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Q8H116 (MNS2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2

Short name=AtMANIa
EC=3.2.1.113
Alternative name(s):
Alpha-mannosidase IA
Gene names
Name:MNS2
Synonyms:MANIA
Ordered Locus Names:At3g21160
ORF Names:MSA6.31
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Class I alpha-mannosidase essential for early N-glycan processing. Progressively trim alpha-1,2-linked mannose residues. Produces Man5GlcNAc2 from Man8GlcNAc2, but only Man6GlcNAc2 from Man9GlcNAc2. Have difficulty acting on the terminal mannose of the b-branch. Involved in root development and cell wall biosynthesis. Ref.5 Ref.6

Catalytic activity

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2. Ref.6

Cofactor

Calcium or manganese. Magnesium can be used to a lesser extent.

Enzyme regulation

Inhibited by kifunensine and 1-deoxymannojirimycin, but not by swainsonine. Ref.5 Ref.6

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Ref.5 Ref.6.

Tissue specificity

Expressed in flowers, siliques, stems, leaves, roots, pollen grains and shoot apical meristems. Ref.5 Ref.6

Disruption phenotype

No visible phenotype; due the redundancy with MNS1. Lack of complex N-glycans, shorter roots and increased lateral root formation in mns1 and mns2 double mutants. Ref.5 Ref.6

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0. Stable from pH 5.0 to 10.0. Ref.6

Temperature dependence:

Optimum temperature is 25 degrees Celsius.

Sequence caution

The sequence BAB01459.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2
PRO_0000397934

Regions

Topological domain1 – 2727Cytoplasmic Potential
Transmembrane28 – 4518Helical; Signal-anchor for type II membrane protein; Potential
Topological domain46 – 572527Lumenal Potential
Coiled coil51 – 8131 Potential

Sites

Active site1801Proton donor By similarity
Active site3121 By similarity
Active site4461 By similarity

Amino acid modifications

Glycosylation3261N-linked (GlcNAc...) Potential
Glycosylation4601N-linked (GlcNAc...) Potential
Disulfide bond377 ↔ 410 By similarity

Experimental info

Sequence conflict1131Y → H in AAK92711. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8H116 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 14614DD4525F9499

FASTA57265,136
        10         20         30         40         50         60 
MARNKLVSGS HGIWKYFNPA FYLRRPRRLA LLIILFVSVS MVVWDRQSLS RDYQFEVSKL 

        70         80         90        100        110        120 
NEEVLRLQQM LEEIKSVTED VSVNSLKDVQ EDPVDAQRMQ RVKEAMVHAW SSYEKYAWGQ 

       130        140        150        160        170        180 
DELQPQTKDG VDSFGGLGAT MIDALDTLYI MGLDEQFQKA REWVASSLDF DKDYAASMFE 

       190        200        210        220        230        240 
TTIRVVGGLL SAYDLSGDKI FLEKAMDIAD RLLPAWDTQS GIPYNIINLK HGNAHNPTWA 

       250        260        270        280        290        300 
GGDSILADSG TEQLEFIALS QRTGDPKYQQ KVEKVISVLN KNFPADGLLP IYINPDTANP 

       310        320        330        340        350        360 
SQSTITFGAM GDSFYEYLLK VWVFGNKTSA VKHYRDMWEK SMNGLLSLVK KSTPLSFTYI 

       370        380        390        400        410        420 
CEKSGNSLID KMDELACFAP GMLALGASGY SDPAEGKKFL TLAEELAWTC YNFYQSTPTK 

       430        440        450        460        470        480 
LAGENYFFNS GSDMSVGTSW NILRPETVES LFYLWRLTGN KTYQEWGWNI FEAFEKNSRI 

       490        500        510        520        530        540 
ESGYVGLKDV NTGVKDNKMQ SFFLAETLKY LYLLFSPTTV IPLDEWVFNT EAHPLKIKSR 

       550        560        570 
NDQVNLKQSN KVLLRKPAFR IRQRHYGRIT KK 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [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]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Class I alpha-mannosidases are required for N-glycan processing and root development in Arabidopsis thaliana."
Liebminger E., Huttner S., Vavra U., Fischl R., Schoberer J., Grass J., Blaukopf C., Seifert G.J., Altmann F., Mach L., Strasser R.
Plant Cell 21:3850-3867(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION, DISRUPTION PHENOTYPE.
[6]"Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible for plant N-glycan maturation."
Kajiura H., Koiwa H., Nakazawa Y., Okazawa A., Kobayashi A., Seki T., Fujiyama K.
Glycobiology 20:235-247(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP000604, AB023045 Genomic DNA. Translation: BAB01459.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE76468.1.
AY050776 mRNA. Translation: AAK92711.1.
BT000893 mRNA. Translation: AAN41293.1.
RefSeqNP_566675.1. NM_113010.2.
UniGeneAt.25787.

3D structure databases

ProteinModelPortalQ8H116.
SMRQ8H116. Positions 98-537.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid7000. 1 interaction.
IntActQ8H116. 1 interaction.
STRING3702.AT3G21160.1-P.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

Proteomic databases

PaxDbQ8H116.
PRIDEQ8H116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G21160.1; AT3G21160.1; AT3G21160.
GeneID821668.
KEGGath:AT3G21160.

Organism-specific databases

TAIRAT3G21160.

Phylogenomic databases

eggNOGNOG300315.
HOGENOMHOG000181987.
InParanoidQ8H116.
KOK01230.
OMATSAVKHY.
PhylomeDBQ8H116.

Enzyme and pathway databases

BioCycARA:AT3G21160-MONOMER.
UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ8H116.

Family and domain databases

Gene3D1.50.10.50. 1 hit.
InterProIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERPTHR11742. PTHR11742. 1 hit.
PfamPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSPR00747. GLYHDRLASE47.
SUPFAMSSF48225. SSF48225. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMNS2_ARATH
AccessionPrimary (citable) accession number: Q8H116
Secondary accession number(s): Q94A04, Q9LJB6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 69 of the entry and version 1 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names