Q8H116 (MNS2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Protein existence	Evidence 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 and magnesium at 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 double mutants mns1 mns2. 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.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Coiled coil Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Magnesium Manganese
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	N-glycan processing Inferred from mutant phenotype Ref.5. Source: TAIR root development Inferred from genetic interaction Ref.5. Source: TAIR
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-mannosidase activity Inferred from direct assay Ref.6Ref.5. Source: TAIR calcium ion binding Inferred from electronic annotation. Source: InterPro mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 572	572	Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2		PRO_0000397934
Regions
	Topological domain	1 – 27	27	Cytoplasmic Potential
	Transmembrane	28 – 45	18	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	46 – 572	527	Lumenal Potential
	Coiled coil	51 – 81	31	Potential
Sites
	Active site	180	1	Proton donor By similarity
	Active site	312	1	By similarity
	Active site	446	1	By similarity
Amino acid modifications
	Glycosylation	326	1	N-linked (GlcNAc...) Potential
	Glycosylation	460	1	N-linked (GlcNAc...) Potential
	Disulfide bond	377 ↔ 410		By similarity
Experimental info
	Sequence conflict	113	1	Y → H in AAK92711. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8H116 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 14614DD4525F9499	FASTA	572	65,136
	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

References

	« Hide 'large scale' referencesShow '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: 10907853] [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: 10819329] [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. , 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: 14593172] [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: 20023195] [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: 19914916] [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.
IPI	IPI00534039.
RefSeq	NP_566675.1. NM_113010.2.
UniGene	At.25787.
3D structure databases
HSSP	HSSP built from PDB template 1FMI based on UniProtKB Q9UKM7.
ProteinModelPortal	Q8H116.
SMR	Q8H116. Positions 85-538.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8H116. 1 interaction.
STRING	Q8H116.
Protein family/group databases
CAZy	GH47. Glycoside Hydrolase Family 47.
Proteomic databases
PRIDE	Q8H116.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G21160.1; AT3G21160.1; AT3G21160.
GeneID	821668.
GenomeReviews	Gene locus AT3G21160 in contig BA000014_GR.
KEGG	ath:AT3G21160.
NMPDR	fig|3702.1.peg.14347.
Organism-specific databases
TAIR	At3g21160.
Phylogenomic databases
InParanoid	Q8H116.
OMA	LLPAWDT.
PhylomeDB	Q8H116.
ProtClustDB	CLSN2914679.
Gene expression databases
Genevestigator	Q8H116.
Family and domain databases
InterPro	IPR001382. Glyco_hydro_47. [Graphical view]
Gene3D	G3DSA:1.50.10.50. Glyco_hydro_47. 1 hit.
KO	K01230.
PANTHER	PTHR11742. Glyco_hydro_47. 1 hit.
Pfam	PF01532. Glyco_hydro_47. 1 hit. [Graphical view]
PRINTS	PR00747. GLYHDRLASE47.
SUPFAM	SSF48225. Glyco_hydro_47. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MNS2_ARATH

Accession

Primary (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:	November 16, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program