MNN10_YEAST
ID MNN10_YEAST Reviewed; 393 AA.
AC P50108; D6VSM5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Probable alpha-1,6-mannosyltransferase MNN10;
DE EC=2.4.1.-;
DE AltName: Full=Bud emergence delay protein 1;
DE AltName: Full=Mannan polymerase II complex MNN10 subunit;
DE Short=M-Pol II subunit MNN10;
GN Name=MNN10; Synonyms=BED1; OrderedLocusNames=YDR245W; ORFNames=YD8419.12;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8991513; DOI=10.1093/glycob/6.1.73;
RA Dean N., Poster J.B.;
RT "Molecular and phenotypic analysis of the S. cerevisiae MNN10 gene
RT identifies a family of related glycosyltransferases.";
RL Glycobiology 6:73-81(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=BF264-15DU;
RX PubMed=8567719; DOI=10.1083/jcb.132.1.137;
RA Mondesert G., Reed S.I.;
RT "BED1, a gene encoding a galactosyltransferase homologue, is required for
RT polarized growth and efficient bud emergence in Saccharomyces cerevisiae.";
RL J. Cell Biol. 132:137-151(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10037752; DOI=10.1074/jbc.274.10.6579;
RA Jungmann J., Rayner J.C., Munro S.;
RT "The Saccharomyces cerevisiae protein Mnn10p/Bed1p is a subunit of a Golgi
RT mannosyltransferase complex.";
RL J. Biol. Chem. 274:6579-6585(1999).
RN [7]
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: Required for polarized growth and efficient budding.
CC -!- FUNCTION: The M-Pol II complex possesses alpha-1,6-mannosyltransferase
CC activity and is probably involved in the elongation of the mannan
CC backbone of N-linked glycans on cell wall and periplasmic proteins.
CC -!- SUBUNIT: Component of the M-Pol II complex composed of ANP1, MNN9,
CC MNN10, MNN11 and HOC1. {ECO:0000269|PubMed:10037752}.
CC -!- INTERACTION:
CC P50108; P32629: ANP1; NbExp=3; IntAct=EBI-11043, EBI-2595;
CC P50108; P47124: HOC1; NbExp=3; IntAct=EBI-11043, EBI-8430;
CC P50108; P46985: MNN11; NbExp=5; IntAct=EBI-11043, EBI-11052;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein. Golgi apparatus, cis-Golgi network membrane;
CC Single-pass type II membrane protein.
CC -!- MISCELLANEOUS: Present with 6280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 34 family.
CC {ECO:0000305}.
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DR EMBL; L42540; AAB48372.1; -; Genomic_DNA.
DR EMBL; U31446; AAC49280.1; -; Genomic_DNA.
DR EMBL; Z49701; CAA89731.1; -; Genomic_DNA.
DR EMBL; AY557792; AAS56118.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12085.1; -; Genomic_DNA.
DR PIR; S54541; S54541.
DR RefSeq; NP_010531.1; NM_001180553.1.
DR AlphaFoldDB; P50108; -.
DR SMR; P50108; -.
DR BioGRID; 32296; 776.
DR ComplexPortal; CPX-1839; alpha-1,6-mannosyltransferase complex, M-Pol II variant.
DR DIP; DIP-892N; -.
DR IntAct; P50108; 21.
DR MINT; P50108; -.
DR STRING; 4932.YDR245W; -.
DR CAZy; GT34; Glycosyltransferase Family 34.
DR iPTMnet; P50108; -.
DR SwissPalm; P50108; -.
DR MaxQB; P50108; -.
DR PaxDb; P50108; -.
DR PRIDE; P50108; -.
DR EnsemblFungi; YDR245W_mRNA; YDR245W; YDR245W.
DR GeneID; 851832; -.
DR KEGG; sce:YDR245W; -.
DR SGD; S000002653; MNN10.
DR VEuPathDB; FungiDB:YDR245W; -.
DR eggNOG; KOG4748; Eukaryota.
DR HOGENOM; CLU_021434_2_1_1; -.
DR InParanoid; P50108; -.
DR OMA; GWQKVDI; -.
DR BioCyc; MetaCyc:G3O-29818-MON; -.
DR BioCyc; YEAST:G3O-29818-MON; -.
DR PRO; PR:P50108; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P50108; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0000136; C:mannan polymerase complex; IDA:UniProtKB.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0007114; P:cell budding; IMP:UniProtKB.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IDA:UniProtKB.
DR GO; GO:0000917; P:division septum assembly; IMP:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:SGD.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR008630; Glyco_trans_34.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR31306; PTHR31306; 1.
DR Pfam; PF05637; Glyco_transf_34; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..393
FT /note="Probable alpha-1,6-mannosyltransferase MNN10"
FT /id="PRO_0000215164"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..393
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 77..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 238
FT /note="N -> I (in Ref. 2; AAC49280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 46748 MW; FAF7DBE3122ECC8E CRC64;
MSSVPYNSQL PISNHLEYDE DEKKSRGSKL GLKYKMIYWR KTLCSSLARW RKLILLISLA
LFLFIWISDS TISRNPSTTS FQGQNSNDNK LSNTGSSINS KRYVPPYSKR SRWSFWNQDP
RIVIILAANE GGGVLRWKNE QEWAIEGISI ENKKAYAKRH GYALTIKDLT TSKRYSHEYR
EGWQKVDILR QTFREFPNAE WFWWLDLDTM IMEPSKSLEE HIFDRLETLA DRELKSFNPL
NLRDDIPYVD YSEEMEFLIT QDCGGFNLGS FLIKNSEWSK LLLDMWWDPV LYEQKHMVWE
HREQDALEAL YENEPWIRSR IGFLPLRTIN AFPPGACSEY SGDSRYFYSE KDHDFVVNMA
GCNFGRDCWG EMQYYTTLME KLNRKWYTRF FFP
