ID   ALG13_YARLI             Reviewed;         196 AA.
AC   Q6C3P1;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=UDP-N-acetylglucosamine transferase subunit ALG13;
DE            EC=2.4.1.141;
DE   AltName: Full=Asparagine-linked glycosylation protein 13;
GN   Name=ALG13; OrderedLocusNames=YALI0E33275g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Involved in protein N-glycosylation. Essential for the second
CC       step of the dolichol-linked oligosaccharide pathway (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-
CC         acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl
CC         diphosphodolichol + UDP; Xref=Rhea:RHEA:23380, Rhea:RHEA-COMP:9519,
CC         Rhea:RHEA-COMP:9520, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58427;
CC         EC=2.4.1.141;
CC   -!- SUBUNIT: Heterodimer with ALG14 to form a functional enzyme.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; CR382131; CAG80325.1; -; Genomic_DNA.
DR   RefSeq; XP_504721.1; XM_504721.1.
DR   AlphaFoldDB; Q6C3P1; -.
DR   SMR; Q6C3P1; -.
DR   STRING; 4952.CAG80325; -.
DR   EnsemblFungi; CAG80325; CAG80325; YALI0_E33275g.
DR   GeneID; 2911943; -.
DR   KEGG; yli:YALI0E33275g; -.
DR   VEuPathDB; FungiDB:YALI0_E33275g; -.
DR   HOGENOM; CLU_085408_2_0_1; -.
DR   InParanoid; Q6C3P1; -.
DR   OMA; NYLYYCK; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0004577; F:N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR   InterPro; IPR039042; Alg13-like.
DR   InterPro; IPR007235; Glyco_trans_28_C.
DR   PANTHER; PTHR12867; PTHR12867; 1.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..196
FT                   /note="UDP-N-acetylglucosamine transferase subunit ALG13"
FT                   /id="PRO_0000215604"
SQ   SEQUENCE   196 AA;  22071 MW;  BF73789F8AAA17C1 CRC64;
     MHESSALSKL YNWDCSVVFI ILNIYTTMLV LVTTGGTVPF EALIELVLSH ESITTLSQLG
     FSKMRVQYGR GNRHIFTKHH KEGVMSITGF EYTDDLAGEM SRAHLVISHA GTGSVLDALR
     IGKHPVVVVN SKLMDNHQIE IAEELFRKRH LLVSGDTDSV GFIKALKMHR EYLFETLPDP
     EEGILQRIIE ETVSFM