PMGT2_DANRE
ID PMGT2_DANRE Reviewed; 578 AA.
AC Q5NDE5; Q502K0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=im:7153239, zgc:112079;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
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].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=22958903; DOI=10.1016/j.ajhg.2012.07.009;
RA Manzini M.C., Tambunan D.E., Hill R.S., Yu T.W., Maynard T.M.,
RA Heinzen E.L., Shianna K.V., Stevens C.R., Partlow J.N., Barry B.J.,
RA Rodriguez J., Gupta V.A., Al-Qudah A.K., Eyaid W.M., Friedman J.M.,
RA Salih M.A., Clark R., Moroni I., Mora M., Beggs A.H., Gabriel S.B.,
RA Walsh C.A.;
RT "Exome sequencing and functional validation in zebrafish identify GTDC2
RT mutations as a cause of Walker-Warburg syndrome.";
RL Am. J. Hum. Genet. 91:541-547(2012).
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 -!- DEVELOPMENTAL STAGE: Expressed in the embryo and larva throughout
CC development, with highest levels in the developing brain, eyes and at
CC the boundaries between somites. {ECO:0000269|PubMed:22958903}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 61 family.
CC {ECO:0000305}.
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DR EMBL; AJ868539; CAI30873.1; -; mRNA.
DR EMBL; BC095667; AAH95667.1; -; mRNA.
DR AlphaFoldDB; Q5NDE5; -.
DR SMR; Q5NDE5; -.
DR STRING; 7955.ENSDARP00000111957; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR PaxDb; Q5NDE5; -.
DR Ensembl; ENSDART00000193303; ENSDARP00000151467; ENSDARG00000010941.
DR ZFIN; ZDB-GENE-050522-242; pomgnt2.
DR eggNOG; KOG4698; Eukaryota.
DR GeneTree; ENSGT00940000160695; -.
DR InParanoid; Q5NDE5; -.
DR PhylomeDB; Q5NDE5; -.
DR Reactome; R-DRE-5173105; O-linked glycosylation.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5NDE5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000010941; Expressed in blastula and 29 other tissues.
DR ExpressionAtlas; Q5NDE5; baseline.
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:0007420; P:brain development; IMP:ZFIN.
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 GO; GO:0060041; P:retina development in camera-type eye; IMP:ZFIN.
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..578
FT /note="Protein O-linked-mannose beta-1,4-N-
FT acetylglucosaminyltransferase 2"
FT /id="PRO_0000249019"
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..578
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 482..578
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 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 282..283
FT /note="Missing (in Ref. 2; AAH95667)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="Y -> H (in Ref. 2; AAH95667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 67056 MW; AEDF250FDC685D23 CRC64;
MNLPAVLNGL LVSVVAALLW KYVRLVEHTS QLEEELQLTR QSQEFSQVRI DYHGALLALQ
EHGTRMVCTG KMHTDRICRF DYLCYCTEAE EFVFFHSNAS VMLPNLGSRR FQPALLDLSS
VEDHNTQYFN FLELPAAALK FMPKPVFVPD VTLILNRFNP DNLMHIFHDD LLPVYYTMQQ
YSDLDDEARL VFMEGWGEGA HFDLYRLLSS KQPLLKDQLK TFGKLMCFTK SYVGLSKMTT
WYQYGFVQPQ GPKANILISG NEIRQFASFL MERLNITREE EEEDDDYIVV FKRTTNRLIL
NEAELLLALA QEFQMRTVTV SLEEQSFDNI IQIISRAAML VSMHGAQMIT SMFLPRGAAV
VELFPYGVNP EQYTPYKTLA SLPGMDLQYV AWRNTMEENT VTFPDRPWDQ GGIVHLEKEE
QERILASKEV PRHLCCRNPE WLFRIYQDTT VDLASFLDVL RDGLKKLNLK KAKVASTVHP
GRVREPKCQT SVQATNEAKL SVSWQIPWNL KYLKVKEVKY EVWIQEQGEN TYMPYILPHQ
NYTFSENIKP FTTYLVWVRC IFNKNLLGPF ADVLICKT
