ID KTR5_YEAST Reviewed; 522 AA. AC P53966; D6W1F0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 168. DE RecName: Full=Probable mannosyltransferase KTR5; DE EC=2.4.1.-; GN Name=KTR5; OrderedLocusNames=YNL029C; ORFNames=N2755; 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; 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 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 [3] RP CHARACTERIZATION. RX PubMed=9090056; RX DOI=10.1002/(sici)1097-0061(19970315)13:3<267::aid-yea72>3.0.co;2-k; RA Lussier M., Sdicu A.-M., Winnett E., Vo D.H., Sheraton J., Duesterhoeft A., RA Storms R.K., Bussey H.; RT "Completion of the Saccharomyces cerevisiae genome sequence allows RT identification of KTR5, KTR6 and KTR7 and definition of the nine-membered RT KRE2/MNT1 mannosyltransferase gene family in this organism."; RL Yeast 13:267-274(1997). RN [4] 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 that transfers an alpha-D- CC mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, CC forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II CC membrane protein {ECO:0000305}. CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 15 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z71305; CAA95891.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10516.1; -; Genomic_DNA. DR PIR; S62941; S62941. DR RefSeq; NP_014369.3; NM_001182868.3. DR AlphaFoldDB; P53966; -. DR SMR; P53966; -. DR BioGRID; 35798; 43. DR DIP; DIP-6646N; -. DR IntAct; P53966; 1. DR STRING; 4932.YNL029C; -. DR CAZy; GT15; Glycosyltransferase Family 15. DR GlyCosmos; P53966; 1 site, No reported glycans. DR GlyGen; P53966; 1 site. DR iPTMnet; P53966; -. DR MaxQB; P53966; -. DR PaxDb; 4932-YNL029C; -. DR PeptideAtlas; P53966; -. DR TopDownProteomics; P53966; -. DR EnsemblFungi; YNL029C_mRNA; YNL029C; YNL029C. DR GeneID; 855703; -. DR KEGG; sce:YNL029C; -. DR AGR; SGD:S000004974; -. DR SGD; S000004974; KTR5. DR VEuPathDB; FungiDB:YNL029C; -. DR eggNOG; KOG4472; Eukaryota. DR GeneTree; ENSGT00940000176287; -. DR HOGENOM; CLU_024327_2_0_1; -. DR InParanoid; P53966; -. DR OMA; TIDEISW; -. DR OrthoDB; 1981584at2759; -. DR BioCyc; YEAST:G3O-33066-MONOMER; -. DR BioGRID-ORCS; 855703; 1 hit in 10 CRISPR screens. DR ChiTaRS; KTR5; yeast. DR PRO; PR:P53966; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P53966; Protein. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD. DR GO; GO:0005794; C:Golgi apparatus; ISS:SGD. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central. DR GO; GO:0000030; F:mannosyltransferase activity; ISS:SGD. DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central. DR GO; GO:0097502; P:mannosylation; IBA:GO_Central. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR InterPro; IPR002685; Glyco_trans_15. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR31121; ALPHA-1,2 MANNOSYLTRANSFERASE KTR1; 1. DR PANTHER; PTHR31121:SF2; MANNOSYLTRANSFERASE KTR5-RELATED; 1. DR Pfam; PF01793; Glyco_transf_15; 2. DR PIRSF; PIRSF018153; Glyco_trans_15; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. PE 1: Evidence at protein level; KW Glycoprotein; Glycosyltransferase; Membrane; Reference proteome; KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..522 FT /note="Probable mannosyltransferase KTR5" FT /id="PRO_0000208246" FT TOPO_DOM 1..16 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 17..37 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 38..522 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 38..82 FT /note="Stem region" FT /evidence="ECO:0000250" FT REGION 83..522 FT /note="Catalytic" FT /evidence="ECO:0000250" FT ACT_SITE 363 FT /note="Nucleophile" FT /evidence="ECO:0000255" FT CARBOHYD 86 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 522 AA; 61728 MW; 3F9D75D3F09D4110 CRC64; MLLIRRTINA FLGCIHCNLT ATCILIAFVI TMYVVLVSEP ASVDGTMGNF LPFSKMDLAT KRDRPFYSNC VNTQDYLLNP SYIKQNASFV MLTRNGELED VIKTINSIEE HFNQWFHYPY VFLNDQPFEE DFKAKVRDVT VGALVEFGTI DEISWNFPSD VKDTFEFYNA IEDQGDRSIL YGNLESYHKM CRFYSGLFYK HPLVQKYEWY WRLEPDVEFF CDITYDPFLE MLRTNKKYGF TIIIPELYWT VPNLFRHTKS FISQKGVTLG SLWKLFTKDY DIFESDDPEL RDWINYDFQA KAKISEKIAI EQLLKKGDDF QQINDDKEGI MNLIHKARSR KHIVEDKFFN EEYNLCHFWS NFEIARLSVF DNDIYNSFFQ YLEKSGGFWK ERWGDAPVHS IGLSLTLDLD DVHYFRDIGY RHSTIQHCPH NAMGNEEFSY LASDSKFKRK NAAYDEGREF GCGCRCRCPK KKREIEDSMG FCVNIWVNLL NQQRGHERHV EALNGNEMEE HIREDYLRQF GN //