ID   ALG14_KLULA             Reviewed;         236 AA.
AC   Q6CJG3;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=UDP-N-acetylglucosamine transferase subunit ALG14;
DE   AltName: Full=Asparagine-linked glycosylation protein 14;
GN   Name=ALG14; OrderedLocusNames=KLLA0F18865g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98634.1; -; Genomic_DNA.
DR   RefSeq; XP_455926.1; XM_455926.1.
DR   AlphaFoldDB; Q6CJG3; -.
DR   STRING; 28985.XP_455926.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   EnsemblFungi; CAG98634; CAG98634; KLLA0_F18865g.
DR   GeneID; 2895545; -.
DR   KEGG; kla:KLLA0_F18865g; -.
DR   eggNOG; KOG3339; Eukaryota.
DR   HOGENOM; CLU_064541_2_2_1; -.
DR   InParanoid; Q6CJG3; -.
DR   OMA; GPGTCCI; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IEA:EnsemblFungi.
DR   GO; GO:0004577; F:N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:EnsemblFungi.
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..236
FT                   /note="UDP-N-acetylglucosamine transferase subunit ALG14"
FT                   /id="PRO_0000123815"
FT   TOPO_DOM        1..7
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P38242"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..236
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38242"
SQ   SEQUENCE   236 AA;  26669 MW;  BA1F8AD2D9531C39 CRC64;
     MLLTTAWCLL IWSVTLLLVR ICLVIPIFHS SREAGPLTKD KDNVGGRMKN LVLFIFLGSG
     GHTGEMLRLI EHYQGMLLES AVTIHVGYSD DDSIIKFKNK IHQISVSNTL RAKVIYHRFD
     KARDVGSSLA GSIKSIIKTA IRSMVLTYRI KSSMRGHPNL TLLNGPGTCC IITFWLKLYH
     IFLWQPSKIV YVESLARTNR LSLTGMILYP LADEFVVQWA DLLPIYPKAK YYGVLV