MNN2_YEAST
ID MNN2_YEAST Reviewed; 597 AA.
AC P38069; D6VQ17;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Alpha-1,2-mannosyltransferase MNN2;
DE EC=2.4.1.-;
DE AltName: Full=Calcium resistance and vanadate sensitivity protein 4;
DE AltName: Full=Mannan synthesis protein MNN2;
GN Name=MNN2; Synonyms=CRV4, LDB8, TTP1; OrderedLocusNames=YBR015C;
GN ORFNames=YBR0220;
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].
RX PubMed=7992511; DOI=10.1002/yea.320100813;
RA Romero P.A., Athanassiadis A., Lussier M., Herscovics A.;
RT "The nucleotide sequence of TTP1, a gene encoding a predicted type II
RT membrane protein.";
RL Yeast 10:1111-1115(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 FUNCTION.
RX PubMed=4578088; DOI=10.1016/s0021-9258(19)43714-9;
RA Raschke W.C., Kern K.A., Antalis C., Ballou C.E.;
RT "Genetic control of yeast mannan structure. Isolation and characterization
RT of mannan mutants.";
RL J. Biol. Chem. 248:4660-4666(1973).
RN [5]
RP FUNCTION.
RX PubMed=4124122; DOI=10.1016/s0021-9258(19)43715-0;
RA Ballou C.E., Kern K.A., Raschke W.C.;
RT "Genetic control of yeast mannan structure. Complementation studies and
RT properties of mannan mutants.";
RL J. Biol. Chem. 248:4667-4671(1973).
RN [6]
RP FUNCTION.
RX PubMed=4578089; DOI=10.1016/s0021-9258(19)43716-2;
RA Hawkins E.R.;
RT "A comparison of yeast mannan mutants by electron microscopy.";
RL J. Biol. Chem. 248:4671-4673(1973).
RN [7]
RP FUNCTION.
RX PubMed=4612040; DOI=10.1016/s0021-9258(19)81290-5;
RA Nakajima T., Ballou C.E.;
RT "Characterization of the carbohydrate fragments obtained from Saccharomyces
RT cerevisiae mannan by alkaline degradation.";
RL J. Biol. Chem. 249:7679-7684(1974).
RN [8]
RP FUNCTION.
RX PubMed=4612041; DOI=10.1016/s0021-9258(19)81291-7;
RA Nakajima T., Ballou C.E.;
RT "Structure of the linkage region between the polysaccharide and protein
RT parts of Saccharomyces cerevisiae mannan.";
RL J. Biol. Chem. 249:7685-7694(1974).
RN [9]
RP FUNCTION.
RX PubMed=1097420; DOI=10.1128/jb.123.2.616-619.1975;
RA Ballou D.L.;
RT "Genetic control of yeast mannan structure: mapping genes mnn2 and mnn4 in
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 123:616-619(1975).
RN [10]
RP FUNCTION.
RX PubMed=355255; DOI=10.1016/s0021-9258(19)46958-5;
RA Karson E.M., Ballou C.E.;
RT "Biosynthesis of yeast mannan. Properties of a mannosylphosphate
RT transferase in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 253:6484-6492(1978).
RN [11]
RP FUNCTION.
RX PubMed=381304; DOI=10.1016/s0021-9258(19)86896-5;
RA Parodi A.J.;
RT "Biosynthesis of yeast mannoproteins. Synthesis of mannan outer chain and
RT of dolichol derivatives.";
RL J. Biol. Chem. 254:8343-8352(1979).
RN [12]
RP FUNCTION.
RX PubMed=6802821; DOI=10.1016/s0021-9258(19)83839-5;
RA Cohen R.E., Zhang W., Ballou C.E.;
RT "Effects of mannoprotein mutations on Saccharomyces cerevisiae core
RT oligosaccharide structure.";
RL J. Biol. Chem. 257:5730-5737(1982).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2082155; DOI=10.1111/j.1365-2958.1990.tb02049.x;
RA Devlin C., Ballou C.E.;
RT "Identification and characterization of a gene and protein required for
RT glycosylation in the yeast Golgi.";
RL Mol. Microbiol. 4:1993-2001(1990).
RN [14]
RP DISRUPTION PHENOTYPE.
RX PubMed=9413431; DOI=10.1007/s004380050592;
RA Nakamura T., Ohmoto T., Hirata D., Tsuchiya E., Miyakawa T.;
RT "Yeast Crv4/Ttp1, a predicted type II membrane protein, is involved in an
RT event important for growth, functionally overlapping with the event
RT regulated by calcineurin- and Mpk1-mediated pathways.";
RL Mol. Gen. Genet. 256:481-487(1997).
RN [15]
RP FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=9756928; DOI=10.1074/jbc.273.41.26836;
RA Rayner J.C., Munro S.;
RT "Identification of the MNN2 and MNN5 mannosyltransferases required for
RT forming and extending the mannose branches of the outer chain mannans of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:26836-26843(1998).
RN [16]
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=18410729; DOI=10.1016/j.devcel.2008.02.016;
RA Schmitz K.R., Liu J., Li S., Setty T.G., Wood C.S., Burd C.G.,
RA Ferguson K.M.;
RT "Golgi localization of glycosyltransferases requires a Vps74p oligomer.";
RL Dev. Cell 14:523-534(2008).
