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Database: UniProt
Entry: A0A1I7VI09_LOALO
LinkDB: A0A1I7VI09_LOALO
Original site: A0A1I7VI09_LOALO 
ID   A0A1I7VI09_LOALO        Unreviewed;       463 AA.
AC   A0A1I7VI09;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   Loa loa (Eye worm) (Filaria loa).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX   NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_2753};
RN   [1] {ECO:0000313|Proteomes:UP000095285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Loa loa.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:EN70_2753}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-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; A0A1I7VI09; -.
DR   STRING; 7209.A0A1I7VI09; -.
DR   WBParaSite; EN70_2753; EN70_2753; EN70_2753.
DR   eggNOG; KOG3916; Eukaryota.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000095285; Unassembled WGS sequence.
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};
KW   Metal-binding {ECO:0000256|RuleBase:RU368121};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095285};
KW   Signal {ECO:0000256|SAM:SignalP};
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   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..463
FT                   /note="Beta-1,4-N-acetylgalactosaminyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009310070"
FT   DOMAIN          183..315
FT                   /note="Galactosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13733"
FT   DOMAIN          319..396
FT                   /note="Galactosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02709"
SQ   SEQUENCE   463 AA;  53177 MW;  AADA42831CE09BDE CRC64;
     MPTVGRFVIT LLLLGAAAHI FLGGDLSFIS DYHIWKPIVE NNKQEIILMH DTNNNSDRDS
     NEIPSNDERK FHLISVAPFA NSVSIPSKFY KLFTNGLLYS NLTTVYPTIN ASIINSSTND
     EPTEIYTKNA YFSKTDENIH NTVLNTTAGS QSSGRLFGNK TLSTCKLISG LQMERQNLSL
     VDCPIIPPGL VGPIKVWYDE PTFEEIERLN PYLELGGHGK PGSCLSRHRV AIIVPYRDRE
     AHLRILLHNL HSLLTKQQLD YAIFVIEQHE NETFNRAKLM NVGYTEAMKL YDWQCFIFHD
     VDLLAEDDRN IYSCPDQPRH MSVAINKFKY RLPYGSIFGG VSAIRTEQFL KMNGFSNSYW
     GWGGEDDDLS IRVTSLGYKI MRYPLEIARY QMVKHESETK NPINRCRYDL LAKTKVRQQM
     DGISSLKYEC YDLHFLPLFT HIKVKLFEQE SKAQLREEGF KKC
//
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