PMGT2_TAKRU
ID PMGT2_TAKRU Reviewed; 590 AA.
AC Q5NDE4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
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 Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
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}.
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DR EMBL; AJ868540; CAI30874.1; -; mRNA.
DR RefSeq; NP_001072049.1; NM_001078581.1.
DR AlphaFoldDB; Q5NDE4; -.
DR SMR; Q5NDE4; -.
DR STRING; 31033.ENSTRUP00000033869; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR GeneID; 777951; -.
DR KEGG; tru:777951; -.
DR CTD; 84892; -.
DR eggNOG; KOG4698; Eukaryota.
DR HOGENOM; CLU_020169_0_0_1; -.
DR InParanoid; Q5NDE4; -.
DR OrthoDB; 820160at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000005226; Unplaced.
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: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..590
FT /note="Protein O-linked-mannose beta-1,4-N-
FT acetylglucosaminyltransferase 2"
FT /id="PRO_0000249020"
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..590
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 494..590
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 590 AA; 68031 MW; 5D619DCAADD0A053 CRC64;
MSVGTLLNGL LVSIVAALLW KYSKLSEHAA LLEEELHMTR QSQELSQAHI DYHVALQALQ
EHGTRMVCTG KMHTDRICRF DYLCYCSEAE EFVFFHSNSS VMLPNLGSRR FQPALLDLSS
VEDHNTQYFN FLELPAATLR FMPKPVFVPD VTLILNRFNP DNLMHVFHDD LLPAFYTMKQ
FLDSDEDARL VFMEGWEEGP HFELYRLLSN KQPLLKEQLR NFGKLMCFTK SYIGLSKMTT
WYQYGFVQPQ GPKANILVSG NEIRHFAKVL MEKMNITRAA GGEKDQGNAE DEKPKDEYIV
VFSRSTTRLI LNEAELIMAL AQEFQMRVVT VSLEEQSFPS IVQVISGASM LVSMHGAQLI
TSLFLPPGAV VVELYPFAVN PDQYTPYRTL ASLPGMDLHY IPWRNTEEEN TVTHPDRPWE
QGGIAHLEKE EQEQIMASKD VPRHLCCRNP EWLFRIYQDT LVDIPSFLEV LQEGVKAKPL
LKKSKLSSTL HPGRVRDPQC QTSVQTSNEA KLTVSWQIPW NLKYLKVREV KYEVWIQEQG
ENTYMPYILP QQNYTFSDNI KPFTTYLVWV RCIFNKNLLG PFADVLMCRT
