PMGT2_CHICK
ID PMGT2_CHICK Reviewed; 577 AA.
AC Q5NDE8;
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;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
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; AJ868536; CAI30870.1; -; mRNA.
DR RefSeq; NP_001012294.1; NM_001012294.1.
DR RefSeq; XP_015137060.1; XM_015281574.1.
DR RefSeq; XP_015137061.1; XM_015281575.1.
DR RefSeq; XP_015137062.1; XM_015281576.1.
DR AlphaFoldDB; Q5NDE8; -.
DR SMR; Q5NDE8; -.
DR STRING; 9031.ENSGALP00000018758; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR PaxDb; Q5NDE8; -.
DR Ensembl; ENSGALT00000018781; ENSGALP00000018758; ENSGALG00000011518.
DR Ensembl; ENSGALT00000091484; ENSGALP00000067430; ENSGALG00000011518.
DR Ensembl; ENSGALT00000091601; ENSGALP00000070717; ENSGALG00000011518.
DR GeneID; 428446; -.
DR KEGG; gga:428446; -.
DR CTD; 84892; -.
DR VEuPathDB; HostDB:geneid_428446; -.
DR eggNOG; KOG4698; Eukaryota.
DR GeneTree; ENSGT00940000160695; -.
DR HOGENOM; CLU_020169_0_0_1; -.
DR InParanoid; Q5NDE8; -.
DR OMA; EFQMRVV; -.
DR OrthoDB; 820160at2759; -.
DR PhylomeDB; Q5NDE8; -.
DR TreeFam; TF332712; -.
DR Reactome; R-GGA-5173105; O-linked glycosylation.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5NDE8; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000011518; Expressed in brain and 13 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 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..577
FT /note="Protein O-linked-mannose beta-1,4-N-
FT acetylglucosaminyltransferase 2"
FT /id="PRO_0000249018"
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..577
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 481..577
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 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 577 AA; 66754 MW; 601E0D178D7F3092 CRC64;
MNIAAVFNAL LVSVLATVLW KYIKLREHAF MVEEELVLMR QSQELSQVQI DYHAALQTLL
EDGTRMVCTG RMHTDRICRF ESLCYSTEAE EFIYFHSNSS VMLPNLGSRR FQPALLDLSS
VEDHNTQYFN FVELPAAALK FMPKPVFVPD VALIANRFNP DNLMHVFHDD LLPIYYTMQQ
FTDLDPETRL FFMEGWSEGV HFDLYKLLSN KQPLLREQLK TLGRLLCFTK SYVGLSKITT
WYQYGFVQPQ GPKANILVSG NEIRQFTKFM MQKLNVSLEE SSSEEYIVVF SRTINRLILN
EAELILALAQ EFQMKTITVS LEEHSFSDIV RLISNASMLV SMHGAQLVMS LFLPRGATVV
ELFPYAINPE HYTPYKTLAT LPGMDLQYIA WQNTAREDTV TYPDRPWDQG GIAHLDKAEQ
ERIIKSTEVP RHLCCRNPEW LFRAYQDTKV DIPSLIHVIR QTVKSKPGPK KKWSGSLYPG
KVRDARCQAS VQGTSEARLS VSWQVPWNLK YLKVREVKYE VWIQEQGENT YMPYILSHQN
HTFSENIKPF TIYLVWIRCI FNKNLLGPFA DVLLCST
