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Protein

Initiation-specific alpha-1,6-mannosyltransferase

Gene

OCH1

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

Mannosyltransferase involved in outer chain elongation of asparagine-linked oligosaccharides of the type Man9GlcNAc2. Adds the first alpha-1,6-mannose to the Man8GlNAc2 and Man9GlcNAc2, but not Man5GlcNAc2, endoplasmic reticulum intermediates. Represents the first enzymatic event required for synthesis of outer chain mannose linkages on yeast secretory proteins. Has also the potential to transfer a second alpha-1,6-mannose to the Man8GlNAc2 core oligosaccharide.6 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.2 Publications

Cofactori

Mn2+1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

GO - Molecular functioni

  • alpha-1,6-mannosyltransferase activity Source: SGD
  • glycolipid 6-alpha-mannosyltransferase activity Source: UniProtKB-EC
  • transferase activity, transferring glycosyl groups Source: SGD

GO - Biological processi

  • mannosylation Source: GOC
  • protein N-linked glycosylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:G3O-30552-MONOMER.

Protein family/group databases

CAZyiGT32. Glycosyltransferase Family 32.

Names & Taxonomyi

Protein namesi
Recommended name:
Initiation-specific alpha-1,6-mannosyltransferaseCurated (EC:2.4.1.2322 Publications)
Alternative name(s):
Outer chain elongation protein 11 Publication
Gene namesi
Name:OCH11 Publication
Synonyms:NGD291 Publication
Ordered Locus Names:YGL038CImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL038C.
SGDiS000003006. OCH1.

Subcellular locationi

  • Endoplasmic reticulum membrane 2 Publications; Single-pass type II membrane protein 1 Publication1 Publication
  • Golgi apparatus membrane 3 Publications; Single-pass type II membrane protein 1 Publication

  • Note: Is recycled between the trans-Golgi network and a late compartment of the endoplasmic reticulum.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515Cytoplasmic1 PublicationAdd
BLAST
Transmembranei16 – 3015Helical; Signal-anchor for type II membrane protein1 PublicationSequence analysisAdd
BLAST
Topological domaini31 – 480450Lumenal1 Publication1 PublicationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Stops growing at the early stage of bud formation and rapidly loses viability at the non-permissive temperature. Exhibits a defect in the initiation of the mannose outer chain. Leads to accumulation of free forms of oligosaccharides (fOSs).6 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871D → A: Loss of mannosyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 480480Initiation-specific alpha-1,6-mannosyltransferasePRO_0000080563Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence analysis
Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence analysis
Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence analysis
Glycosylationi393 – 3931N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP31755.

Expressioni

Inductioni

Expression is regulated by SKN7, SLN1, and CDC4.3 Publications

Interactioni

Protein-protein interaction databases

BioGridi33209. 22 interactions.
DIPiDIP-8030N.
MINTiMINT-4485492.

Structurei

3D structure databases

ProteinModelPortaliP31755.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi187 – 1893DXD motif1 Publication

Domaini

The conserved DXD motif is involved in enzyme activity.1 Publication

Sequence similaritiesi

Belongs to the glycosyltransferase 32 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000067666.
HOGENOMiHOG000174059.
InParanoidiP31755.
KOiK05528.
OMAiTDIMNWT.
OrthoDBiEOG7BP8BZ.

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.

P31755-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRKLSHLIA TRKSKTIVVT VLLIYSLLTF HLSNKRLLSQ FYPSKDDFKQ
60 70 80 90 100
TLLPTTSHSQ DINLKKQITV NKKKNQLHNL RDQLSFAFPY DSQAPIPQRV
110 120 130 140 150
WQTWKVGADD KNFPSSFRTY QKTWSGSYSP DYQYSLISDD SIIPFLENLY
160 170 180 190 200
APVPIVIQAF KLMPGNILKA DFLRYLLLFA RGGIYSDMDT MLLKPIDSWP
210 220 230 240 250
SQNKSWLNNI IDLNKPIPYK NSKPSLLSSD EISHQPGLVI GIEADPDRDD
260 270 280 290 300
WSEWYARRIQ FCQWTIQAKP GHPILRELIL NITATTLASV QNPGVPVSEM
310 320 330 340 350
IDPRFEEDYN VNYRHKRRHD ETYKHSELKN NKNVDGSDIM NWTGPGIFSD
360 370 380 390 400
IIFEYMNNVL RYNSDILLIN PNLNKNDEEG SESATTPAKD VDNDTLSKST
410 420 430 440 450
RKFYKKISES LQSSNSMPWE FFSFLKEPVI VDDVMVLPIT SFSPDVGQMG
460 470 480
AQSSDDKMAF VKHMFSGSWK EDADKNAGHK
Length:480
Mass (Da):55,156
Last modified:July 1, 1993 - v1
Checksum:i6B0ACA09A9B17E72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11095 Genomic DNA. Translation: BAA01869.1.
Z72560 Genomic DNA. Translation: CAA96740.1.
AY692749 Genomic DNA. Translation: AAT92768.1.
BK006941 Genomic DNA. Translation: DAA08062.1.
PIRiS22701.
RefSeqiNP_011477.1. NM_001180903.1.

