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Protein

Alpha-1,2 mannosyltransferase KTR1

Gene

KTR1

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 that transfers a mannose residue from GDP-mannose to a range of acceptors in vitro.

Catalytic activityi

Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.

Cofactori

Pathwayi: protein glycosylation

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei280 – 2801NucleophileSequence analysis

GO - Molecular functioni

  • alpha-1,2-mannosyltransferase activity Source: SGD

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese

Enzyme and pathway databases

BioCyciYEAST:G3O-33632-MONOMER.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT15. Glycosyltransferase Family 15.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1,2 mannosyltransferase KTR1 (EC:2.4.1.-)
Gene namesi
Name:KTR1
Ordered Locus Names:YOR099W
ORF Names:YOR3189W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR099W.
SGDiS000005625. KTR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence analysisAdd
BLAST
Transmembranei17 – 3418Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini35 – 393359LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • Golgi apparatus Source: SGD
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Alpha-1,2 mannosyltransferase KTR1PRO_0000208242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP27810.
PeptideAtlasiP27810.

Interactioni

Protein-protein interaction databases

BioGridi34497. 29 interactions.
DIPiDIP-7181N.
IntActiP27810. 1 interaction.
MINTiMINT-4502784.

Structurei

3D structure databases

ProteinModelPortaliP27810.
SMRiP27810. Positions 64-389.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 6834Stem regionBy similarityAdd
BLAST
Regioni69 – 393325CatalyticBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 15 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000000831.
HOGENOMiHOG000160667.
InParanoidiP27810.
KOiK10967.
OMAiYSCTARF.
OrthoDBiEOG779P83.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002685. Glyco_trans_15.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR31121. PTHR31121. 1 hit.
PfamiPF01793. Glyco_transf_15. 1 hit.
[Graphical view]
PIRSFiPIRSF018153. Glyco_trans_15. 1 hit.
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P27810-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKIMIPASK QPVYKKLGLL LVAVFTVYVF FHGAQYARGS APSPKYSTVL
60 70 80 90 100
SSGSGYKYSK VELPKYTGPR EKATFVTLVR NRDLYSLAES IKSVEDRFNS
110 120 130 140 150
KFNYDWVFLN DEEFTDEFKN VTSALVSGTT KYGVIPKEHW SFPEWIDEEK
160 170 180 190 200
AAQVRKEMGE KRIIYGDSIS YRHMCRFESG FFYRHPLMDD YDWYWRVEPD
210 220 230 240 250
IKLHCDIDYD VFKFMKDNKK KYAFAISIKE YEATIPTLWE TTRKFMEAHP
260 270 280 290 300
ELIHENNMLD FVSDDQGLSY NLCHFWSNFE IAALDLWRSP AYSAYFDYLD
310 320 330 340 350
REGGFFYERW GDAPVHSIGA ALFLDRSEIH HFGDIGYYHV PFHSCPIDTS
360 370 380 390
IRLANKCDCD PSKDFTWHSY SCTTKFYNIN KLPKPAGWQN HIG
Length:393
Mass (Da):46,022
Last modified:August 1, 1992 - v1
Checksum:iF93DDF2953EA287B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62941 Genomic DNA. Translation: CAA44713.1.
X94335 Genomic DNA. Translation: CAA64021.1.
Z75007 Genomic DNA. Translation: CAA99296.1.
BK006948 Genomic DNA. Translation: DAA10876.1.
PIRiS61659.
RefSeqiNP_014742.1. NM_001183518.1.

Genome annotation databases

EnsemblFungiiYOR099W; YOR099W; YOR099W.
GeneIDi854266.
KEGGisce:YOR099W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62941 Genomic DNA. Translation: CAA44713.1.
X94335 Genomic DNA. Translation: CAA64021.1.
Z75007 Genomic DNA. Translation: CAA99296.1.
BK006948 Genomic DNA. Translation: DAA10876.1.
PIRiS61659.
RefSeqiNP_014742.1. NM_001183518.1.

3D structure databases

ProteinModelPortaliP27810.
SMRiP27810. Positions 64-389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34497. 29 interactions.
DIPiDIP-7181N.
IntActiP27810. 1 interaction.
MINTiMINT-4502784.

Protein family/group databases

CAZyiGT15. Glycosyltransferase Family 15.

Proteomic databases

MaxQBiP27810.
PeptideAtlasiP27810.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR099W; YOR099W; YOR099W.
GeneIDi854266.
KEGGisce:YOR099W.

Organism-specific databases

EuPathDBiFungiDB:YOR099W.
SGDiS000005625. KTR1.

Phylogenomic databases

GeneTreeiENSGT00390000000831.
HOGENOMiHOG000160667.
InParanoidiP27810.
KOiK10967.
OMAiYSCTARF.
OrthoDBiEOG779P83.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciYEAST:G3O-33632-MONOMER.

Miscellaneous databases

NextBioi976212.
PROiP27810.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002685. Glyco_trans_15.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR31121. PTHR31121. 1 hit.
PfamiPF01793. Glyco_transf_15. 1 hit.
[Graphical view]
PIRSFiPIRSF018153. Glyco_trans_15. 1 hit.
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast KRE2 defines a new gene family encoding probable secretory proteins, and is required for the correct N-glycosylation of proteins."
    Hill K., Boone C., Goebl M., Puccia R., Sdicu A.-M., Bussey H.
    Genetics 130:273-283(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Ktr1p is an alpha-1,2-mannosyltransferase of Saccharomyces cerevisiae. Comparison of the enzymic properties of soluble recombinant Ktr1p and Kre2p/Mnt1p produced in Pichia pastoris."
    Romero P.A., Lussier M., Sdicu A.-M., Bussey H.
    Biochem. J. 321:289-295(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
    Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
    Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKTR1_YEAST
AccessioniPrimary (citable) accession number: P27810
Secondary accession number(s): D6W2G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 11, 2016
This is version 141 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 5480 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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