RN [19]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SVP26.
RX PubMed=20236934; DOI=10.1074/jbc.m109.086272;
RA Noda Y., Yoda K.;
RT "Svp26 facilitates endoplasmic reticulum to Golgi transport of a set of
RT mannosyltransferases in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 285:15420-15429(2010).
CC -!- FUNCTION: Alpha-1,2-mannosyltransferase, responsible for addition of
CC the first alpha-1,2-linked mannose to form the branches on the mannan
CC backbone of oligosaccharides. {ECO:0000269|PubMed:1097420,
CC ECO:0000269|PubMed:2082155, ECO:0000269|PubMed:355255,
CC ECO:0000269|PubMed:381304, ECO:0000269|PubMed:4124122,
CC ECO:0000269|PubMed:4578088, ECO:0000269|PubMed:4578089,
CC ECO:0000269|PubMed:4612040, ECO:0000269|PubMed:4612041,
CC ECO:0000269|PubMed:6802821, ECO:0000269|PubMed:9756928}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with SVP26. {ECO:0000269|PubMed:20236934}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:18410729,
CC ECO:0000269|PubMed:20236934, ECO:0000269|PubMed:2082155,
CC ECO:0000269|PubMed:9756928}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:16107716, ECO:0000269|PubMed:18410729,
CC ECO:0000269|PubMed:20236934, ECO:0000269|PubMed:2082155,
CC ECO:0000269|PubMed:9756928}. Note=Golgi localization depends on SVP26.
CC -!- DISRUPTION PHENOTYPE: Leads to calcium resistance and vanadate
CC sensitivity. {ECO:0000269|PubMed:9413431}.
CC -!- MISCELLANEOUS: Present with 6730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family. {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; U05211; AAA21860.1; -; Genomic_DNA.
DR EMBL; Z35884; CAA84957.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07137.1; -; Genomic_DNA.
DR PIR; S45870; S45870.
DR RefSeq; NP_009571.1; NM_001178363.1.
DR AlphaFoldDB; P38069; -.
DR SMR; P38069; -.
DR BioGRID; 32718; 239.
DR DIP; DIP-7625N; -.
DR STRING; 4932.YBR015C; -.
DR CAZy; GT71; Glycosyltransferase Family 71.
DR MaxQB; P38069; -.
DR PaxDb; P38069; -.
DR PRIDE; P38069; -.
DR EnsemblFungi; YBR015C_mRNA; YBR015C; YBR015C.
DR GeneID; 852303; -.
DR KEGG; sce:YBR015C; -.
DR SGD; S000000219; MNN2.
DR VEuPathDB; FungiDB:YBR015C; -.
DR eggNOG; ENOG502QQ16; Eukaryota.
DR GeneTree; ENSGT00940000176544; -.
DR HOGENOM; CLU_013298_1_1_1; -.
DR InParanoid; P38069; -.
DR OMA; KGYQYKA; -.
DR BioCyc; MetaCyc:YBR015C-MON; -.
DR BioCyc; YEAST:YBR015C-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P38069; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38069; protein.
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:0000026; F:alpha-1,2-mannosyltransferase activity; IMP:SGD.
DR GO; GO:0046354; P:mannan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
DR GO; GO:0035268; P:protein mannosylation; IBA:GO_Central.
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; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..597
FT /note="Alpha-1,2-mannosyltransferase MNN2"
FT /id="PRO_0000065676"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..597
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 287
FT /note="T -> K (in Ref. 1; AAA21860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 597 AA; 67774 MW; 6C4FA1F4692A261C CRC64;
MLLTKRFSKL FKLTFIVLIL CGLFVITNKY MDENTSVKEY KEYLDRYVQS YSNKYSSSSD
AASADDSTPL RDNDEAGNEK LKSFYNNVFN FLMVDSPKGS TAKQYNEACL LKGDIGDRPD
HYKDLYKLSA KELSKCLELS PDEVASLTKS HKDYVEHIAT LVSPKGTYKG SGIATVGGGK
FSLMAFLIIK TLRNMGTTLP VEVLIPPGDE GETEFCNKIL PKYNSKCIYV SDILPRETIE
KFVFKGYQFK SLALIASSFE NLLLLDADNF PIKPLDNIFN EEPYVSTGLV MWPDFWRRTT
HPLYYDIAGI AVDKKKRVRN SRDDITPPAV YTKDLKDLSD VPLSDLDGTI PDVSTESGQL
MINKTKHLAT ALLSLFYNVN GPTWYYPIFS QKAAGEGDKE TFIAAANFYG LSFYQVRTRT
GVEGYHDEDG FHGVAMLQHD FVQDYGRYLN AMESIGNKYG GTKSADAIKF DKNYSLEKYT
EEFFDNEDLN AKNHVDVMFI HSNFPKFDPY DLSKSNFLTT NGKPARSYTA LKKVKNYDIE
LENFKVLNEY VCVNKNPFKY LDDLLGQDKT EWKRVCGYIT DRLAFLESTH DKAIAGK
