ID   KTR4_YEAST              Reviewed;         464 AA.
AC   P38131; D6VQJ5; P89506;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-SEP-2026, entry version 174.
DE   RecName: Full=Probable mannosyltransferase KTR4;
DE            EC=2.4.1.-;
GN   Name=KTR4; OrderedLocusNames=YBR199W; ORFNames=YBR1411;
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=7975899; DOI=10.1002/yea.320100612;
RA   Mallet L., Bussereau F., Jacquet M.;
RT   "Nucleotide sequence analysis of an 11.7 kb fragment of yeast chromosome II
RT   including BEM1, a new gene of the WD-40 repeat family and a new member of
RT   the KRE2/MNT1 family.";
RL   Yeast 10:819-831(1994).
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
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 5240 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; Z21487; CAA79686.1; -; Genomic_DNA.
DR   EMBL; Z36068; CAA85161.1; -; Genomic_DNA.
DR   EMBL; Z36069; CAA85163.1; -; Genomic_DNA.
DR   EMBL; AY692898; AAT92917.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07315.1; -; Genomic_DNA.
DR   PIR; S34024; S34024.
DR   RefSeq; NP_009758.3; NM_001178547.3.
DR   PDB; 5A07; X-ray; 1.90 A; A/B=33-464.
DR   PDB; 5A08; X-ray; 2.21 A; A/B=33-464.
DR   AlphaFoldDB; P38131; -.
DR   SMR; P38131; -.
DR   BioGRID; 32896; 56.
DR   DIP; DIP-7838N; -.
DR   FunCoup; P38131; 68.
DR   IntAct; P38131; 3.
DR   MINT; P38131; -.
DR   STRING; 4932.YBR199W; -.
DR   iPTMnet; P38131; -.
DR   PaxDb; 4932-YBR199W; -.
DR   PeptideAtlas; P38131; -.
DR   EnsemblFungi; YBR199W_mRNA; YBR199W; YBR199W.
DR   GeneID; 852498; -.
DR   KEGG; sce:YBR199W; -.
DR   AGR; SGD:S000000403; -.
DR   SGD; S000000403; KTR4.
DR   VEuPathDB; FungiDB:YBR199W; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   HOGENOM; CLU_024327_1_1_1; -.
DR   InParanoid; P38131; -.
DR   OMA; WCFFLYQ; -.
DR   OrthoDB; 439943at2759; -.
DR   BioCyc; YEAST:G3O-29140-MONOMER; -.
DR   BioGRID-ORCS; 852498; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P38131; -.
DR   PRO; PR:P38131; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38131; protein.
DR   GO; GO:0000324; C:fungal-type vacuole; 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; IDA:SGD.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; ISS:SGD.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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:SF7; MANNOSYLTRANSFERASE KTR4-RELATED; 1.
DR   Pfam; PF01793; Glyco_transf_15; 1.
DR   PIRSF; PIRSF018153; Glyco_trans_15; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PDBsum; 5A07; -.
DR   PDBsum; 5A08; -.
PE   1: Evidence at protein level;
KW   3D-structure; Glycosyltransferase; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..464
FT                   /note="Probable mannosyltransferase KTR4"
FT                   /id="PRO_0000208245"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..464
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          33..130
FT                   /note="Stem region"
FT                   /evidence="ECO:0000250"
FT   REGION          131..464
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        352
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   HELIX           71..82
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           95..111
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   TURN            128..131
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          133..140
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           146..159
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          168..174
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           178..187
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          194..198
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           212..224
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   TURN            228..231
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           233..240
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           241..245
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           246..248
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           250..252
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          256..260
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           275..281
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          286..289
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          291..293
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           302..312
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           314..316
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           323..327
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           333..338
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          345..347
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          351..355
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           356..360
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           362..374
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           376..379
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           384..395
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           398..400
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          401..403
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          409..411
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          414..416
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   STRAND          429..431
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           440..445
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           448..455
FT                   /evidence="ECO:0007829|PDB:5A07"
FT   HELIX           458..461
FT                   /evidence="ECO:0007829|PDB:5A07"
SQ   SEQUENCE   464 AA;  54556 MW;  207CE3E43A3B4991 CRC64;
     MRFLSKRILK PVLSVIILIS IAVTVVLYFL TANENYLQAV KDSAKSQYAS LRESYKSITG
     KTESADELPD HDAEVLDSIM DRLHEPLYEK DTFDPNEVLA ENKQLYEEFL LQEISEPKVD
     NLVRSGDPLA GKAKGTILSL VRNSDLEDII SSIQQLEEEY NKNFGYPYTF LNDEEFTDEF
     KDGIKSILPK DRVVEFGTIG PDNWNMPDSI DRERYDQEMD KMSKENIQYA EVESYHNMCR
     FYSKEFYHHP LLSKYKYVWR LEPNVNFYCK INYDVFQFMN KNDKIYGFVL NLYDSPQTIE
     TLWTSTMDFV EEHPNYLNVN GAFAWLKDNS QNPKNYDYTQ GYSTCHFWTN FEIVDLDFLR
     SEPYEKYMQY LEEKGGFYYE RWGDAPVRSL ALALFADKSS IHWFRDIGYH HTPYTNCPTC
     PADSDRCNGN CVPGKFTPWS DLDNQNCQAT WIRHSMSEEE LEMY
//