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Q9XEE9 (ALG11_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase

EC=2.4.1.131
Alternative name(s):
Alpha-1,2-mannosyltransferase ALG11
Asparagine-linked glycosylation protein 11
Protein LEAF WILTING 3
Gene names
Name:ALG11
Synonyms:LEW3
Ordered Locus Names:At2g40190
ORF Names:T07M07.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum. Ref.6

Catalytic activity

2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = 2 GDP + D-Man-alpha-(1->2)-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. Ref.6

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.6.

Tissue specificity

Expressed in shoots, leaves, sepals, filaments, siliques, stems, roots and guard cells. Ref.6

Disruption phenotype

Lethality. Ref.6

Miscellaneous

In the absence of ALG11 activity, no N-glycans are produced and transferred to proteins.

Sequence similarities

Belongs to the glycosyltransferase 4 family.

Sequence caution

The sequence AAD25934.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9XEE9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9XEE9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-212: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
PRO_0000412585

Regions

Transmembrane3 – 2321Helical; Potential
Transmembrane204 – 22623Helical; Potential
Compositional bias46 – 494Poly-Gly

Amino acid modifications

Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation3141N-linked (GlcNAc...) Potential
Glycosylation4231N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 212212Missing in isoform 2.
VSP_041714

Experimental info

Mutagenesis1481G → E in lew3; deficiency in N-glycosylation leading to dwarf phenotype, reduced fertility and impaired cellulose synthesis. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 21, 2011. Version 2.
Checksum: 7092C34149CD4AE1

FASTA46352,573
        10         20         30         40         50         60 
MAIYFILYTL LTIIFAVSLS LFLSVINARK SRKRAVGFFH PYTNDGGGGE RVLWCAVKAI 

        70         80         90        100        110        120 
QEENPDLDCV IFTGDHDSSS DSLARRAVDR FGVHLQSPPK VIHLNKRKWI EESTYPHFTM 

       130        140        150        160        170        180 
IGQSLGSVYL AWEALRMFTP LYFLDTSGYA FTYPLARIFG CKVVCYTHYP TISLDMISRV 

       190        200        210        220        230        240 
RQRNSMYNND ASIAKSNWLS TCKLVYYRAF SWMYGMVGSC THLAMVNSSW TKSHIEVLWR 

       250        260        270        280        290        300 
IPERITRVYP PCDTSGLQAF PLERSSDPPK IISVAQFRPE KAHMLQLEAF SLALEKLDAD 

       310        320        330        340        350        360 
VPRPKLQFVG SCRNNSDEER LQKLKDRAVE LKVDGDVQFY KNAMYRELVE LLGNAVAGLH 

       370        380        390        400        410        420 
GMIDEHFGIS VVEYMAAGAI PIAHNSAGPK MDIVLEEDGQ KTGFLAETVE EYAEAILEIV 

       430        440        450        460 
KMNETERLKM AESARKRAAR FSEQRFCEDF KTAIRPIFTG PLK 

« Hide

Isoform 2 [UniParc].

Checksum: CFB26F285390374C
Show »

FASTA25128,261

References

« Hide 'large scale' references
[1]"A cluster of ABA-regulated genes on Arabidopsis thaliana BAC T07M07."
Wang M.L., Belmonte S., Kim U., Dolan M., Morris J.W., Goodman H.M.
Genome Res. 9:325-333(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K. expand/collapse author list , Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"Arabidopsis ORF clones."
Cheuk R., Chen H., Kim C.J., Shinn P., Bowser L., Carninci P., Dale J.M., Hayashizaki Y., Ishida J., Jones T., Kamiya A., Karlin-Neumann G., Kawai J., Lam B., Lin J., Miranda M., Narusaka M., Nguyen M. expand/collapse author list , Onodera C.S., Palm C.J., Quach H.L., Sakurai T., Satou M., Seki M., Southwick A., Toriumi M., Wong C., Wu H.C., Yamada K., Yu G., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-463.
[6]"LEW3, encoding a putative alpha-1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana."
Zhang M., Henquet M., Chen Z., Zhang H., Zhang Y., Ren X., van der Krol S., Gonneau M., Bosch D., Gong Z.
Plant J. 60:983-999(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-148, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF085279 Genomic DNA. Translation: AAD25934.1. Sequence problems.
CP002685 Genomic DNA. Translation: AEC09794.1.
AK227731 mRNA. Translation: BAE99716.1.
BT009712 mRNA. Translation: AAP88346.1.
PIRD84826.
RefSeqNP_181548.2. NM_129577.4. [Q9XEE9-1]
UniGeneAt.21597.

3D structure databases

ProteinModelPortalQ9XEE9.
SMRQ9XEE9. Positions 272-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G40190.1-P.

Protein family/group databases

CAZyGT4. Glycosyltransferase Family 4.

Proteomic databases

PRIDEQ9XEE9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G40190.1; AT2G40190.1; AT2G40190. [Q9XEE9-1]
GeneID818610.
KEGGath:AT2G40190.

Organism-specific databases

TAIRAT2G40190.

Phylogenomic databases

eggNOGCOG0438.
HOGENOMHOG000209670.
InParanoidQ0WT32.
KOK03844.
OMAGTVILAH.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ9XEE9.

Family and domain databases

InterProIPR001296. Glyco_trans_1.
[Graphical view]
PfamPF00534. Glycos_transf_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9XEE9.

Entry information

Entry nameALG11_ARATH
AccessionPrimary (citable) accession number: Q9XEE9
Secondary accession number(s): F4IH01, Q0WT32, Q7DNH4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: May 14, 2014
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names