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Protein

Mannan polymerase complex subunit mnn9

Gene

mnn9

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Required for the addition of the long alpha 1,6-mannose backbone of N-linked glycans on cell wall and periplasmic proteins.By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.By similarity
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Biological processi

  • negative regulation of G0 to G1 transition Source: PomBase
  • protein N-linked glycosylation Source: PomBase
Complete GO annotation...

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT62. Glycosyltransferase Family 62.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan polymerase complex subunit mnn9
Gene namesi
Name:mnn9By similarity
ORF Names:SPAC4F10.10c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC4F10.10c.
PomBaseiSPAC4F10.10c. mnn9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence analysisBy similarity
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini30 – 337308LumenalSequence analysisBy similarityAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Mannan polymerase complex subunit mnn9PRO_0000316855Add
BLAST

Proteomic databases

MaxQBiO36022.

Interactioni

Protein-protein interaction databases

BioGridi279680. 3 interactions.
MINTiMINT-4672963.

Family & Domainsi

Sequence similaritiesi

Belongs to the ANP1/MMN9/VAN1 family.Sequence analysis

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000167461.
InParanoidiO36022.
KOiK05529.
OMAiPYDFNNW.
OrthoDBiEOG73V6VP.
PhylomeDBiO36022.

Family and domain databases

InterProiIPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

O36022-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVYNKSRIV GQLLFVALGI TFIYYLFTPS VNSNAKVQIE NRGGNSYEIY
60 70 80 90 100
DMNKITESSD PIRNKEEVLI LTPIARFYPQ YWKNLLELDY PRNLISLGFI
110 120 130 140 150
VPSSKDGAKV HRELRNAINA VQKGPGDKRF ADVKILIQDS DLSSGQSEAE
160 170 180 190 200
RHKFSAQKER RGKLAATRNT LLLSTLKPST SWVLWLDSDI VETPSTLIQD
210 220 230 240 250
LAEHNEDVLV ANCFQKQGDK LTPYDFNSWV DSQTAQELAS HMDRDEILLE
260 270 280 290 300
GYAELPTYRM LMAKIYEEHK DPSTIMALDG VGTTALLVKA SVHRDGALFP
310 320 330
TFPFYHLIES EGFAKMAKRL GHGVYGLPYY LVFHHNE
Length:337
Mass (Da):38,297
Last modified:January 1, 1998 - v1
Checksum:i4309DAA98590478A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11713.1.
PIRiT38814.
RefSeqiNP_594753.1. NM_001020180.2.

Genome annotation databases

EnsemblFungiiSPAC4F10.10c.1; SPAC4F10.10c.1:pep; SPAC4F10.10c.
GeneIDi2543252.
KEGGispo:SPAC4F10.10c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11713.1.
PIRiT38814.
RefSeqiNP_594753.1. NM_001020180.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279680. 3 interactions.
MINTiMINT-4672963.

Protein family/group databases

CAZyiGT62. Glycosyltransferase Family 62.

Proteomic databases

MaxQBiO36022.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC4F10.10c.1; SPAC4F10.10c.1:pep; SPAC4F10.10c.
GeneIDi2543252.
KEGGispo:SPAC4F10.10c.

Organism-specific databases

EuPathDBiFungiDB:SPAC4F10.10c.
PomBaseiSPAC4F10.10c. mnn9.

Phylogenomic databases

HOGENOMiHOG000167461.
InParanoidiO36022.
KOiK05529.
OMAiPYDFNNW.
OrthoDBiEOG73V6VP.
PhylomeDBiO36022.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi20804273.
PROiO36022.

Family and domain databases

InterProiIPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMNN9_SCHPO
AccessioniPrimary (citable) accession number: O36022
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.