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Q9C512 (MNS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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:
Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1
Short name=AtMANIb
EC=3.2.1.113
Alternative name(s):
Alpha-mannosidase IB
Gene names
Name:MNS1
Synonyms:MANIB
Ordered Locus Names:At1g51590
ORF Names:F19C24.18, F5D21.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length560 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.4 Ref.5

Catalytic activity

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2. Ref.5

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.4 Ref.5

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Ref.4 Ref.5.

Tissue specificity

Expressed in flowers, siliques, stems, leaves, roots, pollen grains, shoot apical meristems, hypocotyls and upper region of the root. Ref.4 Ref.5

Disruption phenotype

No visible phenotype, due the redundancy with MNS2. Lack of complex N-glycans, shorter roots and increased lateral root formation in double mutants mns1 mns2. Ref.4 Ref.5

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0. Stable from pH 4.5 to 6.5. Ref.5

Temperature dependence:

Optimum temperature is 25 degrees Celsius.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9C512-1)

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: Q9C512-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: Missing.
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 560560Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1
PRO_0000397933

Regions

Topological domain1 – 2727Cytoplasmic Potential
Transmembrane28 – 4720Helical; Signal-anchor for type II membrane protein; Potential
Topological domain48 – 560513Lumenal Potential
Coiled coil47 – 8034 Potential

Sites

Active site1791Proton donor By similarity
Active site3121 By similarity
Active site4451 By similarity

Amino acid modifications

Glycosylation3261N-linked (GlcNAc...) Potential
Glycosylation4591N-linked (GlcNAc...) Potential
Disulfide bond377 ↔ 409 By similarity

Natural variations

Alternative sequence1 – 104104Missing in isoform 2.
VSP_039724

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: BCC20CB9E63020B9

FASTA56063,532
        10         20         30         40         50         60 
MARSRSISGY GIWKYLNPAY YLRRPRRLAL LFIVFVSVSM LVWDRINLAR EHEVEVFKLN 

        70         80         90        100        110        120 
EEVSRLEQML EELNGGVGNK PLKTLKDAPE DPVDKQRRQK VKEAMIHAWS SYEKYAWGKD 

       130        140        150        160        170        180 
ELQPRTKDGT DSFGGLGATM VDSLDTLYIM GLDEQFQKAR EWVASSLDFD KDYDASMFET 

       190        200        210        220        230        240 
TIRVVGGLLS AYDLSGDKMF LEKAKDIADR LLPAWNTPTG IPYNIINLRN GNAHNPSWAA 

       250        260        270        280        290        300 
GGDSILADSG TEQLEFIALS QRTGDPKYQQ KVEKVITELN KNFPADGLLP IYINPDNANP 

       310        320        330        340        350        360 
SYSTTTFGAM GDSFYEYLLK VWVQGNKTSA VKPYRDMWEK SMKGLLSLVK KSTPSSFTYI 

       370        380        390        400        410        420 
CEKNGNNLID KMDELACFAP GMLALGASGY GPDEEKKFLS LAGELAWTCY NFYQSTPTKL 

       430        440        450        460        470        480 
AGENYFFTAG QDMSVGTSWN ILRPETVESL FYLWRLTGNK TYQEWGWNIF QAFEKNSRVE 

       490        500        510        520        530        540 
SGYVGLKDVN TGAKDNKMQS FFLAETLKYL YLLFSPSSVI SLDEWVFNTE AHPLKIVARN 

       550        560 
DPRKPTIALR QRKFGHQINV

« Hide

Isoform 2 [UniParc].

Checksum: 16E3C4590FAFCDFC
Show »

FASTA45651,349

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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.
[4]"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.
[5]"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		AC024261 Genomic DNA. Translation: AAG52623.1.
AC025294 Genomic DNA. Translation: AAG50876.1.
CP002684 Genomic DNA. Translation: AEE32686.1.
CP002684 Genomic DNA. Translation: AEE32687.1.
AY081353 mRNA. Translation: AAL91242.1.
AY128845 mRNA. Translation: AAM91245.1.
IPIIPI00530024.
IPI00656810.
PIRE96554.
RefSeqNP_001031171.1. NM_001036094.1.
NP_175570.1. NM_104037.4.
UniGeneAt.26180.
At.37784.
At.66909.

3D structure databases

HSSPHSSP built from PDB template 1FO3 based on UniProtKB Q9UKM7.
ProteinModelPortalQ9C512.
SMRQ9C512. Positions 97-536.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT1G51590.1-P.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

Proteomic databases

PaxDbQ9C512.
PRIDEQ9C512.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G51590.1; AT1G51590.1; AT1G51590.
GeneID841584.
KEGGath:AT1G51590.

Organism-specific databases

TAIRAt1g51590.

Phylogenomic databases

eggNOGNOG300315.
HOGENOMHOG000181987.
InParanoidQ9C512.
KOK01230.
OMATGIPYNI.
PhylomeDBQ9C512.
ProtClustDBCLSN2914679.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ9C512.

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. Glyco_hydro_47. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMNS1_ARATH
AccessionPrimary (citable) accession number: Q9C512
Secondary accession number(s): Q2V4H4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 1, 2001
Last modified: May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents