ID   ALG14_CANGA             Reviewed;         242 AA.
AC   Q6FV75;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=UDP-N-acetylglucosamine transferase subunit ALG14;
DE   AltName: Full=Asparagine-linked glycosylation protein 14;
GN   Name=ALG14; OrderedLocusNames=CAGL0E04180g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380951; CAG58788.1; -; Genomic_DNA.
DR   RefSeq; XP_445869.1; XM_445869.1.
DR   AlphaFoldDB; Q6FV75; -.
DR   STRING; 5478.XP_445869.1; -.
DR   EnsemblFungi; CAG58788; CAG58788; CAGL0E04180g.
DR   GeneID; 2887310; -.
DR   KEGG; cgr:CAGL0E04180g; -.
DR   CGD; CAL0128750; CAGL0E04180g.
DR   VEuPathDB; FungiDB:CAGL0E04180g; -.
DR   eggNOG; KOG3339; Eukaryota.
DR   HOGENOM; CLU_064541_2_2_1; -.
DR   InParanoid; Q6FV75; -.
DR   OMA; GPGTCCI; -.
DR   Proteomes; UP000002428; Chromosome E.
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..242
FT                   /note="UDP-N-acetylglucosamine transferase subunit ALG14"
FT                   /id="PRO_0000123812"
FT   TOPO_DOM        1..6
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P38242"
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P38242"
SQ   SEQUENCE   242 AA;  27335 MW;  9EA27118E191F599 CRC64;
     MPFLSTAHLC ALLLILGCFY IGRLIKVIPI LRFACAGEAE IKPLFIQPKS NDGIHLFVFL
     GSGGHTGEML RLLQNHQEVL LNKRNTFYIG YSDDDSKARF LSMVEKYDFK AERIHFYPFA
     KAREVNAGPI ASIVTISKTL LTGFTNVLSI KMNTLGQPHL TLLNGPGTCC IINFWLKLLE
     WLIYIPYLSN GSNVVYIESL ARIESLSLTG KILYLLADVF VVQWEELKVR KAPRSEYYGI
     LV