ID   ALG14_DEBHA             Reviewed;         232 AA.
AC   Q6BMD0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=UDP-N-acetylglucosamine transferase subunit ALG14;
DE   AltName: Full=Asparagine-linked glycosylation protein 14;
GN   Name=ALG14; OrderedLocusNames=DEHA2F06512g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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. Anchors the
CC       catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with ALG13 to form a functional enzyme.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein
CC       {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single-
CC       pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ALG14 family. {ECO:0000305}.
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DR   EMBL; CR382138; CAG88973.2; -; Genomic_DNA.
DR   RefSeq; XP_460641.2; XM_460641.1.
DR   AlphaFoldDB; Q6BMD0; -.
DR   STRING; 4959.XP_460641.2; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   EnsemblFungi; CAG88973; CAG88973; DEHA2F06512g.
DR   GeneID; 2903152; -.
DR   KEGG; dha:DEHA2F06512g; -.
DR   VEuPathDB; FungiDB:DEHA2F06512g; -.
DR   eggNOG; KOG3339; Eukaryota.
DR   HOGENOM; CLU_064541_2_0_1; -.
DR   InParanoid; Q6BMD0; -.
DR   OMA; GPGTCCI; -.
DR   OrthoDB; 1449763at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR   InterPro; IPR013969; Oligosacch_biosynth_Alg14.
DR   PANTHER; PTHR12154; PTHR12154; 1.
DR   Pfam; PF08660; Alg14; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..232
FT                   /note="UDP-N-acetylglucosamine transferase subunit ALG14"
FT                   /id="PRO_0000123814"
FT   TOPO_DOM        1..10
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P38242"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..232
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38242"
SQ   SEQUENCE   232 AA;  26041 MW;  2D5C562A5842A72B CRC64;
     MDFESQLCIK VVLLLLPFFI IGIRLLWVLP AVNSPAMGSE KEKGLSQIPS ELRGSNIMIF
     LGSGGHTGEM MRILANVDLN NFNRTWVTSS GDSTSILKCK KYEDERLTSG QNKSDYLVLH
     RARTVGESII SSVFSTVRSL ISTIKHLYEL PQFPSILLLN GPGTSVPLAY IIFLLKFLGL
     CKTRIIYIES LARVKQLSVS GLLILPITDR FIVQWKQLAV KYKRAEYYGI LI