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Protein

Alpha-1,2-mannosyltransferase ALG9

Gene

ALG9

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

Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides.1 Publication

Catalytic activityi

Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.1 Publication
Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.1 Publication

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.

GO - Molecular functioni

  • dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity Source: UniProtKB-EC
  • dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity Source: UniProtKB-EC
  • glycolipid mannosyltransferase activity Source: SGD
  • mannosyltransferase activity Source: SGD

GO - Biological processi

  • dolichol-linked oligosaccharide biosynthetic process Source: SGD
  • mannosylation Source: GOC
  • protein glycosylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7189.
YEAST:YNL219C-MONOMER.
BRENDAi2.4.1.259. 984.
ReactomeiR-SCE-446193. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT22. Glycosyltransferase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1,2-mannosyltransferase ALG9 (EC:2.4.1.259, EC:2.4.1.261)
Alternative name(s):
Asparagine-linked glycosylation protein 9
Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
Gene namesi
Name:ALG9
Ordered Locus Names:YNL219C
ORF Names:N1295
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL219C.
SGDiS000005163. ALG9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence analysis
Transmembranei8 – 2821HelicalSequence analysisAdd
BLAST
Topological domaini29 – 6234LumenalSequence analysisAdd
BLAST
Transmembranei63 – 8321HelicalSequence analysisAdd
BLAST
Topological domaini84 – 863CytoplasmicSequence analysis
Transmembranei87 – 10721HelicalSequence analysisAdd
BLAST
Topological domaini108 – 1136LumenalSequence analysis
Transmembranei114 – 13421HelicalSequence analysisAdd
BLAST
Topological domaini135 – 17642CytoplasmicSequence analysisAdd
BLAST
Transmembranei177 – 19721HelicalSequence analysisAdd
BLAST
Topological domaini198 – 21316LumenalSequence analysisAdd
BLAST
Transmembranei214 – 23421HelicalSequence analysisAdd
BLAST
Topological domaini235 – 26834CytoplasmicSequence analysisAdd
BLAST
Transmembranei269 – 28921HelicalSequence analysisAdd
BLAST
Topological domaini290 – 31627LumenalSequence analysisAdd
BLAST
Transmembranei317 – 33721HelicalSequence analysisAdd
BLAST
Topological domaini338 – 34912CytoplasmicSequence analysisAdd
BLAST
Transmembranei350 – 37021HelicalSequence analysisAdd
BLAST
Topological domaini371 – 555185LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 555555Alpha-1,2-mannosyltransferase ALG9PRO_0000215789Add
BLAST

Proteomic databases

MaxQBiP53868.
PeptideAtlasiP53868.

Interactioni

Protein-protein interaction databases

BioGridi35617. 221 interactions.
DIPiDIP-4288N.
IntActiP53868. 7 interactions.
MINTiMINT-507147.

Structurei

3D structure databases

ProteinModelPortaliP53868.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 22 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000004731.
HOGENOMiHOG000205434.
InParanoidiP53868.
KOiK03846.
OMAiWFHASVE.
OrthoDBiEOG70PC6J.

Family and domain databases

InterProiIPR005599. GPI_mannosylTrfase.
[Graphical view]
PANTHERiPTHR22760. PTHR22760. 1 hit.
PfamiPF03901. Glyco_transf_22. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53868-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNCKAVTISL LLLLFLTRVY IQPTFSLISD CDETFNYWEP LNLLVRGFGK
60 70 80 90 100
QTWEYSPEYS IRSWAFLLPF YCILYPVNKF TDLESHWNFF ITRACLGFFS
110 120 130 140 150
FIMEFKLHRE IAGSLALQIA NIWIIFQLFN PGWFHASVEL LPSAVAMLLY
160 170 180 190 200
VGATRHSLRY LSTGSTSNFT KSLAYNFLAS ILGWPFVLIL SLPLCLHYLF
210 220 230 240 250
NHRIISTIRT AFDCCLIFSL TAFAVIVTDS IFYGKLAPVS WNILFYNVIN
260 270 280 290 300
ASEESGPNIF GVEPWYYYPL NLLLNFPLPV LVLAILGIFH LRLWPLWASL
310 320 330 340 350
FTWIAVFTQQ PHKEERFLYP IYGLITLSAS IAFYKVLNLF NRKPILKKGI
360 370 380 390 400
KLSVLLIVAG QAMSRIVALV NNYTAPIAVY EQFSSLNQGG VKAPVVNVCT
410 420 430 440 450
GREWYHFPSS FLLPDNHRLK FVKSGFDGLL PGDFPESGSI FKKIRTLPKG
460 470 480 490 500
MNNKNIYDTG KEWPITRCDY FIDIVAPINL TKDVFNPLHL MDNWNKLACA
510 520 530 540 550
AFIDGENSKI LGRAFYVPEP INRIMQIVLP KQWNQVYGVR YIDYCLFEKP

TETTN
Length:555
Mass (Da):63,777
Last modified:October 1, 1996 - v1
Checksum:i108ED4E0B0C2AAA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96417 Genomic DNA. Translation: CAA65277.1.
Z71495 Genomic DNA. Translation: CAA96122.1.
BK006947 Genomic DNA. Translation: DAA10337.1.
PIRiS63177.
RefSeqiNP_014180.1. NM_001183057.1.

Genome annotation databases

EnsemblFungiiYNL219C; YNL219C; YNL219C.
GeneIDi855502.
KEGGisce:YNL219C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96417 Genomic DNA. Translation: CAA65277.1.
Z71495 Genomic DNA. Translation: CAA96122.1.
BK006947 Genomic DNA. Translation: DAA10337.1.
PIRiS63177.
RefSeqiNP_014180.1. NM_001183057.1.

3D structure databases

ProteinModelPortaliP53868.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35617. 221 interactions.
DIPiDIP-4288N.
IntActiP53868. 7 interactions.
MINTiMINT-507147.

Protein family/group databases

CAZyiGT22. Glycosyltransferase Family 22.

Proteomic databases

MaxQBiP53868.
PeptideAtlasiP53868.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL219C; YNL219C; YNL219C.
GeneIDi855502.
KEGGisce:YNL219C.

Organism-specific databases

EuPathDBiFungiDB:YNL219C.
SGDiS000005163. ALG9.

Phylogenomic databases

GeneTreeiENSGT00390000004731.
HOGENOMiHOG000205434.
InParanoidiP53868.
KOiK03846.
OMAiWFHASVE.
OrthoDBiEOG70PC6J.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:MONOMER-7189.
YEAST:YNL219C-MONOMER.
BRENDAi2.4.1.259. 984.
ReactomeiR-SCE-446193. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

NextBioi979502.
PROiP53868.

Family and domain databases

InterProiIPR005599. GPI_mannosylTrfase.
[Graphical view]
PANTHERiPTHR22760. PTHR22760. 1 hit.
PfamiPF03901. Glyco_transf_22. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Stepwise assembly of the lipid-linked oligosaccharide in the endoplasmic reticulum of Saccharomyces cerevisiae: identification of the ALG9 gene encoding a putative mannosyl transferase."
    Burda P., Te Heesen S., Brachat A., Wach A., Duesterhoeft A., Aebi M.
    Proc. Natl. Acad. Sci. U.S.A. 93:7160-7165(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SS328.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis."
    Frank C.G., Aebi M.
    Glycobiology 15:1156-1163(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.

Entry informationi

Entry nameiALG9_YEAST
AccessioniPrimary (citable) accession number: P53868
Secondary accession number(s): D6W0X1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 119 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. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.