ID   B3GL2_DANRE             Reviewed;         491 AA.
AC   Q502B3;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2;
DE            Short=Beta-1,3-GalNAc-T2;
DE            EC=2.4.1.313 {ECO:0000250|UniProtKB:Q8NCR0};
DE   AltName: Full=Beta-1,3-N-acetylgalactosaminyltransferase II;
GN   Name=b3galnt2; ORFNames=zgc:112351;
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 [LARGE SCALE MRNA].
RC   STRAIN=AB; TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=23453667; DOI=10.1016/j.ajhg.2013.01.016;
RG   UK10K Consortium;
RA   Stevens E., Carss K.J., Cirak S., Foley A.R., Torelli S., Willer T.,
RA   Tambunan D.E., Yau S., Brodd L., Sewry C.A., Feng L., Haliloglu G.,
RA   Orhan D., Dobyns W.B., Enns G.M., Manning M., Krause A., Salih M.A.,
RA   Walsh C.A., Hurles M., Campbell K.P., Manzini M.C., Stemple D., Lin Y.Y.,
RA   Muntoni F.;
RT   "Mutations in B3GALNT2 cause congenital muscular dystrophy and
RT   hypoglycosylation of alpha-dystroglycan.";
RL   Am. J. Hum. Genet. 92:354-365(2013).
CC   -!- FUNCTION: Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a
CC       unique carbohydrate structure, GalNAc-beta-1-3GlcNAc, on N- and O-
CC       glycans. Has no galactose nor galactosaminyl transferase activity
CC       toward any acceptor substrate. Involved in alpha-dystroglycan (dag1)
CC       glycosylation. {ECO:0000269|PubMed:23453667}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-O-(N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl)-L-
CC         threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[beta-
CC         D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-alpha-D-Man]-L-Thr-[protein] +
CC         H(+) + UDP; Xref=Rhea:RHEA:37667, Rhea:RHEA-COMP:13308, Rhea:RHEA-
CC         COMP:13618, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC         ChEBI:CHEBI:136709, ChEBI:CHEBI:137540; EC=2.4.1.313;
CC         Evidence={ECO:0000250|UniProtKB:Q8NCR0};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
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DR   EMBL; BC095777; AAH95777.1; -; mRNA.
DR   RefSeq; NP_001018523.1; NM_001020687.1.
DR   AlphaFoldDB; Q502B3; -.
DR   SMR; Q502B3; -.
DR   STRING; 7955.ENSDARP00000067823; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   PaxDb; Q502B3; -.
DR   GeneID; 553716; -.
DR   KEGG; dre:553716; -.
DR   CTD; 148789; -.
DR   ZFIN; ZDB-GENE-050522-358; b3galnt2.
DR   eggNOG; KOG2287; Eukaryota.
DR   InParanoid; Q502B3; -.
DR   OrthoDB; 640360at2759; -.
DR   PhylomeDB; Q502B3; -.
DR   Reactome; R-DRE-5173105; O-linked glycosylation.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q502B3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008376; F:acetylgalactosaminyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IMP:UniProtKB.
DR   GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..491
FT                   /note="UDP-GalNAc:beta-1,3-N-
FT                   acetylgalactosaminyltransferase 2"
FT                   /id="PRO_0000248364"
FT   TOPO_DOM        1..2
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3..23
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..491
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   491 AA;  54876 MW;  18290B02B0785BCF CRC64;
     MRSAAAALSV CVLAVLLHWI CWTDRSAELL GFRAADRPKA DVREVLVGVL SARHNHELRQ
     AIRDTWLGYL KQHPHFQNRV LVKFIIGAQG CSVPLEDLED QYSCSQLELS EAAVSGQEMA
     ILSVPDSSAL LQSDVPVLSL DFKVLHSVVI TQLGVFPNKP PHYLKGNITV RLLQVDQEEA
     VISARFSSVS PGTAADGMFY KPVEQFILPK GFEGTLLWEA EDSTALMSVN TSALRLNNGG
     GVLHFRSIEE GTLPHRNALG FPGLAGGFTF TVYDVEVLSE MLRGRSGRQK IREAQLKGED
     EALQEESLRH GDMVFVDVVG TYRNVPSKLL QFYKWSVENA DFSLLLKTDD DCFIDVDAVL
     MKMQRRRLTH TSLWWGNFRQ NWAVDRVGKW QELEYASPAY PAFACGSGYV VSRDLVQWLA
     SNAQHLKAYQ GEDVSMGIWM AAVGPRKYQD SGWLCEKECY VDMLSSPQHS AEELRLLWSR
     KNKCGDPCGC S