ID   YUR1_YEAST              Reviewed;         428 AA.
AC   P26725; D6VW45;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   04-NOV-2026, entry version 190.
DE   RecName: Full=Probable mannosyltransferase YUR1;
DE            EC=2.4.1.-;
GN   Name=YUR1; OrderedLocusNames=YJL139C; ORFNames=J0657;
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].
RX   PubMed=2041753; DOI=10.1093/nar/19.10.2781;
RA   Foreman P.K., Davis R.W., Sachs A.B.;
RT   "The Saccharomyces cerevisiae RPB4 gene is tightly linked to the TIF2
RT   gene.";
RL   Nucleic Acids Res. 19:2781-2781(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8813765;
RX   DOI=10.1002/(sici)1097-0061(19960630)12:8%3c787::aid-yea954%3e3.0.co;2-4;
RA   Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT   "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT   chromosome X reveals 14 known genes and 13 new open reading frames
RT   including homologues of genes clustered on the right arm of chromosome
RT   XI.";
RL   Yeast 12:787-797(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   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).
CC   -!- FUNCTION: Possible glycosyltransferase involved in N-linked
CC       glycosylation. Transfers an alpha-D-mannosyl residue from GDP-mannose
CC       into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-
CC       D-mannose linkage.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC       membrane protein.
CC   -!- MISCELLANEOUS: Present with 6400 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 15 family.
CC       {ECO:0000305}.
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DR   EMBL; X58099; CAA41111.1; -; Genomic_DNA.
DR   EMBL; X87371; CAA60816.1; -; Genomic_DNA.
DR   EMBL; Z49414; CAA89434.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08661.1; -; Genomic_DNA.
DR   PIR; S36856; S36856.
DR   RefSeq; NP_012396.1; NM_001181572.1.
DR   AlphaFoldDB; P26725; -.
DR   SMR; P26725; -.
DR   BioGRID; 33618; 158.
DR   DIP; DIP-2605N; -.
DR   FunCoup; P26725; 37.
DR   IntAct; P26725; 3.
DR   STRING; 4932.YJL139C; -.
DR   CAZy; GT15; Glycosyltransferase Family 15.
DR   GlyCosmos; P26725; 5 sites, No reported glycans.
DR   GlyGen; P26725; 5 sites.
DR   PaxDb; 4932-YJL139C; -.
DR   PeptideAtlas; P26725; -.
DR   EnsemblFungi; YJL139C_mRNA; YJL139C; YJL139C.
DR   GeneID; 853302; -.
DR   KEGG; sce:YJL139C; -.
DR   AGR; SGD:S000003675; -.
DR   SGD; S000003675; YUR1.
DR   VEuPathDB; FungiDB:YJL139C; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   HOGENOM; CLU_024327_4_2_1; -.
DR   InParanoid; P26725; -.
DR   OMA; ADEVHHF; -.
DR   OrthoDB; 439943at2759; -.
DR   BioCyc; YEAST:YJL139C-MONOMER; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 853302; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P26725; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P26725; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000030; F:mannosyltransferase activity; IDA:SGD.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:SGD.
DR   GO; GO:0009101; P:glycoprotein biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IMP:SGD.
DR   FunFam; 3.90.550.10:FF:000051; Alpha-1,2-mannosyltransferase (Ktr4); 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   InterPro; IPR002685; Glyco_trans_15.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR31121; ALPHA-1,2 MANNOSYLTRANSFERASE KTR1; 1.
DR   PANTHER; PTHR31121:SF10; MANNOSYLTRANSFERASE KTR2-RELATED; 1.
DR   Pfam; PF01793; Glyco_transf_15; 1.
DR   PIRSF; PIRSF018153; Glyco_trans_15; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..428
FT                   /note="Probable mannosyltransferase YUR1"
FT                   /id="PRO_0000208250"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..24
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        25..428
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          25..88
FT                   /note="Stem region"
FT                   /evidence="ECO:0000250"
FT   REGION          89..428
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        313
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   428 AA;  50836 MW;  E4F1CF97480DB3CA CRC64;
     MAKGGSLYIV GIFLPIWTFM IYIFGKELFL IRKYQKIDST YTALSQRVKE QYDTSRRRNY
     FPKVKLSRNS YDDYTLNYTR QNDSDSFHLR ENATILMLVR NSELEGALDS MRSLEDRFNN
     KYHYDWTFLN DVPFDQDFIE ATTSMASGKT QYALIPPEDW NRPQWINDTL FEERLRVMED
     EGVLYGGSKS YRNMCRFNSG FFFRQSILDN YDYYFRVEPN VKYYCDFPYD PFRVMRLKGK
     KYGFVISLYE YEETIPTLWD AVEEYLVASE ETILRKEDSA YAFLTDSGLV GKHYPVVEAN
     SDYNLCHFWS NFEIGDLNFF RSDEYKHFFE TLDAKGGFYY ERWGDAPVHS IGVSLLLRPD
     EIIHFDELGY FHSPFGTCPA SYAVRLDQRC RCKSDDESVI DITPHSCLMR WWKNGSGKYF
     LKEEQDEI
//