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Protein

Mannan polymerase complexes subunit MNN9

Gene

MNN9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The M-Pol I and M-Pol II complexes possess alpha-1,6-mannosyltransferase activity and are probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins. May also provide alpha-1,2-mannosyltransferase activity to the M-Pol I complex.1 Publication

Pathwayi

GO - Biological processi

  • cell wall mannoprotein biosynthetic process Source: UniProtKB
  • mannosylation Source: GOC
  • protein N-linked glycosylation Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-33963-MONOMER.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT62. Glycosyltransferase Family 62.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan polymerase complexes subunit MNN9
Short name:
M-pol I subunit MNN9
Alternative name(s):
M-Pol II subunit MNN9
Gene namesi
Name:MNN9
Ordered Locus Names:YPL050C
ORF Names:P7102.01
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL050C.
SGDiS000005971. MNN9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1716CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei18 – 3316Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini34 – 395362LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • alpha-1,6-mannosyltransferase complex Source: SGD
  • cis-Golgi network Source: SGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi cis cisterna Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi236 – 2361D → A: Reduced activity of the M-Pol I complex. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 395394Mannan polymerase complexes subunit MNN9PRO_0000193670Add
BLAST

Proteomic databases

MaxQBiP39107.
PaxDbiP39107.

Expressioni

Gene expression databases

GenevestigatoriP39107.

Interactioni

Subunit structurei

The M-Pol I complex contains MNN9 and VAN1. The M-Pol II complex is composed of ANP1, MNN9, MNN10, MNN11 and HOC1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANP1P326296EBI-11082,EBI-2595
VAN1P236423EBI-11082,EBI-20237

Protein-protein interaction databases

BioGridi36130. 31 interactions.
DIPiDIP-783N.
IntActiP39107. 21 interactions.
MINTiMINT-552187.
STRINGi4932.YPL050C.

Structurei

Secondary structure

1
395
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi101 – 1033Combined sources
Turni108 – 1147Combined sources
Beta strandi116 – 1227Combined sources
Helixi128 – 1358Combined sources
Helixi141 – 1433Combined sources
Beta strandi144 – 1507Combined sources
Helixi154 – 17118Combined sources
Helixi175 – 1773Combined sources
Beta strandi180 – 1867Combined sources
Helixi204 – 22421Combined sources
Beta strandi229 – 2357Combined sources
Beta strandi239 – 2413Combined sources
Helixi246 – 2516Combined sources
Beta strandi256 – 26813Combined sources
Turni269 – 2724Combined sources
Beta strandi273 – 2786Combined sources
Helixi288 – 2958Combined sources
Turni308 – 3125Combined sources
Helixi317 – 3204Combined sources
Beta strandi331 – 3355Combined sources
Beta strandi338 – 3447Combined sources
Helixi345 – 3495Combined sources
Helixi364 – 37411Combined sources
Beta strandi379 – 38911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZF8X-ray1.98A93-395[»]
ProteinModelPortaliP39107.
SMRiP39107. Positions 95-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ANP1/MMN9/VAN1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG73762.
GeneTreeiENSGT00390000005201.
HOGENOMiHOG000167461.
InParanoidiP39107.
KOiK05529.
OMAiPYDFNNW.
OrthoDBiEOG73V6VP.

