KTR4_YEAST
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 03-AUG-2022, entry version 159.
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 PDBsum; 5A07; -.
DR PDBsum; 5A08; -.
DR AlphaFoldDB; P38131; -.
DR SMR; P38131; -.
DR BioGRID; 32896; 49.
DR DIP; DIP-7838N; -.
DR IntAct; P38131; 3.
DR MINT; P38131; -.
DR STRING; 4932.YBR199W; -.
DR CAZy; GT15; Glycosyltransferase Family 15.
DR iPTMnet; P38131; -.
DR MaxQB; P38131; -.
DR PaxDb; P38131; -.
DR PRIDE; P38131; -.
DR EnsemblFungi; YBR199W_mRNA; YBR199W; YBR199W.
DR GeneID; 852498; -.
DR KEGG; sce:YBR199W; -.
DR SGD; S000000403; KTR4.
DR VEuPathDB; FungiDB:YBR199W; -.
DR eggNOG; KOG4472; Eukaryota.
DR GeneTree; ENSGT00940000176287; -.
DR HOGENOM; CLU_024327_1_1_1; -.
DR InParanoid; P38131; -.
DR OMA; CVTGRFT; -.
DR BioCyc; YEAST:G3O-29140-MON; -.
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: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; IBA:GO_Central.
DR GO; GO:0097502; P:mannosylation; 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 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 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..110
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 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..244
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
