PMGT2_MOUSE
ID PMGT2_MOUSE Reviewed; 605 AA.
AC Q8BW41; Q58F17; Q8BXZ9; Q8K0M5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2;
DE Short=POMGnT2;
DE EC=2.4.1.312 {ECO:0000250|UniProtKB:Q8NAT1};
DE AltName: Full=Extracellular O-linked N-acetylglucosamine transferase-like;
DE AltName: Full=Glycosyltransferase-like domain-containing protein 2;
GN Name=Pomgnt2; Synonyms=Ago61, Eogtl, Gtdc2;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Ovary;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=22958903; DOI=10.1016/j.ajhg.2012.07.009;
RA Manzini M.C., Tambunan D.E., Hill R.S., Yu T.W., Maynard T.M.,
RA Heinzen E.L., Shianna K.V., Stevens C.R., Partlow J.N., Barry B.J.,
RA Rodriguez J., Gupta V.A., Al-Qudah A.K., Eyaid W.M., Friedman J.M.,
RA Salih M.A., Clark R., Moroni I., Mora M., Beggs A.H., Gabriel S.B.,
RA Walsh C.A.;
RT "Exome sequencing and functional validation in zebrafish identify GTDC2
RT mutations as a cause of Walker-Warburg syndrome.";
RL Am. J. Hum. Genet. 91:541-547(2012).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24256719; DOI=10.1038/srep03288;
RA Yagi H., Nakagawa N., Saito T., Kiyonari H., Abe T., Toda T., Wu S.W.,
RA Khoo K.H., Oka S., Kato K.;
RT "AGO61-dependent GlcNAc modification primes the formation of functional
RT glycans on alpha-dystroglycan.";
RL Sci. Rep. 3:3288-3288(2013).
CC -!- FUNCTION: O-linked mannose beta-1,4-N-acetylglucosaminyltransferase
CC that transfers UDP-N-acetyl-D-glucosamine to the 4-position of the
CC mannose to generate N-acetyl-D-glucosamine-beta-1,4-O-D-mannosylprotein
CC (By similarity). Involved in the biosynthesis of the phosphorylated O-
CC mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-
CC acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate
CC structure present in alpha-dystroglycan (DAG1), which is required for
CC binding laminin G-like domain-containing extracellular proteins with
CC high affinity (PubMed:24256719). {ECO:0000250|UniProtKB:Q8NAT1,
CC ECO:0000269|PubMed:24256719}.
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->4)-alpha-
CC D-mannosyl)-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:37663,
CC Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:13618, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137323,
CC ChEBI:CHEBI:137540; EC=2.4.1.312;
CC Evidence={ECO:0000250|UniProtKB:Q8NAT1};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:24256719}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8NAT1}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NAT1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BW41-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BW41-2; Sequence=VSP_020354, VSP_020355;
CC -!- TISSUE SPECIFICITY: Mainly expressed in the central nervous system.
CC {ECO:0000269|PubMed:24256719}.
CC -!- DEVELOPMENTAL STAGE: Expressed during brain development. At 14.5 dpc,
CC expressed throughout the cortical plate and the developing brain, as
CC well as throughout the eye, including the lens and cornea. Cortical
CC expression is already detected at 12.5 dpc, peaks between 14.5 and 16.5
CC dpc and is reduced at birth. {ECO:0000269|PubMed:22958903}.
CC -!- DISRUPTION PHENOTYPE: Newborn are slightly smaller and die within the
CC first day of birth due to abnormal basal lamina formation and neuronal
CC migration defects. Defects are due to a lack of laminin-binding
CC glycans. {ECO:0000269|PubMed:24256719}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 61 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31348.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK042747; BAC31348.1; ALT_SEQ; mRNA.
DR EMBL; AK054403; BAC35765.1; -; mRNA.
DR EMBL; AK133802; BAE21851.1; -; mRNA.
DR EMBL; BC025056; AAH25056.1; -; mRNA.
DR EMBL; BC030931; AAH30931.1; -; mRNA.
DR CCDS; CCDS23643.1; -. [Q8BW41-2]
DR RefSeq; NP_001276487.1; NM_001289558.1. [Q8BW41-2]
DR RefSeq; NP_001276488.1; NM_001289559.1. [Q8BW41-2]
DR RefSeq; NP_001276489.1; NM_001289560.1. [Q8BW41-2]
DR RefSeq; NP_705768.4; NM_153540.4. [Q8BW41-2]
DR RefSeq; XP_011241257.1; XM_011242955.1. [Q8BW41-2]
DR AlphaFoldDB; Q8BW41; -.
