MNN9_YEAST
ID MNN9_YEAST Reviewed; 395 AA.
AC P39107; D6W3W4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Mannan polymerase complexes subunit MNN9;
DE Short=M-pol I subunit MNN9;
DE AltName: Full=M-Pol II subunit MNN9;
GN Name=MNN9; OrderedLocusNames=YPL050C; ORFNames=P7102.01;
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 26109 / X2180;
RX PubMed=8146181; DOI=10.1073/pnas.91.7.2723;
RA Yip C.L., Welch S.K., Klebl F., Gilbert T., Seidel P., Grant F.J.,
RA O'Hara P.J., Mackay V.L.;
RT "Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1 genes
RT required for complex glycosylation of secreted proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2723-2727(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 PROTEIN SEQUENCE OF 2-11, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9434768; DOI=10.1006/bbrc.1997.7888;
RA Hashimoto H., Yoda K.;
RT "Novel membrane protein complexes for protein glycosylation in the yeast
RT Golgi apparatus.";
RL Biochem. Biophys. Res. Commun. 241:682-686(1997).
RN [5]
RP PROTEIN SEQUENCE OF 143-153, AND SUBCELLULAR LOCATION.
RC STRAIN=RSY455;
RX PubMed=11095735; DOI=10.1073/pnas.250472397;
RA Todorow Z., Spang A., Carmack E., Yates J., Schekman R.;
RT "Active recycling of yeast Golgi mannosyltransferase complexes through the
RT endoplasmic reticulum.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13643-13648(2000).
RN [6]
RP ACTIVITY OF M-POL COMPLEXES, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9430634; DOI=10.1093/emboj/17.2.423;
RA Jungmann J., Munro S.;
RT "Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with
RT alpha-1,6-mannosyltransferase activity.";
RL EMBO J. 17:423-434(1998).
RN [7]
RP FUNCTION, COMPOSITION OF THE M-POL I COMPLEX, AND MUTAGENESIS OF ASP-236.
RX PubMed=12235155; DOI=10.1074/jbc.m208023200;
RA Stolz J., Munro S.;
RT "The components of the Saccharomyces cerevisiae mannosyltransferase complex
RT M-Pol I have distinct functions in mannan synthesis.";
RL J. Biol. Chem. 277:44801-44808(2002).
RN [8]
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 [9]
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: The M-Pol I and M-Pol II complexes possess alpha-1,6-
CC mannosyltransferase activity and are probably involved in the
CC elongation of the mannan backbone of N-linked glycans on cell wall and
CC periplasmic proteins. May also provide alpha-1,2-mannosyltransferase
CC activity to the M-Pol I complex. {ECO:0000269|PubMed:12235155}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: The M-Pol I complex contains MNN9 and VAN1. The M-Pol II
CC complex is composed of ANP1, MNN9, MNN10, MNN11 and HOC1.
CC {ECO:0000269|PubMed:9430634, ECO:0000269|PubMed:9434768}.
CC -!- INTERACTION:
CC P39107; P32629: ANP1; NbExp=6; IntAct=EBI-11082, EBI-2595;
CC P39107; P23642: VAN1; NbExp=4; IntAct=EBI-11082, EBI-20237;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11095735}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:9434768}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:9434768}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:9434768}. Note=Cis-Golgi (PubMed:9430634). Recycles
CC between endoplasmic reticulum and Golgi (PubMed:11095735).
CC {ECO:0000269|PubMed:11095735, ECO:0000269|PubMed:9430634}.
CC -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ANP1/MMN9/VAN1 family. {ECO:0000305}.
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DR EMBL; L23752; AAA53677.1; -; Genomic_DNA.
DR EMBL; U44030; AAB68171.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11380.1; -; Genomic_DNA.
DR PIR; S43746; S43746.
DR RefSeq; NP_015275.1; NM_001183864.1.
DR PDB; 3ZF8; X-ray; 1.98 A; A=93-395.
DR PDBsum; 3ZF8; -.
DR AlphaFoldDB; P39107; -.
DR SMR; P39107; -.
