ALG13_YEAST
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 03-AUG-2022, entry version 156.
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;
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=N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl
CC diphosphodolichol + UDP; Xref=Rhea:RHEA:23380, Rhea:RHEA-COMP:9519,
CC Rhea:RHEA-COMP:9520, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58427;
CC 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}.
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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 PDBsum; 2JZC; -.
DR PDBsum; 2KS6; -.
DR AlphaFoldDB; P53178; -.
DR BMRB; P53178; -.
DR SMR; P53178; -.
DR BioGRID; 33201; 97.
DR ComplexPortal; CPX-1643; UDP-N-acetylglucosamine transferase complex.
DR DIP; DIP-4726N; -.
DR IntAct; P53178; 1.
DR STRING; 4932.YGL047W; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR MaxQB; P53178; -.
DR PaxDb; P53178; -.
DR PRIDE; P53178; -.
DR EnsemblFungi; YGL047W_mRNA; YGL047W; YGL047W.
DR GeneID; 852835; -.
DR KEGG; sce:YGL047W; -.
DR SGD; S000003015; ALG13.
DR VEuPathDB; FungiDB:YGL047W; -.
DR eggNOG; KOG3349; Eukaryota.
DR GeneTree; ENSGT00510000047493; -.
DR HOGENOM; CLU_085408_2_0_1; -.
DR InParanoid; P53178; -.
DR OMA; NYLYYCK; -.
DR BioCyc; MetaCyc:MON3O-20; -.
DR BioCyc; YEAST:MON3O-20; -.
DR BRENDA; 2.4.1.141; 984.
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:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IPI:SGD.
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:SGD.
DR InterPro; IPR007235; Glyco_trans_28_C.
DR Pfam; PF04101; Glyco_tran_28_C; 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 157..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