DR SMR; Q8BW41; -.
DR BioGRID; 229636; 1.
DR STRING; 10090.ENSMUSP00000095868; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR GlyConnect; 2638; 4 N-Linked glycans (2 sites).
DR GlyGen; Q8BW41; 3 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q8BW41; -.
DR PhosphoSitePlus; Q8BW41; -.
DR SwissPalm; Q8BW41; -.
DR MaxQB; Q8BW41; -.
DR PaxDb; Q8BW41; -.
DR PeptideAtlas; Q8BW41; -.
DR PRIDE; Q8BW41; -.
DR ProteomicsDB; 289457; -. [Q8BW41-1]
DR ProteomicsDB; 289458; -. [Q8BW41-2]
DR Antibodypedia; 29340; 158 antibodies from 26 providers.
DR Ensembl; ENSMUST00000084743; ENSMUSP00000095868; ENSMUSG00000066235. [Q8BW41-2]
DR Ensembl; ENSMUST00000216669; ENSMUSP00000149077; ENSMUSG00000066235. [Q8BW41-2]
DR Ensembl; ENSMUST00000217610; ENSMUSP00000149753; ENSMUSG00000066235. [Q8BW41-2]
DR GeneID; 215494; -.
DR KEGG; mmu:215494; -.
DR UCSC; uc009sek.2; mouse. [Q8BW41-2]
DR CTD; 84892; -.
DR MGI; MGI:2143424; Pomgnt2.
DR VEuPathDB; HostDB:ENSMUSG00000066235; -.
DR eggNOG; KOG4698; Eukaryota.
DR GeneTree; ENSGT00940000160695; -.
DR HOGENOM; CLU_020169_0_0_1; -.
DR InParanoid; Q8BW41; -.
DR OMA; EFQMRVV; -.
DR OrthoDB; 820160at2759; -.
DR PhylomeDB; Q8BW41; -.
DR TreeFam; TF332712; -.
DR Reactome; R-MMU-5173105; O-linked glycosylation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 215494; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8BW41; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BW41; protein.
DR Bgee; ENSMUSG00000066235; Expressed in facial nucleus and 221 other tissues.
DR ExpressionAtlas; Q8BW41; baseline and differential.
DR Genevisible; Q8BW41; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0035269; P:protein O-linked mannosylation; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007657; Glycosyltransferase_61.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR20961; PTHR20961; 1.
DR Pfam; PF04577; Glyco_transf_61; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..605
FT /note="Protein O-linked-mannose beta-1,4-N-
FT acetylglucosaminyltransferase 2"
FT /id="PRO_0000249015"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..580
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 488..584
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 573..580
FT /note="CRCAGVQH -> ADVLVCST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_020354"
FT VAR_SEQ 581..605
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_020355"
FT CONFLICT 567
FT /note="S -> T (in Ref. 2; AAH30931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 69378 MW; 2A70A214653D9E12 CRC64;
MHLSAVFNAL LVSVLAAVLW KHVRLREHAA TLEEELALGQ QSLDPVLGLK IDYPKALQIL
MEGGTHMVCT GRTHTDRICR FKWLCYSNEA EEFIFFHGNS SVMLPNLGSR RFQPALLDLS
TVEDHNAQYF NFVELPAAAL RFMPKPVFVP DVALIANRFN PDNLMHVFHD DLLPLFYTLR
QFPGLAQEAR LFFMEGWGEG AHFDLYKLLS PKQPLLRAQL KTLGRLLCFS HAFVGLSKVT
TWYQYGFVQP QGPKANILVS GNEIRQFTRF MTERLNVSHA GAPLGEEYIL VFSRTQNRLI
LNEAELLLEL AQEFQMKTVT VSLEDHTFAD VVRLVSNASM LVSMHGAQLV TALFLPRGAT
VVELFPYAVN PDHYTPYKTL ATLPGMDLQY VAWRNMIREN TVTHPERPWD QGGITHLDRA
EQARILQSRE VPRHLCCRNP EWLFRIYQDT RVDIPSLMQS IRRVVKGRPG PRRQRWAISL
YPGKVREARC QASVQGATEA RLSVSWQIPW NLKYLKVREV KYEVWLQEQG ENTYVPYMLT
LQNHTFTENI KPFTTYLVWV RCIFNRSLLG PFCRCAGVQH VASRPWPGLW RAPLAGSAFP
GPQFC
