PMGT2_CANLF
ID PMGT2_CANLF Reviewed; 580 AA.
AC Q5NDE9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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.
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}.
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; AJ868535; CAI30869.1; -; mRNA.
DR RefSeq; NP_001010957.1; NM_001010957.1.
DR RefSeq; XP_005634220.1; XM_005634163.2.
DR AlphaFoldDB; Q5NDE9; -.
DR SMR; Q5NDE9; -.
DR STRING; 9612.ENSCAFP00000043129; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR PaxDb; Q5NDE9; -.
DR Ensembl; ENSCAFT00000095069; ENSCAFP00000073358; ENSCAFG00000030823.
DR Ensembl; ENSCAFT00845037846; ENSCAFP00845029654; ENSCAFG00845021458.
DR GeneID; 485621; -.
DR KEGG; cfa:485621; -.
DR CTD; 84892; -.
DR VEuPathDB; HostDB:ENSCAFG00845021458; -.
DR eggNOG; KOG4698; Eukaryota.
DR GeneTree; ENSGT00940000160695; -.
DR InParanoid; Q5NDE9; -.
DR OrthoDB; 820160at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002254; Chromosome 23.
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; IBA:GO_Central.
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 2: Evidence at transcript 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_0000249013"
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:0000255"
SQ SEQUENCE 580 AA; 65995 MW; F71FDE7E48AE0DDE CRC64;
MHLSAVLNAL LVSVLAAVLW KHVRLREHAA ALEEEVAAGR QAPAPGPAPR ADYARALQLL
SEGGTHMVCT GRTHTDRVCR FKWLCYSNEA EEFIFFHGNA SVMLPNLGSR RFQPALLDLS
TVEDHNTQYF NFVELPAAAL RFLPKPVFVP DVALVANRFN PDNLMHVFHD DLLPLFYTLR
QFPGLAHEAR LFFMEGWSEG AHFDLYKLLS PKQPLLRAQL KTLGRLLCFS HAFVGLSKVT
TWYQYGFVQP QGPKANILVS GNEIRQFARF MMEKLNVSQA GAPLGEEYIL VFSRTQNRLI
LNEAELLLAL AQEFQMKTVT VSLEDQAFAD VVRLVSNASM LVSVHGAQLV TALFLPRGAT
VVELFPYAVN PDHYTPYKTL ATLPGMDLQY VAWRNMMPEN TVTHPERPWD QGGIAHLDRA
EQARILQSRE VPRHLCCRNP EWLFRIYQDT KVDIPSLIQT VRRVVKGRPG PRKQKWTVGL
YPGKVREARC QASVQGASEA RLTVSWQIPW NLKYLKVREV KYEVWLQEQG ENTYVPYILA
LQNHTFTENI KPFTTYLVWV RCIFNKTLLG PFADVLVCNT
