ALG3_YEAST
ID ALG3_YEAST Reviewed; 458 AA.
AC P38179; D6VPS1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase;
DE EC=2.4.1.258;
DE AltName: Full=Asparagine-linked glycosylation protein 3;
DE AltName: Full=Dol-P-Man-dependent alpha(1-3)-mannosyltransferase;
DE AltName: Full=Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase;
DE AltName: Full=Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase;
DE AltName: Full=HM-1 killer toxin resistance protein;
GN Name=ALG3; Synonyms=RHK1; OrderedLocusNames=YBL082C; ORFNames=YBL0720;
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=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-406.
RX PubMed=7754714; DOI=10.1002/yea.320100913;
RA Cusick M.E.;
RT "Sequence of a segment of yeast chromosome II shows two novel genes, one
RT almost entirely hydrophobic and the other extremely asparagine-serine
RT rich.";
RL Yeast 10:1251-1256(1994).
RN [5]
RP FUNCTION.
RX PubMed=9108275; DOI=10.1007/s004380050401;
RA Kimura T., Kitamoto N., Kito Y., Iimura Y., Shirai T., Komiyama T.,
RA Furuichi Y., Sakka K., Ohmiya K.;
RT "A novel yeast gene, RHK1, is involved in the synthesis of the cell wall
RT receptor for the HM-1 killer toxin that inhibits beta-1,3-glucan
RT synthesis.";
RL Mol. Gen. Genet. 254:139-147(1997).
RN [6]
RP CHARACTERIZATION, AND VARIANT ALG3-1.
RX PubMed=8842708; DOI=10.1093/glycob/6.4.439;
RA Aebi M., Gassenhuber J., Domdey H., Te Heesen S.;
RT "Cloning and characterization of the ALG3 gene of Saccharomyces
RT cerevisiae.";
RL Glycobiology 6:439-444(1996).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=11308030; DOI=10.1515/bc.2001.039;
RA Sharma C.B., Knauer R., Lehle L.;
RT "Biosynthesis of lipid-linked oligosaccharides in yeast: the ALG3 gene
RT encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase.";
RL Biol. Chem. 382:321-328(2001).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3
CC linkage to Man(5)GlcNAc(2)-PP-Dol. Sensitive to H.mrakii HM-1 killer
CC toxin. {ECO:0000269|PubMed:11308030, ECO:0000269|PubMed:9108275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a
CC dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+);
CC Xref=Rhea:RHEA:29527, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:12627, Rhea:RHEA-COMP:12628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132515,
CC ChEBI:CHEBI:132516; EC=2.4.1.258;
CC Evidence={ECO:0000269|PubMed:11308030};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 58 family.
CC {ECO:0000305}.
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DR EMBL; X79489; CAA56024.1; -; Genomic_DNA.
DR EMBL; Z35844; CAA84904.1; -; Genomic_DNA.
DR EMBL; M89908; AAA75352.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07041.1; -; Genomic_DNA.
DR PIR; S45424; S45424.
DR RefSeq; NP_009471.1; NM_001178322.1.
DR AlphaFoldDB; P38179; -.
DR BioGRID; 32621; 183.
DR DIP; DIP-4854N; -.
DR MINT; P38179; -.
DR STRING; 4932.YBL082C; -.
DR CAZy; GT58; Glycosyltransferase Family 58.
DR MaxQB; P38179; -.
DR PaxDb; P38179; -.
DR PRIDE; P38179; -.
DR DNASU; 852196; -.
DR EnsemblFungi; YBL082C_mRNA; YBL082C; YBL082C.
DR GeneID; 852196; -.
DR KEGG; sce:YBL082C; -.
DR SGD; S000000178; ALG3.
DR VEuPathDB; FungiDB:YBL082C; -.
DR eggNOG; KOG2762; Eukaryota.
DR GeneTree; ENSGT00390000013904; -.
DR HOGENOM; CLU_035382_3_0_1; -.
DR InParanoid; P38179; -.
DR OMA; DWETYMI; -.
DR BioCyc; MetaCyc:YBL082C-MON; -.
DR BioCyc; YEAST:YBL082C-MON; -.
DR BRENDA; 2.4.1.258; 984.
DR Reactome; R-SCE-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR UniPathway; UPA00378; -.
DR PRO; PR:P38179; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38179; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IMP:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052925; F:dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity; IDA:SGD.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IDA:SGD.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
DR InterPro; IPR007873; Glycosyltransferase_ALG3.
DR PANTHER; PTHR12646; PTHR12646; 1.
DR Pfam; PF05208; ALG3; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..458
FT /note="Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-
FT mannosyltransferase"
FT /id="PRO_0000080565"
FT TOPO_DOM 1..41
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..137
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..216
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..302
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..381
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..458
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MUTAGEN 275
FT /note="A->V: In ALG3-1; leads to an underglycosylation of
FT secretory proteins."
FT CONFLICT 86
FT /note="G -> R (in Ref. 4; AAA75352)"
FT /evidence="ECO:0000305"
FT CONFLICT 187..198
FT /note="LGAIVASRCHQR -> FRGYRGQQVPSA (in Ref. 4; AAA75352)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="S -> Q (in Ref. 4; AAA75352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 52861 MW; 1C2FEAD6D459C249 CRC64;
MEGEQSPQGE KSLQRKQFVR PPLDLWQDLK DGVRYVIFDC RANLIVMPLL ILFESMLCKI
IIKKVAYTEI DYKAYMEQIE MIQLDGMLDY SQVSGGTGPL VYPAGHVLIY KMMYWLTEGM
DHVERGQVFF RYLYLLTLAL QMACYYLLHL PPWCVVLACL SKRLHSIYVL RLFNDCFTTL
FMVVTVLGAI VASRCHQRPK LKKSLALVIS ATYSMAVSIK MNALLYFPAM MISLFILNDA
NVILTLLDLV AMIAWQVAVA VPFLRSFPQQ YLHCAFNFGR KFMYQWSINW QMMDEEAFND
KRFHLALLIS HLIALTTLFV TRYPRILPDL WSSLCHPLRK NAVLNANPAK TIPFVLIASN
FIGVLFSRSL HYQFLSWYHW TLPILIFWSG MPFFVGPIWY VLHEWCWNSY PPNSQASTLL
LALNTVLLLL LALTQLSGSV ALAKSHLRTT SSMEKKLN