DR BioGRID; 36130; 40.
DR ComplexPortal; CPX-1672; alpha-1,6-mannosyltransferase complex, M-Pol I variant.
DR ComplexPortal; CPX-1839; alpha-1,6-mannosyltransferase complex, M-Pol II variant.
DR DIP; DIP-783N; -.
DR IntAct; P39107; 21.
DR MINT; P39107; -.
DR STRING; 4932.YPL050C; -.
DR CAZy; GT62; Glycosyltransferase Family 62.
DR MaxQB; P39107; -.
DR PaxDb; P39107; -.
DR PRIDE; P39107; -.
DR EnsemblFungi; YPL050C_mRNA; YPL050C; YPL050C.
DR GeneID; 856057; -.
DR KEGG; sce:YPL050C; -.
DR SGD; S000005971; MNN9.
DR VEuPathDB; FungiDB:YPL050C; -.
DR eggNOG; ENOG502QRPX; Eukaryota.
DR GeneTree; ENSGT00940000176370; -.
DR HOGENOM; CLU_017872_4_0_1; -.
DR InParanoid; P39107; -.
DR OMA; LVYHYNE; -.
DR BioCyc; MetaCyc:G3O-33963-MON; -.
DR BioCyc; YEAST:G3O-33963-MON; -.
DR BRENDA; 2.4.1.232; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:P39107; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P39107; protein.
DR GO; GO:0005801; C:cis-Golgi network; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:UniProtKB.
DR GO; GO:0000136; C:mannan polymerase complex; IDA:SGD.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR GO; GO:0097502; P:mannosylation; IDA:ComplexPortal.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:SGD.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9434768"
FT CHAIN 2..395
FT /note="Mannan polymerase complexes subunit MNN9"
FT /id="PRO_0000193670"
FT TOPO_DOM 2..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..395
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MUTAGEN 236
FT /note="D->A: Reduced activity of the M-Pol I complex."
FT /evidence="ECO:0000269|PubMed:12235155"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3ZF8"
FT TURN 108..114
FT /evidence="ECO:0007829|PDB:3ZF8"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:3ZF8"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:3ZF8"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:3ZF8"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:3ZF8"
FT HELIX 154..171
FT /evidence="ECO:0007829|PDB:3ZF8"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:3ZF8"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:3ZF8"
FT HELIX 204..224
FT /evidence="ECO:0007829|PDB:3ZF8"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:3ZF8"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3ZF8"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:3ZF8"
FT STRAND 256..268
FT /evidence="ECO:0007829|PDB:3ZF8"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:3ZF8"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:3ZF8"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:3ZF8"
FT TURN 308..312
FT /evidence="ECO:0007829|PDB:3ZF8"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:3ZF8"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:3ZF8"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:3ZF8"
FT HELIX 345..349
FT /evidence="ECO:0007829|PDB:3ZF8"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:3ZF8"
FT STRAND 379..389
FT /evidence="ECO:0007829|PDB:3ZF8"
SQ SEQUENCE 395 AA; 45955 MW; 461783BB4D700987 CRC64;
MSLSLVSYRL RKNPWVNIFL PVLAIFLIYI IFFQRDQSLL GLNGQSISQH KWAHEKENTF
YFPFTKKYKM PKYSYKKKSG WLFNDHVEDI IPEGHIAHYD LNKLHSTSEA AVNKEHILIL
TPMQTFHQQY WDNLLQLNYP RELIELGFIT PRTATGDLAL KKLENAIKKV QTDKKTQRFS
KITILRQNSQ SFDKLMEKER HALDVQKERR AAMALARNEL LFSTIGPHTS WVLWLDADII
ETPPSLIQDM TKHNKAILAA NIYQRFYDEE KKQPSIRPYD FNNWQESDTG LEIASQMGDD
EIIVEGYAEI ATYRPLMAHF YDANGVPGEE MALDGVGGGC TLVKAEVHRD GAMFPNFPFY
HLIETEGFAK MAKRLNYDVF GLPNYLVYHI EEENH
