ID   A0A0R3PAZ7_ANGCS        Unreviewed;       374 AA.
AC   A0A0R3PAZ7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Beta-1,4-N-acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU368121};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU368121};
DE   AltName: Full=Beta-4-GalNAcT {ECO:0000256|RuleBase:RU368121};
OS   Angiostrongylus costaricensis (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000080001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ACOC_0000080001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the transfer of galactose onto proteins or lipids.
CC       {ECO:0000256|RuleBase:RU368121}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU368121};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU368121}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606,
CC       ECO:0000256|RuleBase:RU368121}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|RuleBase:RU368121}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
CC       {ECO:0000256|ARBA:ARBA00005735, ECO:0000256|RuleBase:RU368121}.
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DR   AlphaFoldDB; A0A0R3PAZ7; -.
DR   WBParaSite; ACOC_0000080001-mRNA-1; ACOC_0000080001-mRNA-1; ACOC_0000080001.
DR   OMA; CDPGGPR; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000050601; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00899; b4GalT; 1.
DR   InterPro; IPR003859; Galactosyl_T.
DR   InterPro; IPR027791; Galactosyl_T_C.
DR   InterPro; IPR027995; Galactosyl_T_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR19300; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19300:SF57; BETA-1,4-N-ACETYLGALACTOSAMINYLTRANSFERASE BRE-4; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF13733; Glyco_transf_7N; 1.
DR   PRINTS; PR02050; B14GALTRFASE.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU368121};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU368121}; Manganese {ECO:0000256|RuleBase:RU368121};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368121};
KW   Metal-binding {ECO:0000256|RuleBase:RU368121};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW   ECO:0000256|RuleBase:RU368121};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368121};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU368121};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU368121}.
FT   TRANSMEM        348..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368121"
FT   DOMAIN          70..202
FT                   /note="Galactosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13733"
FT   DOMAIN          217..285
FT                   /note="Galactosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02709"
SQ   SEQUENCE   374 AA;  42709 MW;  EBFC9C631CF54C10 CRC64;
     LENTVVYHQN DSHSTISHLP SDTTVRATVD SELLLNESST DDGELAFSLT YCFTNTSYPF
     TSQSSSLKLC PLVPPRLVGP IRVWMDSPSF SALQKLYPYL EPGGHGQPKN CRSRHKVAVV
     VPYRDRDSHL RILLHNLHSL LTKQQLDYAI IVVEQVANQT FNRAKLMNVG YAEGIKLYLW
     ECFIFHDVDL LPEDDRNLYS CPTIPRHMII DLLPIYCRFM LPYTAIFGGI SAMTVGQLRS
     INGFSNRYWG WGGEDDDLAD RVSVAGYKVA RYPAPIARYK MIKHEHEAKS NPVNKCRYKL
     MAQTRTQWKA DGLNSLKYEV VKHELLPLYT HILVDLLEND EHKAIKRFLH ITLSVSVLFL
     SGLCSFLLLN HLVK
//