ID   ALG12_YEAST             Reviewed;         551 AA.
AC   P53730; D6W1K4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 188.
DE   RecName: Full=Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase {ECO:0000305|PubMed:15987956};
DE            EC=2.4.1.260 {ECO:0000269|PubMed:15987956};
DE   AltName: Full=Asparagine-linked glycosylation protein 12;
DE   AltName: Full=Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase;
DE   AltName: Full=Extracellular mutant protein 39;
DE   AltName: Full=Mannosyltransferase ALG12;
GN   Name=ALG12; Synonyms=ECM39; OrderedLocusNames=YNR030W; ORFNames=N3265;
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=9169873; DOI=10.1038/387s093;
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   [2]
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   [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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION.
RX   PubMed=10336995; DOI=10.1093/glycob/9.6.617;
RA   Burda P., Jakob C.A., Beinhauer J., Hegemann J.H., Aebi M.;
RT   "Ordered assembly of the asymmetrically branched lipid-linked
RT   oligosaccharide in the endoplasmic reticulum is ensured by the substrate
RT   specificity of the individual glycosyltransferases.";
RL   Glycobiology 9:617-625(1999).
RN   [6]
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   [7]
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   [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).
CC   -!- FUNCTION: Mannosyltransferase that operates in the biosynthetic pathway
CC       of dolichol-linked oligosaccharides, the glycan precursors employed in
CC       protein asparagine (N)-glycosylation. The assembly of dolichol-linked
CC       oligosaccharides begins on the cytosolic side of the endoplasmic
CC       reticulum membrane and finishes in its lumen. The sequential addition
CC       of sugars to dolichol pyrophosphate produces dolichol-linked
CC       oligosaccharides containing fourteen sugars, including two GlcNAcs,
CC       nine mannoses and three glucoses. Once assembled, the oligosaccharide
CC       is transferred from the lipid to nascent proteins by
CC       oligosaccharyltransferases. In the lumen of the endoplasmic reticulum,
CC       adds the eighth mannose residue in an alpha-1,6 linkage onto
CC       Man(7)GlcNAc(2)-PP-dolichol to produce Man(8)GlcNAc(2)-PP-dolichol.
CC       {ECO:0000269|PubMed:10336995, ECO:0000269|PubMed:15987956}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
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-diphospho-di-
CC         trans,poly-cis-dolichol + a di-trans,poly-cis-dolichyl beta-D-
CC         mannosyl phosphate = an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-
CC         D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC         (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC         alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + a di-
CC         trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:29535,
CC         Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, Rhea:RHEA-COMP:19518,
CC         Rhea:RHEA-COMP:19519, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683,
CC         ChEBI:CHEBI:58211, ChEBI:CHEBI:132517, ChEBI:CHEBI:132519;
CC         EC=2.4.1.260; Evidence={ECO:0000269|PubMed:15987956};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29536;
CC         Evidence={ECO:0000305|PubMed:15987956};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:15987956}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- MISCELLANEOUS: Present with 3550 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC       {ECO:0000305}.
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DR   EMBL; Z71645; CAA96310.1; -; Genomic_DNA.
DR   EMBL; AY692956; AAT92975.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10570.1; -; Genomic_DNA.
DR   PIR; S63361; S63361.
DR   RefSeq; NP_014427.1; NM_001183207.1.
DR   AlphaFoldDB; P53730; -.
DR   BioGRID; 35854; 122.
DR   DIP; DIP-4259N; -.
DR   FunCoup; P53730; 470.
DR   IntAct; P53730; 23.
DR   MINT; P53730; -.
DR   STRING; 4932.YNR030W; -.
DR   PaxDb; 4932-YNR030W; -.
DR   PeptideAtlas; P53730; -.
DR   EnsemblFungi; YNR030W_mRNA; YNR030W; YNR030W.
DR   GeneID; 855764; -.
DR   KEGG; sce:YNR030W; -.
DR   AGR; SGD:S000005313; -.
DR   SGD; S000005313; ALG12.
DR   VEuPathDB; FungiDB:YNR030W; -.
DR   eggNOG; KOG2516; Eukaryota.
DR   HOGENOM; CLU_008917_4_0_1; -.
DR   InParanoid; P53730; -.
DR   OMA; WWVEVRM; -.
DR   OrthoDB; 19039at2759; -.
DR   BioCyc; MetaCyc:MONOMER3O-256; -.
DR   BioCyc; YEAST:MONOMER3O-256; -.
DR   BRENDA; 2.4.1.260; 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   BioGRID-ORCS; 855764; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P53730; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53730; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IMP:SGD.
DR   GO; GO:0052917; F:dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase activity; IMP:FlyBase.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:SGD.
DR   GO; GO:0009101; P:glycoprotein biosynthetic process; IMP:SGD.
DR   InterPro; IPR005599; GPI_mannosylTrfase.
DR   PANTHER; PTHR22760:SF1; DOL-P-MAN:MAN(7)GLCNAC(2)-PP-DOL ALPHA-1,6-MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 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..551
FT                   /note="Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-
FT                   mannosyltransferase"
FT                   /id="PRO_0000215786"
FT   TOPO_DOM        1..2
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..61
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..89
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..178
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..202
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        224..227
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        249..275
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..303
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        325..331
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        353..365
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        387..417
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        439..551
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   551 AA;  62672 MW;  B08A94BBF260502F CRC64;
     MRWSVLDTVL LTVISFHLIQ APFTKVEESF NIQAIHDILT YSVFDISQYD HLKFPGVVPR
     TFVGAVIIAM LSRPYLYLSS LIQTSRPTSI DVQLVVRGIV GLTNGLSFIY LKNCLQDMFD
     EITEKKKEEN EDKDIYIYDS AGTWFLLFLI GSFHLMFYST RTLPNFVMTL PLTNVALGWV
     LLGRYNAAIF LSALVAIVFR LEVSALSAGI ALFSVIFKKI SLFDAIKFGI FGLGLGSAIS
     ITVDSYFWQE WCLPEVDGFL FNVVAGYASK WGVEPVTAYF THYLRMMFMP PTVLLLNYFG
     YKLAPAKLKI VSLASLFHII VLSFQPHKEW RFIIYAVPSI MLLGATGAAH LWENMKVKKI
     TNVLCLAILP LSIMTSFFIS MAFLYISRMN YPGGEALTSF NDMIVEKNIT NATVHISIPP
     CMTGVTLFGE LNYGVYGINY DKTENTTLLQ EMWPSFDFLI THEPTASQLP FENKTTNHWE
     LVNTTKMFTG FDPTYIKNFV FQERVNVLSL LKQIIFDKTP TVFLKELTAN SIVKSDVFFT
     YKRIKQDEKT D
//