Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glycolipid 2-alpha-mannosyltransferase

Gene

KRE2

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

Required for the attachment of the third mannose residue of O-linked saccharides.

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 sitei329 – 3291NucleophileSequence analysis

GO - Molecular functioni

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

GO - Biological processi

  • cell wall mannoprotein biosynthetic process Source: SGD
  • N-glycan processing 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-30008-MONOMER.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT15. Glycosyltransferase Family 15.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycolipid 2-alpha-mannosyltransferase (EC:2.4.1.-)
Alternative name(s):
Alpha-1,2-mannosyltransferase
Gene namesi
Name:KRE2
Synonyms:MNT1
Ordered Locus Names:YDR483W
ORF Names:D8035.26
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR483W.
SGDiS000002891. KRE2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence analysisAdd
BLAST
Transmembranei12 – 3019Helical; Signal-anchor for type II membrane proteinAdd
BLAST
Topological domaini31 – 442412LumenalSequence 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 – 442442Glycolipid 2-alpha-mannosyltransferasePRO_0000208241Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi197 – 1971N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP27809.
PRIDEiP27809.

Interactioni

Protein-protein interaction databases

BioGridi32535. 26 interactions.
DIPiDIP-5373N.
IntActiP27809. 11 interactions.
MINTiMINT-514227.

Structurei

Secondary structure

1
442
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi106 – 1105Combined sources
Helixi111 – 1133Combined sources
Beta strandi123 – 1286Combined sources
Helixi131 – 1333Combined sources
Helixi134 – 14714Combined sources
Turni148 – 1514Combined sources
Beta strandi156 – 1627Combined sources
Helixi166 – 17510Combined sources
Beta strandi180 – 1845Combined sources
Helixi187 – 1893Combined sources
Helixi198 – 20811Combined sources
Turni209 – 2113Combined sources
Turni213 – 2164Combined sources
Helixi218 – 22912Combined sources
Helixi231 – 2333Combined sources
Helixi235 – 2373Combined sources
Beta strandi241 – 2455Combined sources
Helixi260 – 2667Combined sources
Beta strandi271 – 2744Combined sources
Beta strandi276 – 2783Combined sources
Helixi281 – 2833Combined sources
Helixi287 – 29711Combined sources
Helixi299 – 3013Combined sources
Helixi308 – 3114Combined sources
Beta strandi322 – 3243Combined sources
Beta strandi328 – 3325Combined sources
Helixi333 – 3364Combined sources
Helixi339 – 35113Combined sources
Helixi353 – 3564Combined sources
Helixi361 – 37212Combined sources
Helixi375 – 3773Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi386 – 3883Combined sources
Beta strandi391 – 3933Combined sources
Helixi398 – 4036Combined sources
Helixi410 – 4123Combined sources
Helixi422 – 4298Combined sources
Helixi437 – 4415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4NX-ray2.01A/B97-442[»]
1S4OX-ray2.01A/B97-442[»]
1S4PX-ray2.01A/B97-442[»]
ProteinModelPortaliP27809.
SMRiP27809. Positions 104-442.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27809.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni31 – 11888Stem regionAdd
BLAST
Regioni119 – 442324CatalyticAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 15 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000000831.
HOGENOMiHOG000160667.
InParanoidiP27809.
KOiK10967.
OMAiHFHCDID.
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.

P27809-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALFLSKRLL RFTVIAGAVI VLLLTLNSNS RTQQYIPSSI SAAFDFTSGS
60 70 80 90 100
ISPEQQVISE ENDAKKLEQS ALNSEASEDS EAMDEESKAL KAAAEKADAP
110 120 130 140 150
IDTKTTMDYI TPSFANKAGK PKACYVTLVR NKELKGLLSS IKYVENKINK
160 170 180 190 200
KFPYPWVFLN DEPFTEEFKE AVTKAVSSEV KFGILPKEHW SYPEWINQTK
210 220 230 240 250
AAEIRADAAT KYIYGGSESY RHMCRYQSGF FWRHELLEEY DWYWRVEPDI
260 270 280 290 300
KLYCDINYDV FKWMQENEKV YGFTVSIHEY EVTIPTLWQT SMDFIKKNPE
310 320 330 340 350
YLDENNLMSF LSNDNGKTYN LCHFWSNFEI ANLNLWRSPA YREYFDTLDH
360 370 380 390 400
QGGFFYERWG DAPVHSIAAA LFLPKDKIHY FSDIGYHHPP YDNCPLDKEV
410 420 430 440
YNSNNCECDQ GNDFTFQGYS CGKEYYDAQG LVKPKNWKKF RE
Length:442
Mass (Da):51,387
Last modified:August 1, 1992 - v1
Checksum:iE2A54786F8C8AA60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81110 Genomic DNA. Translation: AAA34784.1.
X62647 Genomic DNA. Translation: CAA44516.1.
U33050 Genomic DNA. Translation: AAB64906.1.
Z29988 Genomic DNA. Translation: CAA82879.1.
BK006938 Genomic DNA. Translation: DAA12316.1.
PIRiS32592.
RefSeqiNP_010771.1. NM_001180791.1.

Genome annotation databases

EnsemblFungiiYDR483W; YDR483W; YDR483W.
GeneIDi852094.
KEGGisce:YDR483W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81110 Genomic DNA. Translation: AAA34784.1.
X62647 Genomic DNA. Translation: CAA44516.1.
U33050 Genomic DNA. Translation: AAB64906.1.
Z29988 Genomic DNA. Translation: CAA82879.1.
BK006938 Genomic DNA. Translation: DAA12316.1.
PIRiS32592.
RefSeqiNP_010771.1. NM_001180791.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4NX-ray2.01A/B97-442[»]
1S4OX-ray2.01A/B97-442[»]
1S4PX-ray2.01A/B97-442[»]
ProteinModelPortaliP27809.
SMRiP27809. Positions 104-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32535. 26 interactions.
DIPiDIP-5373N.
IntActiP27809. 11 interactions.
MINTiMINT-514227.

Protein family/group databases

CAZyiGT15. Glycosyltransferase Family 15.

Proteomic databases

MaxQBiP27809.
PRIDEiP27809.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR483W; YDR483W; YDR483W.
GeneIDi852094.
KEGGisce:YDR483W.

Organism-specific databases

EuPathDBiFungiDB:YDR483W.
SGDiS000002891. KRE2.

Phylogenomic databases

GeneTreeiENSGT00390000000831.
HOGENOMiHOG000160667.
InParanoidiP27809.
KOiK10967.
OMAiHFHCDID.
OrthoDBiEOG779P83.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciYEAST:G3O-30008-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP27809.
PROiP27809.

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. "Glycosylation in Saccharomyces cerevisiae: cloning and characterization of an alpha-1,2-mannosyltransferase structural gene."
    Haeusler A., Robbins P.W.
    Glycobiology 2:77-84(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-197.
  2. "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].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(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. "Nucleotide sequence of the SAC2 gene of Saccharomyces cerevisiae."
    Koelling R., Lee A., Chen E.Y., Botstein D.
    Yeast 10:1211-1216(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-442.
    Strain: ATCC 204508 / S288c.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKRE2_YEAST
AccessioniPrimary (citable) accession number: P27809
Secondary accession number(s): D6VTA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 6, 2016
This is version 158 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 13000 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.