MNT3_YEAST
ID MNT3_YEAST Reviewed; 630 AA.
AC P40549; D6VVR6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Alpha-1,3-mannosyltransferase MNT3;
DE EC=2.4.1.-;
GN Name=MNT3; OrderedLocusNames=YIL014W;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 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 [4]
RP CHARACTERIZATION.
RX PubMed=10521541; DOI=10.1093/glycob/9.10.1045;
RA Romero P.A., Lussier M., Veronneau S., Sdicu A.-M., Herscovics A.,
RA Bussey H.;
RT "Mnt2p and Mnt3p of Saccharomyces cerevisiae are members of the Mnn1p
RT family of alpha-1,3-mannosyltransferases responsible for adding the
RT terminal mannose residues of O-linked oligosaccharides.";
RL Glycobiology 9:1045-1051(1999).
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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Mannosyltransferase involved in adding the 4th and 5th
CC mannose residues of O-linked glycans.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 2310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR EMBL; Z46881; CAA86979.1; -; Genomic_DNA.
DR EMBL; AY558107; AAS56433.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08532.1; -; Genomic_DNA.
DR PIR; S49969; S49969.
DR RefSeq; NP_012251.3; NM_001179364.3.
DR AlphaFoldDB; P40549; -.
DR BioGRID; 34977; 65.
DR DIP; DIP-4122N; -.
DR IntAct; P40549; 1.
DR STRING; 4932.YIL014W; -.
DR CAZy; GT71; Glycosyltransferase Family 71.
DR MaxQB; P40549; -.
DR PaxDb; P40549; -.
DR PRIDE; P40549; -.
DR EnsemblFungi; YIL014W_mRNA; YIL014W; YIL014W.
DR GeneID; 854801; -.
DR KEGG; sce:YIL014W; -.
DR SGD; S000001276; MNT3.
DR VEuPathDB; FungiDB:YIL014W; -.
DR eggNOG; ENOG502RZ48; Eukaryota.
DR GeneTree; ENSGT00940000176340; -.
DR HOGENOM; CLU_015387_1_0_1; -.
DR InParanoid; P40549; -.
DR OMA; FFWLGQL; -.
DR BioCyc; MetaCyc:G3O-31290-MON; -.
DR BioCyc; YEAST:G3O-31290-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P40549; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40549; protein.
DR GO; GO:0000324; C:fungal-type vacuole; 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:0000033; F:alpha-1,3-mannosyltransferase activity; IMP:SGD.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:SGD.
DR InterPro; IPR022751; Alpha_mannosyltransferase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF11051; Mannosyl_trans3; 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..630
FT /note="Alpha-1,3-mannosyltransferase MNT3"
FT /id="PRO_0000080560"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..630
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 630 AA; 72410 MW; 6B087DD003D8CD91 CRC64;
MLKSLKSRRL ILKRLVTLLL SLFFSYLIFS ASRNVTSSNK LNNHASERTA VESSAFNWIE
KRQHQVRSEN LMNRLSAYFL PFLSRSSHKE RVLLRQLGNN EIAKSDKCRY IFEVLYKIDP
DWDNAQTAKF YNVDGVDNTL ASLLGERLRS YDYCFLSGQL DPTAIFANST VNPHDLQNRM
FPFLKKINEE SKTVMWPIIT DMTTGEAVPA PEVDMESSNF NGNFWSNWNR LSKGRGFVLT
IAEKDVPLFL KQLKVMEFSK NELPFQIVST GNELSAESIA KISETAKETE QRVYLVDCST
VLDTNFANTY ISFFQNKWVA TLFNTFEEYI LLDADVVPFV GSDYFFDSPS YRESGILLFK
DRVMENEQTF QYCIEMLNEV EPSAQERRFI GSRLVFDSSL PFSSETSEEA SVYYNFFKKL
RLHHVDSGLV VVNKLEKLNG LLMSFMLNLD GKLQRCVYGD KEIFWLGQLY AGQDYSINPV
DGSIIGPVNE EPENDDGHKS GMYYICSTQI AHSDSKNRLL WVNGGLKTCK ISNSAEDDFG
REPEYFKSRY GDISKLKRIY DASLNVEGLI VPDVSVHPWM QIKECSNYMY CAYATGDGHT
NSELDEGRLI TFTEKELRYI NDISRTWNAN
