ID   B3GL2_XENLA             Reviewed;         486 AA.
AC   Q6NRQ1;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
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 laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-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; BC070684; AAH70684.1; -; mRNA.
DR   RefSeq; NP_001084830.1; NM_001091361.1.
DR   AlphaFoldDB; Q6NRQ1; -.
DR   SMR; Q6NRQ1; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   DNASU; 431874; -.
DR   GeneID; 431874; -.
DR   KEGG; xla:431874; -.
DR   CTD; 431874; -.
DR   Xenbase; XB-GENE-1012161; b3galnt2.L.
DR   OMA; EKTCESG; -.
DR   OrthoDB; 640360at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 431874; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008376; F:acetylgalactosaminyltransferase activity; ISS:UniProtKB.
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..486
FT                   /note="UDP-GalNAc:beta-1,3-N-
FT                   acetylgalactosaminyltransferase 2"
FT                   /id="PRO_0000248365"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..486
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   486 AA;  55701 MW;  412B4D46BCCF29BE CRC64;
     MRHLLFLCPC VIGVAFHLWL FNFSGLFSWF LVWSPHSYDI VVGVLSARHN HELRNVIRHT
     WLQHLNHHSS LSQRVLVKFI IGSHGCDIPV EDREDPYSCK LLNITNPTLK QEIESFSIPD
     SAAVITEHHV VNVNFRVLYP VVITRLGVFQ HDSAAGFQRN ITVKLFQTEH EEALFSARFS
     PASSGVQVNG IWYKPVEQFI LPEGFEGTVV WESHDPEGLL SGNVHHVIVN DGGGIFRLTT
     VKEGLLPYEF TEGVEGIAGG FTYTIHEGET LLNTLETRPE RIQNHLAALE KEDALLQEES
     TTFQDIVFVN VVDTYRNVPS KLLNFYRWTV QLTRFEFLLK TDDDCFIDID NVLKMVAQKE
     LQKENAWWGN FRLNWAVDRT GKWQELEYLS PAYPAFACGS GYIISNDIVQ WLAVNSQRLK
     TYQGEDVSMG IWMSAIGPSR YQDSRWLCEK KCEAGMLSSP QYTPQELMEI WQQKERCGNP
     CACEDR