PMGT2_XENTR
ID PMGT2_XENTR Reviewed; 576 AA.
AC Q5NDE6; A4IIA6; Q28HA5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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; ORFNames=TEgg056h10.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
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 TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) 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; AJ868538; CAI30872.1; -; mRNA.
DR EMBL; CR760963; CAJ82077.1; -; mRNA.
DR EMBL; BC135937; AAI35938.1; -; mRNA.
DR RefSeq; NP_001011203.1; NM_001011203.1.
DR RefSeq; XP_012820049.1; XM_012964595.2.
DR RefSeq; XP_012820050.1; XM_012964596.2.
DR RefSeq; XP_012820051.1; XM_012964597.2.
DR RefSeq; XP_012820052.1; XM_012964598.2.
DR RefSeq; XP_017950117.1; XM_018094628.1.
DR AlphaFoldDB; Q5NDE6; -.
DR SMR; Q5NDE6; -.
DR STRING; 8364.ENSXETP00000047662; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR PaxDb; Q5NDE6; -.
DR DNASU; 496628; -.
DR Ensembl; ENSXETT00000047662; ENSXETP00000047662; ENSXETG00000022021.
DR GeneID; 496628; -.
DR KEGG; xtr:496628; -.
DR CTD; 84892; -.
DR Xenbase; XB-GENE-973748; pomgnt2.
DR eggNOG; KOG4698; Eukaryota.
DR HOGENOM; CLU_020169_0_0_1; -.
DR InParanoid; Q5NDE6; -.
DR OMA; EQNFPRI; -.
DR OrthoDB; 820160at2759; -.
DR PhylomeDB; Q5NDE6; -.
DR TreeFam; TF332712; -.
DR Reactome; R-XTR-5173105; O-linked glycosylation.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000022021; Expressed in egg cell and 12 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 InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007657; Glycosyltransferase_61.
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..576
FT /note="Protein O-linked-mannose beta-1,4-N-
FT acetylglucosaminyltransferase 2"
FT /id="PRO_0000249023"
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..576
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 482..576
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 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 441
FT /note="L -> F (in Ref. 2; CAJ82077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 66693 MW; DDE8E5E30CA173EB CRC64;
MNISAVFNAL LVSIMAAVLW KHVKLLEQFY VIEEELELTR QSQELSQVRI DYQAALQALV
EDGTRMVCSG RMHTDRVCRF ESLCYSTEAE EFVFFHSNSS IMLPNLGPRR FQPALLDLSS
VDDHNTQYFN FIELPAAALK FMPKPVFVPD VALIMNRFNP DNLMHVFHDD LIPIFYTIQQ
FADLDFESRL FFMEGWNEGL HFELYKFMSN KQPLLKEQLK TLGRLLCFTK SYVGLSKITT
WYQYGFVQPQ GPKANILVSG NEIRHFAKFM MGKLNITKDQ NAAEAYIVLF SRSMNRLIVN
EAELLLALAQ EFQMKTITVS LEDHSFADIV RLISNATMLV SMHGAQLITS LFLPKGAIVV
ELFPYGVNPE HYTPYKTLST LPGMELQYVA WQNTEEENTI AYPNRPWEQG GIVHLDKTEQ
ERIKKSKEVP RHLCCRNPEW LFRIYQDTKV NISSLIQVIK SKTKLGSRRQ KWTQGLYPGK
VRESKCQASA QGTGEAKLFV SWQIPWNLKF LKVRDVKYEV WIQEQGENSY MPYILSQQNY
TFSENIKPLT TYLVWIRCIF NKTLLGPFAE VLVCNT
