ALG14_YEAST
ID ALG14_YEAST Reviewed; 237 AA.
AC P38242; D6VQ69;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=UDP-N-acetylglucosamine transferase subunit ALG14;
DE AltName: Full=Asparagine-linked glycosylation protein 14;
GN Name=ALG14; OrderedLocusNames=YBR070C; ORFNames=YBR0711;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7985423; DOI=10.1002/yea.320100711;
RA van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M.,
RA Steensma H.Y.;
RT "Sequence analysis of a 31 kb DNA fragment from the right arm of
RT Saccharomyces cerevisiae chromosome II.";
RL Yeast 10:959-964(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15282802; DOI=10.1002/yea.1133;
RA Sundin B.A., Chiu C.-H., Riffle M., Davis T.N., Muller E.G.D.;
RT "Localization of proteins that are coordinately expressed with Cln2 during
RT the cell cycle.";
RL Yeast 21:793-800(2004).
RN [6]
RP FUNCTION.
RX PubMed=15615718; DOI=10.1074/jbc.m413941200;
RA Chantret I., Dancourt J., Barbat A., Moore S.E.H.;
RT "Two proteins homologous to the N- and C-terminal domains of the bacterial
RT glycosyltransferase Murg are required for the second step of dolichyl-
RT linked oligosaccharide synthesis in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:9236-9242(2005).
RN [7]
RP FUNCTION, INTERACTION WITH ALG13, AND SUBCELLULAR LOCATION.
RX PubMed=16100110; DOI=10.1074/jbc.m507569200;
RA Gao X.-D., Tachikawa H., Sato T., Jigami Y., Dean N.;
RT "Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum
RT to form a novel bipartite UDP-N-acetylglucosamine transferase required for
RT the second step of N-linked glycosylation.";
RL J. Biol. Chem. 280:36254-36262(2005).
RN [8]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=17686769; DOI=10.1074/jbc.m704410200;
RA Averbeck N., Keppler-Ross S., Dean N.;
RT "Membrane topology of the Alg14 endoplasmic reticulum UDP-GlcNAc
RT transferase subunit.";
RL J. Biol. Chem. 282:29081-29088(2007).
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. {ECO:0000269|PubMed:15615718,
CC ECO:0000269|PubMed:16100110}.
CC -!- SUBUNIT: Heterodimer with ALG13 to form a functional enzyme.
CC -!- INTERACTION:
CC P38242; P53178: ALG13; NbExp=3; IntAct=EBI-21477, EBI-23770;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:16100110,
CC ECO:0000269|PubMed:17686769}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:15282802}; Single-
CC pass membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ALG14 family. {ECO:0000305}.
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DR EMBL; X76294; CAA53927.1; -; Genomic_DNA.
DR EMBL; Z35939; CAA85014.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07189.1; -; Genomic_DNA.
DR PIR; S45463; S45463.
DR RefSeq; NP_009626.1; NM_001178418.1.
DR AlphaFoldDB; P38242; -.
DR SMR; P38242; -.
DR BioGRID; 32773; 303.
DR ComplexPortal; CPX-1643; UDP-N-acetylglucosamine transferase complex.
DR DIP; DIP-5670N; -.
DR IntAct; P38242; 5.
DR MINT; P38242; -.
DR STRING; 4932.YBR070C; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; P38242; -.
DR MaxQB; P38242; -.
DR PaxDb; P38242; -.
DR PRIDE; P38242; -.
DR EnsemblFungi; YBR070C_mRNA; YBR070C; YBR070C.
DR GeneID; 852362; -.
DR KEGG; sce:YBR070C; -.
DR SGD; S000000274; ALG14.
DR VEuPathDB; FungiDB:YBR070C; -.
DR eggNOG; KOG3339; Eukaryota.
DR GeneTree; ENSGT00390000002579; -.
DR HOGENOM; CLU_064541_2_2_1; -.
DR InParanoid; P38242; -.
DR OMA; GPGTCCI; -.
DR BioCyc; MetaCyc:MON3O-23; -.
DR BioCyc; YEAST:MON3O-23; -.
DR BRENDA; 2.4.1.141; 984.
DR PRO; PR:P38242; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38242; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:SGD.
DR GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IPI:SGD.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IMP:SGD.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IDA:SGD.
DR InterPro; IPR013969; Oligosacch_biosynth_Alg14.
DR PANTHER; PTHR12154; PTHR12154; 1.
DR Pfam; PF08660; Alg14; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..237
FT /note="UDP-N-acetylglucosamine transferase subunit ALG14"
FT /id="PRO_0000123818"
FT TOPO_DOM 1..7
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:17686769"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17686769"
SQ SEQUENCE 237 AA; 27035 MW; 53E2D17E18593156 CRC64;
MKTAYLASLV LIVSTAYVIR LIAILPFFHT QAGTEKDTKD GVNLLKIRKS SKKPLKIFVF
LGSGGHTGEM IRLLENYQDL LLGKSIVYLG YSDEASRQRF AHFIKKFGHC KVKYYEFMKA
REVKATLLQS VKTIIGTLVQ SFVHVVRIRF AMCGSPHLFL LNGPGTCCII SFWLKIMELL
LPLLGSSHIV YVESLARINT PSLTGKILYW VVDEFIVQWQ ELRDNYLPRS KWFGILV
