KTR3_YEAST
ID KTR3_YEAST Reviewed; 404 AA.
AC P38130; D6VQK3; E9P931;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Probable mannosyltransferase KTR3;
DE EC=2.4.1.-;
GN Name=KTR3; OrderedLocusNames=YBR205W; ORFNames=YBR1445;
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=ATCC 204508 / S288c;
RX PubMed=8368014; DOI=10.1002/yea.320090714;
RA Bussereau F., Mallet L., Gaillon L., Jacquet M.;
RT "A 12.8 kb segment, on the right arm of chromosome II from Saccharomyces
RT cerevisiae including part of the DUR1,2 gene, contains five putative new
RT genes.";
RL Yeast 9:797-806(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 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 [6]
RP INTERACTION WITH SVP26.
RX PubMed=16107716; DOI=10.1128/mcb.25.17.7696-7710.2005;
RA Inadome H., Noda Y., Adachi H., Yoda K.;
RT "Immunoisolation of the yeast Golgi subcompartments and characterization of
RT a novel membrane protein, Svp26, discovered in the Sed5-containing
RT compartments.";
RL Mol. Cell. Biol. 25:7696-7710(2005).
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 -!- SUBUNIT: Interacts with SVP26. {ECO:0000269|PubMed:16107716}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 704 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; Z21487; CAA79693.1; -; Genomic_DNA.
DR EMBL; Z36074; CAA85169.1; -; Genomic_DNA.
DR EMBL; AY693211; AAT93230.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07323.1; -; Genomic_DNA.
DR PIR; S34031; S34031.
DR RefSeq; NP_009764.3; NM_001178553.3.
DR AlphaFoldDB; P38130; -.
DR SMR; P38130; -.
DR BioGRID; 32902; 76.
DR DIP; DIP-1723N; -.
DR IntAct; P38130; 17.
DR MINT; P38130; -.
DR STRING; 4932.YBR205W; -.
DR CAZy; GT15; Glycosyltransferase Family 15.
DR iPTMnet; P38130; -.
DR MaxQB; P38130; -.
DR PaxDb; P38130; -.
DR PRIDE; P38130; -.
DR EnsemblFungi; YBR205W_mRNA; YBR205W; YBR205W.
DR GeneID; 852504; -.
DR KEGG; sce:YBR205W; -.
DR SGD; S000000409; KTR3.
DR VEuPathDB; FungiDB:YBR205W; -.
DR eggNOG; KOG4472; Eukaryota.
DR GeneTree; ENSGT00940000176287; -.
DR HOGENOM; CLU_024327_0_0_1; -.
DR InParanoid; P38130; -.
DR OMA; YCDIQYD; -.
DR BioCyc; MetaCyc:G3O-29145-MON; -.
DR BioCyc; YEAST:G3O-29145-MON; -.
DR PRO; PR:P38130; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38130; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP: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:0006491; P:N-glycan processing; IGI:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IGI:SGD.
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 SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..404
FT /note="Probable mannosyltransferase KTR3"
FT /id="PRO_0000208244"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 45..404
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 45..83
FT /note="Stem region"
FT /evidence="ECO:0000250"
FT REGION 84..404
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT ACT_SITE 295
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CONFLICT 100
FT /note="W -> R (in Ref. 4; AAT93230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 47482 MW; 199F184731C4F381 CRC64;
MSVHHKKKLM PKSALLIRKY QKGIRSSFIG LIIVLSFLFF MSGSRSPEVP IAQGTSVSRV
ASKDYLMPFT DKSQGVIHPV DDGKKEKGVM VTLARNSDLW NLVKSIRHVE DRFNNRYHYD
WVFLNDQPFS DEFKRVTSAL VSGKAKYGTI PKDHWSIPSW IDTEKFDEKR LAMGKLDIPY
GSSVPYRHMC RFQSGFIWRH PLLEEYEWFW RVDTDITLFC DIQYDIFKFL KVNNKKYGFI
LSVSEYERTI PTLWETTKKF IKKNPKFLHK NNLMKFISND DGDTYNMCHF WTNFEIGSLD
FFRSDAYREY FDYLDSSGGF FYERWGDAPV HSIAASLFLD KSEIHFFDGL GFHHPDFTSC
PIEQKIRLQN KCICEPSKDV TWTPDYFCTR KYFSAGNYKL PPGI
