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Q93Y37 (MNS3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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 MNS3
EC=3.2.1.113
Gene names
Name:MNS3
Ordered Locus Names:At1g30000
ORF Names:T1P2.10
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 length624 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Class I alpha-mannosidase essential for early N-glycan processing. Removes preferentially alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man8GlcNAc2. Involved in root development and cell wall biosynthesis. Ref.4

Catalytic activity

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

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

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus › cis-Golgi network membrane Probable; Single-pass type II membrane protein Ref.4.

Tissue specificity

Expressed in flowers, siliques, stems, leaves, roots, stamens and sepals. Ref.4

Disruption phenotype

Formation of aberrant N-glycan structures. Ref.4

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Sequence caution

The sequence AAG52061.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 624624Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3
PRO_0000397935

Regions

Topological domain1 – 4343Cytoplasmic Potential
Transmembrane44 – 6421Helical; Signal-anchor for type II membrane protein; Potential
Topological domain65 – 624560Lumenal Potential

Sites

Active site2121Proton donor By similarity
Active site3571 By similarity
Active site5261 By similarity

Amino acid modifications

Glycosylation691N-linked (GlcNAc...) Potential
Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation3771N-linked (GlcNAc...) Potential
Glycosylation5031N-linked (GlcNAc...) Potential
Disulfide bond428 ↔ 471 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q93Y37 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: A28B82AD7FAAD29D

FASTA62469,069
        10         20         30         40         50         60 
MSKSLPYSVK DIHYDNAKFR HRSPLKVFSQ SLLTLSTKRN YASCSTGKFL ILILFFGVAC 

        70         80         90        100        110        120 
LMLMSKSPNE SGLNEKGKVT FVGGLRLGGL LRKPPRLPPR LSPDEGQLRG SSTNGSTISN 

       130        140        150        160        170        180 
SDPKWAARQQ SVKEAFDHAW SGYRKYAMGY DELMPISQKG VDGLGGLGAT VVDALDTAMI 

       190        200        210        220        230        240 
MGLDNIVSEA GSWVETHLLE RISQKGQVNL FETTIRVLGG LLSAYHLSGG EQGTVNMTHV 

       250        260        270        280        290        300 
GPKPVIYLNI AKDLADRLLS AFTSSPTPVP FCDVILHEST AHPAPGGASS TAEVASVQLE 

       310        320        330        340        350        360 
FNYLSSISGD PKYSTEAMKV LAHIKTLPKT EGLVPIYISP QTGDFVGENI RLGSRGDSYY 

       370        380        390        400        410        420 
EYLIKVWLQQ GAKLNSNFTY LHDMYIEAMK GVRHLLVQNS IPKGLVFVGE LPYGSKGEFS 

       430        440        450        460        470        480 
PKMDHLVCFL PGTLALGATK GLTKEQALKE NLLSFEDLEN LKLAEDLAKT CFEMYEVTAT 

       490        500        510        520        530        540 
GLAPEIAYFH TKDYTEDGLD GGNKSSMYAN DIIIKPADRH NLLRPETVES LFVLYRITKD 

       550        560        570        580        590        600 
TKYRDQGWQI FEAFEKYTKV KSGGYTSLDD VTEVPPHRRD KMETFFLGET LKYLYLLFGD 

       610        620 
DSVIPLDKFV FNTEAHPLPI RRNT

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC022455 Genomic DNA. Translation: AAG52061.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE31166.1.
AY054482 mRNA. Translation: AAK96673.1.
AY093280 mRNA. Translation: AAM13279.1.
IPIIPI00521182.
PIRH86423.
RefSeqNP_564345.1. NM_102740.2.
UniGeneAt.26476.

3D structure databases

HSSPHSSP built from PDB template 1FO3 based on UniProtKB Q9UKM7.
ProteinModelPortalQ93Y37.
SMRQ93Y37. Positions 128-620.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT1G30000.1-P.

Protein family/group databases

CAZyGH47. Glycoside Hydrolase Family 47.

Proteomic databases

PaxDbQ93Y37.
PRIDEQ93Y37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G30000.1; AT1G30000.1; AT1G30000.
GeneID839879.
KEGGath:AT1G30000.

Organism-specific databases

TAIRAt1g30000.

Phylogenomic databases

eggNOGNOG300315.
HOGENOMHOG000181987.
InParanoidQ93Y37.
KOK01230.
OMAHFNLHAQ.
PhylomeDBQ93Y37.
ProtClustDBCLSN2917102.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ93Y37.

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 nameMNS3_ARATH
AccessionPrimary (citable) accession number: Q93Y37
Secondary accession number(s): Q9C8R9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 1, 2001
Last modified: May 1, 2013
This is version 68 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

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