ID ALG13_YEAST Reviewed; 202 AA. AC P53178; D6VU93; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-NOV-2026, entry version 170. 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=YGL047W; 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 [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9234674; RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9; RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.; RT "The characterization of two new clusters of duplicated genes suggests a RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."; RL Yeast 13:861-869(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; DOI=10.1038/387s081; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [3] 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 [4] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [5] 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 [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 ALG14, 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). CC -!- FUNCTION: Involved in protein N-glycosylation. Essential for the second CC step of the dolichol-linked oligosaccharide pathway. CC {ECO:0000269|PubMed:15615718, ECO:0000269|PubMed:16100110}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acetyl-alpha-D-glucosaminyl-diphospho-di-trans,poly-cis- CC dolichol + UDP-N-acetyl-alpha-D-glucosamine = an N,N'- CC diacetylchitobiosyl-diphospho-di-trans,poly-cis-dolichol + UDP + CC H(+); Xref=Rhea:RHEA:23380, Rhea:RHEA-COMP:19507, Rhea:RHEA- CC COMP:19510, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269, ChEBI:CHEBI:57705, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58427; EC=2.4.1.141; CC -!- SUBUNIT: Heterodimer with ALG14 to form a functional enzyme. CC -!- INTERACTION: CC P53178; P53178: ALG13; NbExp=3; IntAct=EBI-23770, EBI-23770; CC P53178; P38242: ALG14; NbExp=3; IntAct=EBI-23770, EBI-21477; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16100110}. CC -!- MISCELLANEOUS: Present with 1950 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z72569; CAA96749.1; -; Genomic_DNA. DR EMBL; BK006941; DAA08054.1; -; Genomic_DNA. DR PIR; S64051; S64051. DR RefSeq; NP_011468.1; NM_001180912.1. DR PDB; 2JZC; NMR; -; A=2-202. DR PDB; 2KS6; NMR; -; A=2-202. DR AlphaFoldDB; P53178; -. DR BMRB; P53178; -. DR SMR; P53178; -. DR BioGRID; 33201; 99. DR ComplexPortal; CPX-1643; UDP-N-acetylglucosamine transferase complex. DR DIP; DIP-4726N; -. DR FunCoup; P53178; 412. DR IntAct; P53178; 1. DR STRING; 4932.YGL047W; -. DR iPTMnet; P53178; -. DR PaxDb; 4932-YGL047W; -. DR PeptideAtlas; P53178; -. DR EnsemblFungi; YGL047W_mRNA; YGL047W; YGL047W. DR GeneID; 852835; -. DR KEGG; sce:YGL047W; -. DR AGR; SGD:S000003015; -. DR SGD; S000003015; ALG13. DR VEuPathDB; FungiDB:YGL047W; -. DR eggNOG; KOG3349; Eukaryota. DR HOGENOM; CLU_085408_2_0_1; -. DR InParanoid; P53178; -. DR OMA; ACDTRGI; -. DR OrthoDB; 20273at2759; -. DR BioCyc; MetaCyc:MONOMER3O-20; -. DR BioCyc; YEAST:MONOMER3O-20; -. DR BRENDA; 2.4.1.141; 984. DR BioGRID-ORCS; 852835; 8 hits in 10 CRISPR screens. DR EvolutionaryTrace; P53178; -. DR PRO; PR:P53178; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P53178; protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0098548; C:cytoplasmic side of Golgi membrane; IDA:ComplexPortal. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IPI:ComplexPortal. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0004577; F:N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IDA:ComplexPortal. DR FunFam; 3.40.50.2000:FF:000244; UDP-N-acetylglucosamine transferase subunit ALG13; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1. DR InterPro; IPR007235; Glyco_trans_28_C. DR InterPro; IPR052474; UDP-GlcNAc_transferase. DR PANTHER; PTHR47043; UDP-N-ACETYLGLUCOSAMINE TRANSFERASE SUBUNIT ALG13; 1. DR PANTHER; PTHR47043:SF1; UDP-N-ACETYLGLUCOSAMINE TRANSFERASE SUBUNIT ALG13; 1. DR Pfam; PF04101; Glyco_tran_28_C; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. PE 1: Evidence at protein level; KW 3D-structure; Endoplasmic reticulum; Glycosyltransferase; KW Reference proteome; Transferase. FT CHAIN 1..202 FT /note="UDP-N-acetylglucosamine transferase subunit ALG13" FT /id="PRO_0000215605" FT STRAND 9..12 FT /evidence="ECO:0007829|PDB:2JZC" FT STRAND 15..17 FT /evidence="ECO:0007829|PDB:2KS6" FT HELIX 20..26 FT /evidence="ECO:0007829|PDB:2JZC" FT HELIX 29..36 FT /evidence="ECO:0007829|PDB:2JZC" FT TURN 37..39 FT /evidence="ECO:0007829|PDB:2JZC" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:2JZC" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:2JZC" FT HELIX 58..62 FT /evidence="ECO:0007829|PDB:2JZC" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:2KS6" FT TURN 73..76 FT /evidence="ECO:0007829|PDB:2KS6" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:2JZC" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:2JZC" FT STRAND 91..96 FT /evidence="ECO:0007829|PDB:2JZC" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:2JZC" FT HELIX 103..110 FT /evidence="ECO:0007829|PDB:2JZC" FT STRAND 114..118 FT /evidence="ECO:0007829|PDB:2JZC" FT HELIX 120..128 FT /evidence="ECO:0007829|PDB:2JZC" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:2KS6" FT HELIX 145..156 FT /evidence="ECO:0007829|PDB:2JZC" FT STRAND 158..162 FT /evidence="ECO:0007829|PDB:2KS6" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:2JZC" FT HELIX 169..176 FT /evidence="ECO:0007829|PDB:2JZC" FT STRAND 187..189 FT /evidence="ECO:0007829|PDB:2JZC" FT HELIX 192..199 FT /evidence="ECO:0007829|PDB:2JZC" SQ SEQUENCE 202 AA; 22661 MW; 9D5CDB366BBC1ED0 CRC64; MGIIEEKALF VTCGATVPFP KLVSCVLSDE FCQELIQYGF VRLIIQFGRN YSSEFEHLVQ ERGGQRESQK IPIDQFGCGD TARQYVLMNG KLKVIGFDFS TKMQSIIRDY SDLVISHAGT GSILDSLRLN KPLIVCVNDS LMDNHQQQIA DKFVELGYVW SCAPTETGLI AGLRASQTEK LKPFPVSHNP SFERLLVETI YS //