ALG9_YEAST
ID ALG9_YEAST Reviewed; 555 AA.
AC P53868; D6W0X1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Alpha-1,2-mannosyltransferase ALG9;
DE EC=2.4.1.259;
DE EC=2.4.1.261;
DE AltName: Full=Asparagine-linked glycosylation protein 9;
DE AltName: Full=Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase;
DE AltName: Full=Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase;
GN Name=ALG9; OrderedLocusNames=YNL219C; ORFNames=N1295;
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=SS328;
RX PubMed=8692962; DOI=10.1073/pnas.93.14.7160;
RA Burda P., Te Heesen S., Brachat A., Wach A., Duesterhoeft A., Aebi M.;
RT "Stepwise assembly of the lipid-linked oligosaccharide in the endoplasmic
RT reticulum of Saccharomyces cerevisiae: identification of the ALG9 gene
RT encoding a putative mannosyl transferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7160-7165(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=15987956; DOI=10.1093/glycob/cwj002;
RA Frank C.G., Aebi M.;
RT "ALG9 mannosyltransferase is involved in two different steps of lipid-
RT linked oligosaccharide biosynthesis.";
RL Glycobiology 15:1156-1163(2005).
RN [4]
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 [5]
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).
CC -!- FUNCTION: Catalyzes the transfer of mannose from Dol-P-Man to lipid-
CC linked oligosaccharides. {ECO:0000269|PubMed:15987956}.
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->3)-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:29531,
CC Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12628,
CC Rhea:RHEA-COMP:12629, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58211, ChEBI:CHEBI:132516, ChEBI:CHEBI:132517;
CC EC=2.4.1.259; Evidence={ECO:0000269|PubMed:15987956};
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->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC (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->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-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:29539, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:12630, Rhea:RHEA-COMP:12631, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132519,
CC ChEBI:CHEBI:132520; EC=2.4.1.261;
CC Evidence={ECO:0000269|PubMed:15987956};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000305}.
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DR EMBL; X96417; CAA65277.1; -; Genomic_DNA.
DR EMBL; Z71495; CAA96122.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10337.1; -; Genomic_DNA.
DR PIR; S63177; S63177.
DR RefSeq; NP_014180.1; NM_001183057.1.
DR AlphaFoldDB; P53868; -.
DR BioGRID; 35617; 284.
DR DIP; DIP-4288N; -.
DR IntAct; P53868; 7.
DR STRING; 4932.YNL219C; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR iPTMnet; P53868; -.
DR MaxQB; P53868; -.
DR PaxDb; P53868; -.
DR PRIDE; P53868; -.
DR EnsemblFungi; YNL219C_mRNA; YNL219C; YNL219C.
DR GeneID; 855502; -.
DR KEGG; sce:YNL219C; -.
DR SGD; S000005163; ALG9.
DR VEuPathDB; FungiDB:YNL219C; -.
DR eggNOG; KOG2515; Eukaryota.
DR GeneTree; ENSGT00950000183090; -.
DR HOGENOM; CLU_018152_1_1_1; -.
DR InParanoid; P53868; -.
DR OMA; GKDWHRY; -.
DR BioCyc; MetaCyc:YNL219C-MON; -.
DR BioCyc; YEAST:YNL219C-MON; -.
DR BRENDA; 2.4.1.259; 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:P53868; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53868; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IMP:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0052926; F:dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IDA:SGD.
DR GO; GO:0052918; F:dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IDA:SGD.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP:SGD.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:SGD.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:SGD.
DR InterPro; IPR039484; ALG9-like.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR PANTHER; PTHR22760:SF2; PTHR22760:SF2; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..555
FT /note="Alpha-1,2-mannosyltransferase ALG9"
FT /id="PRO_0000215789"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..62
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..113
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..213
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..316
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..555
FT /note="Lumenal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 555 AA; 63777 MW; 108ED4E0B0C2AAA7 CRC64;
MNCKAVTISL LLLLFLTRVY IQPTFSLISD CDETFNYWEP LNLLVRGFGK QTWEYSPEYS
IRSWAFLLPF YCILYPVNKF TDLESHWNFF ITRACLGFFS FIMEFKLHRE IAGSLALQIA
NIWIIFQLFN PGWFHASVEL LPSAVAMLLY VGATRHSLRY LSTGSTSNFT KSLAYNFLAS
ILGWPFVLIL SLPLCLHYLF NHRIISTIRT AFDCCLIFSL TAFAVIVTDS IFYGKLAPVS
WNILFYNVIN ASEESGPNIF GVEPWYYYPL NLLLNFPLPV LVLAILGIFH LRLWPLWASL
FTWIAVFTQQ PHKEERFLYP IYGLITLSAS IAFYKVLNLF NRKPILKKGI KLSVLLIVAG
QAMSRIVALV NNYTAPIAVY EQFSSLNQGG VKAPVVNVCT GREWYHFPSS FLLPDNHRLK
FVKSGFDGLL PGDFPESGSI FKKIRTLPKG MNNKNIYDTG KEWPITRCDY FIDIVAPINL
TKDVFNPLHL MDNWNKLACA AFIDGENSKI LGRAFYVPEP INRIMQIVLP KQWNQVYGVR
YIDYCLFEKP TETTN
