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   27-MAR-2024, entry version 187.
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; 67.
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; 4932-YPL050C; -.
DR   PeptideAtlas; P39107; -.
DR   EnsemblFungi; YPL050C_mRNA; YPL050C; YPL050C.
DR   GeneID; 856057; -.
DR   KEGG; sce:YPL050C; -.
DR   AGR; SGD:S000005971; -.
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; IPKTREG; -.
DR   OrthoDB; 2965755at2759; -.
DR   BioCyc; MetaCyc:G3O-33963-MONOMER; -.
DR   BioCyc; YEAST:G3O-33963-MONOMER; -.
DR   BRENDA; 2.4.1.232; 984.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 856057; 0 hits in 10 CRISPR screens.
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   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43083:SF6; MANNAN POLYMERASE COMPLEXES SUBUNIT MNN9; 1.
DR   PANTHER; PTHR43083; MANNAN POLYMERASE II; 1.
DR   Pfam; PF03452; Anp1; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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
//