PMGT2_BOVIN
ID PMGT2_BOVIN Reviewed; 580 AA.
AC Q5NDF2; Q08DC6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
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.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) 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; AJ868532; CAI30866.1; -; mRNA.
DR EMBL; BC123822; AAI23823.1; -; mRNA.
DR RefSeq; NP_001011682.1; NM_001011682.2.
DR RefSeq; XP_005222438.1; XM_005222381.3.
DR PDB; 7E9J; X-ray; 2.40 A; A/B=45-580.
DR PDB; 7E9K; X-ray; 2.05 A; A/B/D/E=45-580.
DR PDB; 7E9L; X-ray; 2.10 A; A/B=45-580.
DR PDBsum; 7E9J; -.
DR PDBsum; 7E9K; -.
DR PDBsum; 7E9L; -.
DR AlphaFoldDB; Q5NDF2; -.
DR SMR; Q5NDF2; -.
DR STRING; 9913.ENSBTAP00000000583; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR PaxDb; Q5NDF2; -.
DR PRIDE; Q5NDF2; -.
DR Ensembl; ENSBTAT00000000583; ENSBTAP00000000583; ENSBTAG00000000459.
DR GeneID; 497030; -.
DR KEGG; bta:497030; -.
DR CTD; 84892; -.
DR VEuPathDB; HostDB:ENSBTAG00000000459; -.
DR eggNOG; KOG4698; Eukaryota.
DR GeneTree; ENSGT00940000160695; -.
DR HOGENOM; CLU_020169_0_0_1; -.
DR InParanoid; Q5NDF2; -.
DR OMA; EFQMRVV; -.
DR OrthoDB; 820160at2759; -.
DR TreeFam; TF332712; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000000459; Expressed in floor plate of diencephalon and 102 other tissues.
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 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Membrane; 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_0000249012"
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"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:7E9K"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:7E9K"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:7E9K"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 419..427
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 440..446
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 454..462
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:7E9K"
FT HELIX 510..514
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 520..528
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 534..546
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 555..564
FT /evidence="ECO:0007829|PDB:7E9K"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:7E9K"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:7E9L"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:7E9K"
SQ SEQUENCE 580 AA; 66067 MW; DA2AD2E3140D6D6B CRC64;
MHLSAVLNAL LVSVLAAVLW KHVRLREHAA SLEEELAVGR RAADPAPALR IDYPKALQIL
TEGGTHMVCT GRTHTDRLCR FKWLCYSSEA EEFIFFHGNA SVMLPSLGSR RFQPALLDLS
TVEDHNTQYF NFVELPAAAL RFMPKPVFVP DVALIANRFN PDNLMHVFHD DLLPLFYTLR
QFPGLAREAR LFFMEGWGEG AHFDLYKLLS PKQPLLRAQL KALGRLLCFS HAFVGLSKVT
TWYQYGFVQP QGPKANILVS GNEIRQFAHF LMEKLNVSQA GGPLGEEYIL VFSRTQNRLI
LNEAELLLAL AQEFQMKTVT VSLEDHAFAD VVRLVSNASM LVSMHGAQLV TALFLPRGAA
VVELFPYAVN PDHYTPYKTL ATLPGMDLQY IAWQNTMPEN TVTHPERPWD QGGIAHLDRA
EQARILQSRE VPRHLCCRNP EWLFRIYQDT KVDIPSLIQT IRRVVKGHPG PRKQKWTVSL
YPGKVREARC QASVQGASEA RLSVSWQIPW NLKYLKVREV KYEVWLQEQG ENTYVPYMLA
LQNHTFTENI KPFTTYLVWI RCIFNKTLLG PFADVLVCST
