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Protein

Initiation-specific alpha-1,6-mannosyltransferase

Gene

och1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mannosyltransferase involved in outer chain elongation of asparagine-linked oligosaccharides of the type Man9GlcNAc2. May otherwise add the first alpha-1,6-mannose to the Man8GlNAc2 core oligosaccharide from the ER. Represents the first enzymatic event required for synthesis of outer chain mannose linkages on yeast secretory proteins.2 Publications

Catalytic activityi

Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-mannose linkage.1 Publication

Cofactori

Mn2+By similarity

GO - Molecular functioni

GO - Biological processi

  • cell wall mannoprotein biosynthetic process Source: PomBase
  • glycoprotein biosynthetic process Source: UniProtKB
  • N-glycan processing Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.232. 5613.

Protein family/group databases

CAZyiGT32. Glycosyltransferase Family 32.

Names & Taxonomyi

Protein namesi
Recommended name:
Initiation-specific alpha-1,6-mannosyltransferase (EC:2.4.1.2321 Publication)
Gene namesi
Name:och11 Publication
ORF Names:SPAC1006.05cImported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1006.05c.
PomBaseiSPAC1006.05c. och1.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Single-pass type II membrane protein By similarity
  • Golgi apparatus membrane By similarity; Single-pass type II membrane protein By similarity

  • Note: Is recycled between the trans-Golgi network and a late compartment of the endoplasmic reticulum.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicBy similarity
Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini29 – 396368LumenalBy similarityAdd
BLAST

GO - Cellular componenti

  • alpha-1,6-mannosyltransferase complex Source: PomBase
  • cytosol Source: PomBase
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Initiation-specific alpha-1,6-mannosyltransferasePRO_0000080562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9UTR6.

Interactioni

Protein-protein interaction databases

BioGridi279579. 4 interactions.
MINTiMINT-4711157.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi229 – 2313DXD motifBy similarity

Domaini

The conserved DXD motif is involved in enzyme activity.By similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 32 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000174059.
InParanoidiQ9UTR6.
KOiK05528.
OrthoDBiEOG7BP8BZ.
PhylomeDBiQ9UTR6.

Family and domain databases

InterProiIPR007577. GlycoTrfase_DXD_sugar-bd_CS.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF04488. Gly_transf_sug. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9UTR6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLRLRSIV IGAAIAGSIL LLFNHGSIEG MEDLTEISML EDYTPEAANK
60 70 80 90 100
DYVGQQEEEE LLYDQPSYIE EEEDPDLEAY LSDLEREELE HSLEELDEEN
110 120 130 140 150
NYKLHLRYSF SQLQDFDEEN EAVHMIVPKD TYEFEVPYHA DIPKLIWQTS
160 170 180 190 200
KDPFDREVMK YTRFWRINHP SYSHAVLDDE QSKALVISSF GDSSVSKISQ
210 220 230 240 250
AYAMMPLPVL KADFFRYLVL LAKGGIYSDI DTAPLKHINN WIPREYRKRN
260 270 280 290 300
IRLIVGIEAD PDRPDWNDYY ARRVQFCQWT IAAAPGHPIL WELVRRITDE
310 320 330 340 350
TWKLHDSKKL SKNGESVMEW TGPGIWTDAI MDYLNWQYGP FSVENITNLE
360 370 380 390
EPYLVGDVLI LPITAFSPGV GHMGSKSPND PMAYVQHFFA GSWKDD
Length:396
Mass (Da):45,930
Last modified:March 1, 2002 - v2
Checksum:i824B8932495642F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAD24818.1.
PIRiT50453.
RefSeqiNP_594852.1. NM_001020281.2.

Genome annotation databases

EnsemblFungiiSPAC1006.05c.1; SPAC1006.05c.1:pep; SPAC1006.05c.
GeneIDi2543147.
KEGGispo:SPAC1006.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAD24818.1.
PIRiT50453.
RefSeqiNP_594852.1. NM_001020281.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279579. 4 interactions.
MINTiMINT-4711157.

Protein family/group databases

CAZyiGT32. Glycosyltransferase Family 32.

Proteomic databases

MaxQBiQ9UTR6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1006.05c.1; SPAC1006.05c.1:pep; SPAC1006.05c.
GeneIDi2543147.
KEGGispo:SPAC1006.05c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1006.05c.
PomBaseiSPAC1006.05c. och1.

Phylogenomic databases

HOGENOMiHOG000174059.
InParanoidiQ9UTR6.
KOiK05528.
OrthoDBiEOG7BP8BZ.
PhylomeDBiQ9UTR6.

Enzyme and pathway databases

BRENDAi2.4.1.232. 5613.

Miscellaneous databases

PROiQ9UTR6.

Family and domain databases

InterProiIPR007577. GlycoTrfase_DXD_sugar-bd_CS.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF04488. Gly_transf_sug. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Schizosaccharomyces pombe och1(+) encodes alpha-1,6-mannosyltransferase that is involved in outer chain elongation of N-linked oligosaccharides."
    Yoko-o T., Tsukahara K., Watanabe T., Hata-Sugi N., Yoshimatsu K., Nagasu T., Jigami Y.
    FEBS Lett. 489:75-80(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION.
    Strain: 972 / ATCC 24843.
  2. "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.
  3. "Salt stress induces the expression of Schizosaccharomyces pombe och1+, which encodes an initiation-specific alpha-1,6-mannosyltransferase for N-linked outer chain synthesis of cell wall mannoproteins."
    Yamamoto K., Okamoto M., Yoko-o T., Jigami Y.
    Biosci. Biotechnol. Biochem. 67:927-929(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiOCH1_SCHPO
AccessioniPrimary (citable) accession number: Q9UTR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 103 of the entry and version 2 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.