ID   B3GL2_XENTR             Reviewed;         488 AA.
AC   Q5M900;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
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;
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 [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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; BC087761; AAH87761.1; -; mRNA.
DR   RefSeq; NP_001011210.1; NM_001011210.1.
DR   AlphaFoldDB; Q5M900; -.
DR   SMR; Q5M900; -.
DR   STRING; 8364.ENSXETP00000046540; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   DNASU; 496641; -.
DR   GeneID; 496641; -.
DR   KEGG; xtr:496641; -.
DR   CTD; 148789; -.
DR   Xenbase; XB-GENE-1012156; b3galnt2.
DR   InParanoid; Q5M900; -.
DR   OrthoDB; 640360at2759; -.
DR   Reactome; R-XTR-5173105; O-linked glycosylation.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; 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; ISS: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..488
FT                   /note="UDP-GalNAc:beta-1,3-N-
FT                   acetylgalactosaminyltransferase 2"
FT                   /id="PRO_0000248366"
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..488
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   488 AA;  55986 MW;  CB5EE6B324DEF2E3 CRC64;
     MRHLLLLFLC PCAIGVAFHL WLFNFSGLFT WFPVWSQRSY DIVVGVLSAR HNHELRNVIR
     HTWLQHLKQH SSLSQRILVK FIIGSHGCDI PVEDREDPYS CKLLNITNPT FKQEIESFSI
     PDIAALLTEH HVVNVNFRVL YPVVITRLGV FQHDSAAGFH RNITVKLFQT EHEEALFSAR
     FSPASSGVQV NGIWYKPVEQ FILPEGFEGT VVWESHDPEG LLSGNVHRVI VNDGGGIFRI
     TTVKEGLLPY EFTEGVEGIA GGFTYTIHEG EALLNTLETR PERIQIHLAA LEKEDALLQE
     ESTTFQDIVF VHVVDTYRNV PSKLLNFYQW TAEFTSFEFL LKTDDDCFID IENVLEKIAH
     KQLQKENTWW GNFRLNWAVD RTGKWQELEY LSPAYPAFAC GSGYVISQDI VQWLASNSQR
     LKTYQGEDVS MGIWMSAIGP SRYQDSHWLC EKKCEAGMLS SPQYTPQELL ELWQQKERCG
     NPCACEDR