MNT2_YEAST
ID MNT2_YEAST Reviewed; 558 AA.
AC P53059; D6VV78;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Alpha-1,3-mannosyltransferase MNT2;
DE EC=2.4.1.-;
GN Name=MNT2; OrderedLocusNames=YGL257C; ORFNames=NRD558;
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 96604 / S288c / FY1679;
RX PubMed=8972578;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1555::aid-yea43>3.0.co;2-q;
RA Coissac E., Maillier E., Robineau S., Netter P.;
RT "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome
RT VII of Saccharomyces cerevisiae.";
RL Yeast 12:1555-1562(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 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).
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 1170 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; X94357; CAA64130.1; -; Genomic_DNA.
DR EMBL; Z72779; CAA96977.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07862.1; -; Genomic_DNA.
DR PIR; S61604; S61604.
DR RefSeq; NP_011257.1; NM_001181123.1.
DR AlphaFoldDB; P53059; -.
DR SMR; P53059; -.
DR BioGRID; 33022; 87.
DR STRING; 4932.YGL257C; -.
DR CAZy; GT71; Glycosyltransferase Family 71.
DR MaxQB; P53059; -.
DR PaxDb; P53059; -.
DR PRIDE; P53059; -.
DR EnsemblFungi; YGL257C_mRNA; YGL257C; YGL257C.
DR GeneID; 852635; -.
DR KEGG; sce:YGL257C; -.
DR SGD; S000003226; MNT2.
DR VEuPathDB; FungiDB:YGL257C; -.
DR eggNOG; ENOG502RZ48; Eukaryota.
DR GeneTree; ENSGT00940000176340; -.
DR HOGENOM; CLU_015387_0_1_1; -.
DR InParanoid; P53059; -.
DR OMA; HTLLWFN; -.
DR BioCyc; MetaCyc:G3O-30725-MON; -.
DR BioCyc; YEAST:G3O-30725-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P53059; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53059; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; 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..558
FT /note="Alpha-1,3-mannosyltransferase MNT2"
FT /id="PRO_0000080559"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..558
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 558 AA; 64853 MW; 3E58ED62B4E291B6 CRC64;
MRRKNRLFIL VVLLGIVLVV YYSQLNSLDL VEPVQSSSSG NGGCWSYYEG LTPGWLNDFY
DVNQITPNPA KDVIELVTRI KIFFNCLQQV DGHNIQRLRD IEKKLFPYIN FEKLETDESA
FWHTTTRWNG EVYHASMLEF DPKNHQFLRS KPINFDTGLS FWENWLHTVT QSGSKGIVIS
ASDVQLNETI RLLKVLRFIK NDYPIQIVHN ADLSQDSMKS IIKYARSLDT AEYPAQELWF
LNVHSLLNPK YSKKFTTYSN KWLALTFSSF EIPILMDSDT VPFVSIEKFY ELEEFQKTGV
LFFKDRVISD DLFESSELKI LREIVYGCIG LDLEDESKIH EQVEDPVVAQ VLENMFIKKY
KHHLESGLVI LHKGKHLFSM LTSIALQFSP IAEYFHGDKD FFWLGELLSN NRFTFHPVDA
SNIGQLGNVV SKESTGEFYQ ICSVQLSHTD RDGSLLWLNG GLNICKKTSW EYDYEHRQRL
NDMFQNADEL REYYASPVKL EGIIIPDTSI SGWINSGECF LFNYCTLFKE GEFGKLIKFK
EDEKLRLSQI VDIWNKDI
