwissPalm; Q91X88; -.
DR EPD; Q91X88; -.
DR jPOST; Q91X88; -.
DR MaxQB; Q91X88; -.
DR PaxDb; Q91X88; -.
DR PeptideAtlas; Q91X88; -.
DR PRIDE; Q91X88; -.
DR ProteomicsDB; 289699; -. [Q91X88-1]
DR ProteomicsDB; 289700; -. [Q91X88-2]
DR ProteomicsDB; 289701; -. [Q91X88-3]
DR Antibodypedia; 32757; 109 antibodies from 24 providers.
DR DNASU; 68273; -.
DR Ensembl; ENSMUST00000106494; ENSMUSP00000102103; ENSMUSG00000028700. [Q91X88-2]
DR Ensembl; ENSMUST00000106496; ENSMUSP00000102105; ENSMUSG00000028700. [Q91X88-3]
DR Ensembl; ENSMUST00000106498; ENSMUSP00000102107; ENSMUSG00000028700. [Q91X88-1]
DR Ensembl; ENSMUST00000120083; ENSMUSP00000112751; ENSMUSG00000028700. [Q91X88-1]
DR Ensembl; ENSMUST00000121052; ENSMUSP00000112911; ENSMUSG00000028700. [Q91X88-1]
DR GeneID; 68273; -.
DR KEGG; mmu:68273; -.
DR UCSC; uc008ugh.2; mouse. [Q91X88-1]
DR UCSC; uc008ugi.2; mouse. [Q91X88-3]
DR UCSC; uc008ugj.1; mouse. [Q91X88-2]
DR CTD; 55624; -.
DR MGI; MGI:1915523; Pomgnt1.
DR VEuPathDB; HostDB:ENSMUSG00000028700; -.
DR eggNOG; ENOG502QSG3; Eukaryota.
DR GeneTree; ENSGT00530000063632; -.
DR HOGENOM; CLU_024847_0_0_1; -.
DR InParanoid; Q91X88; -.
DR OMA; HKKRSWY; -.
DR OrthoDB; 1324622at2759; -.
DR PhylomeDB; Q91X88; -.
DR TreeFam; TF320555; -.
DR Reactome; R-MMU-5173105; O-linked glycosylation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 68273; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Pomgnt1; mouse.
DR PRO; PR:Q91X88; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91X88; protein.
DR Bgee; ENSMUSG00000028700; Expressed in lacrimal gland and 268 other tissues.
DR Genevisible; Q91X88; MM.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047223; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; ISO:MGI.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP: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 Alternative splicing; Disulfide bond; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..660
FT /note="Protein O-linked-mannose beta-1,2-N-
FT acetylglucosaminyltransferase 1"
FT /id="PRO_0000191391"
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:0000255"
FT REGION 68..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..288
FT /note="Carbohydrate-binding stem domain"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT REGION 300..646
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT REGION 473..481
FT /note="Interaction with O-glycosylated substrate
FT glycoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT REGION 506..512
FT /note="Interaction with O-glycosylated substrate
FT glycoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT REGION 600..605
FT /note="Interaction with O-glycosylated substrate
FT glycoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT REGION 634..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
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:0000250|UniProtKB:Q8WZA1"
FT BINDING 179
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 207
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 307..311
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 338
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 371
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 394..395
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 395
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 500
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 506..507
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT DISULFID 254..281
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT DISULFID 269..279
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT DISULFID 421..490
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT DISULFID 562..596
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014972"
FT VAR_SEQ 23..40
FT /note="LTWKYKLTNQRALRRFCQ -> MEGTKEVKDSNGKIQDHG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014973"
FT VAR_SEQ 218..250
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014974"
FT CONFLICT 424
FT /note="A -> S (in Ref. 2; BAB29863)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="H -> P (in Ref. 2; BAB22251)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 75110 MW; 4DE09765C0F3EF7C CRC64;
MDDWKPSPLI KPFGARKKRS WYLTWKYKLT NQRALRRFCQ TGAVLFLLVT VIVNIKLILD
TRRAISEANE DPEPEQDYDE ALGRLESPRR RGSSPRRVLD VEVYSSRSKV YVAVDGTTVL
EDEAREQGRG IHVIVLNQAT GHVMAKRVFD TYSPHEDEAM VLFLNMVAPG RVLICTVKDE
GSFHLKDTAK ALLRSLGSQA GPALGWRDTW AFVGRKGGPV LGEKHSKSPA LSSWGDPVLL
KTDVPLSSAE EAECHWADTE LNRRRRRFCS KVEGYGSVCS CKDPTPIEFS PDPLPDNKVL
NVPVAVIAGN RPNYLYRMLR SLLSAQGVSP QMITVFIDGY YEEPMDVVAL FGLRGIQHTP
ISIKNARVSQ HYKASLTATF NLFPEAKFAV VLEEDLDIAV DFFSFLSQSI HLLEEDDSLY
CISAWNDQGY EHTAEDPALL YRVETMPGLG WVLRKSLYKE ELEPKWPTPE KLWDWDMWMR
MPEQRRGREC IIPDVSRSYH FGIVGLNMNG YFHEAYFKKH KFNTVPGVQL RNVDSLKKEA
YEVEIHRLLS EAEVLDHSKD PCEDSFLPDT EGHTYVAFIR METDDDFATW TQLAKCLHIW
DLDVRGNHRG LWRLFRKKNH FLVVGVPASP YSVKKPPSVT PIFLEPPPKE EGAPGAAEQT
