YUR1_YEAST
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 03-AUG-2022, entry version 173.
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<787::aid-yea954>3.0.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; 154.
DR DIP; DIP-2605N; -.
DR IntAct; P26725; 2.
DR MINT; P26725; -.
DR STRING; 4932.YJL139C; -.
DR CAZy; GT15; Glycosyltransferase Family 15.
DR MaxQB; P26725; -.
DR PaxDb; P26725; -.
DR PRIDE; P26725; -.
DR EnsemblFungi; YJL139C_mRNA; YJL139C; YJL139C.
DR GeneID; 853302; -.
DR KEGG; sce:YJL139C; -.
DR SGD; S000003675; YUR1.
DR VEuPathDB; FungiDB:YJL139C; -.
DR eggNOG; KOG4472; Eukaryota.
DR GeneTree; ENSGT00940000176287; -.
DR HOGENOM; CLU_024327_4_2_1; -.
DR InParanoid; P26725; -.
DR OMA; DWYFRVE; -.
DR BioCyc; YEAST:YJL139C-MON; -.
DR UniPathway; UPA00378; -.
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: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:0000030; F:mannosyltransferase activity; IDA:SGD.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:SGD.
DR GO; GO:0097502; P:mannosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:SGD.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002685; Glyco_trans_15.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR31121; PTHR31121; 1.
DR Pfam; PF01793; Glyco_transf_15; 1.
DR PIRSF; PIRSF018153; Glyco_trans_15; 1.
DR SUPFAM; SSF53448; SSF53448; 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
