PMGT2_RAT
ID PMGT2_RAT Reviewed; 580 AA.
AC Q5NDF0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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, Gtdc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Kiefer-Meyer M.C., Pagny S., Durambure G., Faye L., Gomord V.,
RA Mollicone R., Oriol R.;
RT "Phylogeny of xylosyltransferases.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-276, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(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-
CC mannosylprotein. 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 (By similarity). {ECO:0000250|UniProtKB:Q8NAT1}.
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:0000250|UniProtKB:Q8NAT1}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8NAT1}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NAT1}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 61 family.
CC {ECO:0000305}.
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DR EMBL; AJ868534; CAI30868.1; -; mRNA.
DR RefSeq; NP_001009437.1; NM_001009437.1.
DR RefSeq; XP_008764903.1; XM_008766681.2.
DR RefSeq; XP_008764905.1; XM_008766683.2.
DR AlphaFoldDB; Q5NDF0; -.
DR SMR; Q5NDF0; -.
DR STRING; 10116.ENSRNOP00000063923; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR GlyGen; Q5NDF0; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q5NDF0; -.
DR PaxDb; Q5NDF0; -.
DR PRIDE; Q5NDF0; -.
DR Ensembl; ENSRNOT00000026363; ENSRNOP00000063923; ENSRNOG00000019492.
DR Ensembl; ENSRNOT00000100933; ENSRNOP00000079681; ENSRNOG00000019492.
DR GeneID; 316091; -.
DR KEGG; rno:316091; -.
DR CTD; 84892; -.
DR RGD; 1304827; Pomgnt2.
DR eggNOG; KOG4698; Eukaryota.
DR GeneTree; ENSGT00940000160695; -.
DR HOGENOM; CLU_020169_0_0_1; -.
DR InParanoid; Q5NDF0; -.
DR OMA; EFQMRVV; -.
DR OrthoDB; 820160at2759; -.
DR PhylomeDB; Q5NDF0; -.
DR Reactome; R-RNO-5173105; O-linked glycosylation.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5NDF0; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000019492; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q5NDF0; RN.
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:RGD.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR CDD; cd00063; FN3; 1.
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 Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..580
FT /note="Protein O-linked-mannose beta-1,4-N-
FT acetylglucosaminyltransferase 2"
FT /id="PRO_0000249017"
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..580
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:0007744|PubMed:24090084"
SQ SEQUENCE 580 AA; 66717 MW; 7A444F0927DD63C6 CRC64;
MHLSAVFNAL LVSVLAAVLW KHVRLREHAA TLEEELALGQ QSLDPVPGLR IDYPKALQIL
MEGGTHMVCT GRTHTDRICR FKWLCYSNEA EEFIFFHGNS SVMLPNLGSR RFQPALLDLS
TVEDHNAQYF NFVELPAAAL RFMPKPVFVP DVALIANRFN PDNLMHVFHD DLLPLFYTLR
QFPGLAQEAR LFFMEGWGEG AHFDLYKLLS PKQPLLRSQL 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 RYEVWLQEQG ENTYVPYMLT
LQNHTFTENI KPFTTYLVWV RCIFNRSLLG PFADVLVCST