Family and domain databases

InterProiIPR005109. Anp1.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF03452. Anp1. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSLVSYRL RKNPWVNIFL PVLAIFLIYI IFFQRDQSLL GLNGQSISQH
60 70 80 90 100
KWAHEKENTF YFPFTKKYKM PKYSYKKKSG WLFNDHVEDI IPEGHIAHYD
110 120 130 140 150
LNKLHSTSEA AVNKEHILIL TPMQTFHQQY WDNLLQLNYP RELIELGFIT
160 170 180 190 200
PRTATGDLAL KKLENAIKKV QTDKKTQRFS KITILRQNSQ SFDKLMEKER
210 220 230 240 250
HALDVQKERR AAMALARNEL LFSTIGPHTS WVLWLDADII ETPPSLIQDM
260 270 280 290 300
TKHNKAILAA NIYQRFYDEE KKQPSIRPYD FNNWQESDTG LEIASQMGDD
310 320 330 340 350
EIIVEGYAEI ATYRPLMAHF YDANGVPGEE MALDGVGGGC TLVKAEVHRD
360 370 380 390
GAMFPNFPFY HLIETEGFAK MAKRLNYDVF GLPNYLVYHI EEENH
Length:395
Mass (Da):45,955
Last modified:January 23, 2007 - v3
Checksum:i461783BB4D700987
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23752 Genomic DNA. Translation: AAA53677.1.
U44030 Genomic DNA. Translation: AAB68171.1.
BK006949 Genomic DNA. Translation: DAA11380.1.
PIRiS43746.
RefSeqiNP_015275.1. NM_001183864.1.

Genome annotation databases

EnsemblFungiiYPL050C; YPL050C; YPL050C.
GeneIDi856057.
KEGGisce:YPL050C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23752 Genomic DNA. Translation: AAA53677.1.
U44030 Genomic DNA. Translation: AAB68171.1.
BK006949 Genomic DNA. Translation: DAA11380.1.
PIRiS43746.
RefSeqiNP_015275.1. NM_001183864.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZF8X-ray1.98A93-395[»]
ProteinModelPortaliP39107.
SMRiP39107. Positions 95-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36130. 31 interactions.
DIPiDIP-783N.
IntActiP39107. 21 interactions.
MINTiMINT-552187.
STRINGi4932.YPL050C.

Protein family/group databases

CAZyiGT62. Glycosyltransferase Family 62.

Proteomic databases

MaxQBiP39107.
PaxDbiP39107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL050C; YPL050C; YPL050C.
GeneIDi856057.
KEGGisce:YPL050C.

Organism-specific databases

EuPathDBiFungiDB:YPL050C.
SGDiS000005971. MNN9.

Phylogenomic databases

eggNOGiNOG73762.
GeneTreeiENSGT00390000005201.
HOGENOMiHOG000167461.
InParanoidiP39107.
KOiK05529.
OMAiPYDFNNW.
OrthoDBiEOG73V6VP.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciYEAST:G3O-33963-MONOMER.

Miscellaneous databases

NextBioi981026.
PROiP39107.

Gene expression databases

GenevestigatoriP39107.

Family and domain databases

InterProiIPR005109. Anp1.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF03452. Anp1. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1 genes required for complex glycosylation of secreted proteins."
    Yip C.L., Welch S.K., Klebl F., Gilbert T., Seidel P., Grant F.J., O'Hara P.J., Mackay V.L.
    Proc. Natl. Acad. Sci. U.S.A. 91:2723-2727(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26109 / X2180.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Novel membrane protein complexes for protein glycosylation in the yeast Golgi apparatus."
    Hashimoto H., Yoda K.
    Biochem. Biophys. Res. Commun. 241:682-686(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11, SUBCELLULAR LOCATION, SUBUNIT.
  5. "Active recycling of yeast Golgi mannosyltransferase complexes through the endoplasmic reticulum."
    Todorow Z., Spang A., Carmack E., Yates J., Schekman R.
    Proc. Natl. Acad. Sci. U.S.A. 97:13643-13648(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 143-153, SUBCELLULAR LOCATION.
    Strain: RSY455.
  6. "Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with alpha-1,6-mannosyltransferase activity."
    Jungmann J., Munro S.
    EMBO J. 17:423-434(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVITY OF M-POL COMPLEXES, SUBUNIT, SUBCELLULAR LOCATION.
  7. "The components of the Saccharomyces cerevisiae mannosyltransferase complex M-Pol I have distinct functions in mannan synthesis."
    Stolz J., Munro S.
    J. Biol. Chem. 277:44801-44808(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COMPOSITION OF THE M-POL I COMPLEX, MUTAGENESIS OF ASP-236.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMNN9_YEAST
AccessioniPrimary (citable) accession number: P39107
Secondary accession number(s): D6W3W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1630 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.