Genome annotation databases

EnsemblFungiiYGL038C; YGL038C; YGL038C.
GeneIDi852845.
KEGGisce:YGL038C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11095 Genomic DNA. Translation: BAA01869.1.
Z72560 Genomic DNA. Translation: CAA96740.1.
AY692749 Genomic DNA. Translation: AAT92768.1.
BK006941 Genomic DNA. Translation: DAA08062.1.
PIRiS22701.
RefSeqiNP_011477.1. NM_001180903.1.

3D structure databases

ProteinModelPortaliP31755.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33209. 22 interactions.
DIPiDIP-8030N.
MINTiMINT-4485492.

Protein family/group databases

CAZyiGT32. Glycosyltransferase Family 32.

Proteomic databases

MaxQBiP31755.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL038C; YGL038C; YGL038C.
GeneIDi852845.
KEGGisce:YGL038C.

Organism-specific databases

EuPathDBiFungiDB:YGL038C.
SGDiS000003006. OCH1.

Phylogenomic databases

GeneTreeiENSGT00530000067666.
HOGENOMiHOG000174059.
InParanoidiP31755.
KOiK05528.
OMAiTDIMNWT.
OrthoDBiEOG7BP8BZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-30552-MONOMER.

Miscellaneous databases

NextBioi972428.
PROiP31755.

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. "OCH1 encodes a novel membrane bound mannosyltransferase: outer chain elongation of asparagine-linked oligosaccharides."
    Nakayama K., Nagasu T., Shimma Y., Kuromitsu J.-R., Jigami Y.
    EMBO J. 11:2511-2519(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, GLYCOSYLATION, SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION, CATALYTIC ACTIVITY.
    Strain: EHF-2C.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Isolation of new temperature-sensitive mutants of Saccharomyces cerevisiae deficient in mannose outer chain elongation."
    Nagasu T., Shimma Y., Nakanishi Y., Kuromitsu J., Iwama K., Nakayama K., Suzuki K., Jigami Y.
    Yeast 8:535-547(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Structure of the N-linked oligosaccharides that show the complete loss of alpha-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae."
    Nakanishi-Shindo Y., Nakayama K., Tanaka A., Toda Y., Jigami Y.
    J. Biol. Chem. 268:26338-26345(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  7. "Glycoprotein biosynthesis in Saccharomyces cerevisiae: ngd29, an N-glycosylation mutant allelic to och1 having a defect in the initiation of outer chain formation."
    Lehle L., Eiden A., Lehnert K., Haselbeck A., Kopetzki E.
    FEBS Lett. 370:41-45(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Localization of a yeast early Golgi mannosyltransferase, Och1p, involves retrograde transport."
    Harris S.L., Waters M.G.
    J. Cell Biol. 132:985-998(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Use of imidazoleglycerolphosphate dehydratase (His3) as a biological reporter in yeast."
    Horecka J., Sprague G.F. Jr.
    Methods Enzymol. 326:107-119(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "Defects in protein glycosylation cause SHO1-dependent activation of a STE12 signaling pathway in yeast."
    Cullen P.J., Schultz J., Horecka J., Stevenson B.J., Jigami Y., Sprague G.F. Jr.
    Genetics 155:1005-1018(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  11. "The eukaryotic two-component histidine kinase Sln1p regulates OCH1 via the transcription factor, Skn7p."
    Li S., Dean S., Li Z., Horecka J., Deschenes R.J., Fassler J.S.
    Mol. Biol. Cell 13:412-424(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  12. "Cdc4 is involved in the transcriptional control of OCH1, a gene encoding alpha-1,6-mannosyltransferase in Saccharomyces cerevisiae."
    Cui Z., Horecka J., Jigami Y.
    Yeast 19:69-77(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. "Retrograde transport of the mannosyltransferase Och1p to the early Golgi requires a component of the COG transport complex."
    Bruinsma P., Spelbrink R.G., Nothwehr S.F.
    J. Biol. Chem. 279:39814-39823(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  15. "Activity of recycling Golgi mannosyltransferases in the yeast endoplasmic reticulum."
    Karhinen L., Makarow M.
    J. Cell Sci. 117:351-358(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "Saccharomyces cerevisiae alpha1,6-mannosyltransferase has a catalytic potential to transfer a second mannose molecule."
    Kitajima T., Chiba Y., Jigami Y.
    FEBS J. 273:5074-5085(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, DOMAIN, MUTAGENESIS OF ASP-187.
  17. "Metabolism of free oligosaccharides is facilitated in the och1Delta mutant of Saccharomyces cerevisiae."
    Hirayama H., Suzuki T.
    Glycobiology 21:1341-1348(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  18. "Endoplasmic reticulum-associated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae."
    Chantret I., Kodali V.P., Lahmouich C., Harvey D.J., Moore S.E.
    J. Biol. Chem. 286:41786-41800(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiOCH1_YEAST
AccessioniPrimary (citable) accession number: P31755
Secondary accession number(s): D6VUA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 11, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 9490 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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.