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Protein

Alpha-mannosidase 2

Gene

GMII

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway. Converts GlcNAcMan5GlcNAc2 (Man5Gn) into GlcNAcMan3GlcNAc2 (MGn) by sequential removal of two alpha1,6- and alpha1,3-linked mannose residues from the alpha1,6-mannose branch of the substrate. To a lesser extent, also able to cleave beta1,2-xylosylated Man5Gn-glycopeptide (Man5GnX-GP) and pyridylaminated substrates Man5Gn-PA and Man5GnX-PA, but not active toward Man5-glycopeptide (PubMed:16460512, PubMed:21478158). Required for resistance to salt stress (PubMed:18408158).3 Publications

Catalytic activityi

Hydrolysis of the terminal (1->3)- and (1->6)-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3.2 Publications

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit. Not sensitive to EDTA and not significantly stimulated by cations such as Ca2+, Co2+, Mn2+, Ni2+ or Zn2+ (PubMed:16460512).1 Publication

Enzyme regulationi

Inhibited by 1 mM Cu2+ and by the class II alpha-mannosidase inhibitor swainsonine.1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi162 – 1621ZincBy similarity
Metal bindingi164 – 1641ZincBy similarity
Active sitei276 – 2761NucleophileBy similarity
Metal bindingi276 – 2761ZincBy similarity
Metal bindingi564 – 5641ZincBy similarity

GO - Molecular functioni

GO - Biological processi

  • hyperosmotic salinity response Source: UniProtKB
  • mannose metabolic process Source: GO_Central
  • N-glycan processing Source: GO_Central
  • protein deglycosylation Source: GO_Central
  • protein N-linked glycosylation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT5G14950-MONOMER.
BRENDAi3.2.1.114. 399.
ReactomeiR-ATH-975578. Reactions specific to the complex N-glycan synthesis pathway.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-mannosidase 21 Publication (EC:3.2.1.1141 Publication)
Alternative name(s):
Golgi alpha-mannosidase II1 Publication
Short name:
AMan II
Short name:
AtGMII1 Publication
Short name:
Man II
Protein hybrid glycosylation 11 Publication
Gene namesi
Name:GMII1 Publication
Synonyms:HGL11 Publication
Ordered Locus Names:At5g14950Imported
ORF Names:F2G14.70Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G14950.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5050CytoplasmicCuratedAdd
BLAST
Transmembranei51 – 7121Helical; Signal-anchorSequence analysisAdd
BLAST
Topological domaini72 – 11731102LumenalCuratedAdd
BLAST

GO - Cellular componenti

  • endosome Source: TAIR
  • Golgi apparatus Source: TAIR
  • Golgi membrane Source: GO_Central
  • integral component of membrane Source: UniProtKB-KW
  • trans-Golgi network Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Predominant presence of unprocessed hybrid N-glycans (PubMed:16460512). Reduced levels of glycoprotein N-glycans (PubMed:21478158). Increased sensitivity to salt stress (PubMed:18408158).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11731173Alpha-mannosidase 2PRO_0000432115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi262 – 2621N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi467 – 4671N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi675 – 6751N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi772 – 7721N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi782 – 7821N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi991 – 9911N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi1098 – 10981N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi1108 – 11081N-linked (GlcNAc...)PROSITE-ProRule annotation

Post-translational modificationi

Glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9LFR0.
PRIDEiQ9LFR0.

PTM databases

iPTMnetiQ9LFR0.
SwissPalmiQ9LFR0.

Expressioni

Gene expression databases

GenevisibleiQ9LFR0. AT.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Protein-protein interaction databases

STRINGi3702.AT5G14950.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LFR0.
SMRiQ9LFR0. Positions 114-1047.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 38 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1958. Eukaryota.
ENOG410XQMZ. LUCA.
HOGENOMiHOG000293253.
KOiK01231.
OMAiASLKDGW.
OrthoDBiEOG093600KX.
PhylomeDBiQ9LFR0.

Family and domain databases

Gene3Di1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
IPR013780. Glyco_hydro_b.
[Graphical view]
PfamiPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTiSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMiSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9LFR0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFSSYIGNS RRSSTGGGTG GWGQSLLPTA LSKSKLAINR KPRKRTLVVN
60 70 80 90 100
FIFANFFVIA LTVSLLFFLL TLFHFGVPGP ISSRFLTSRS NRIVKPRKNI
110 120 130 140 150
NRRPLNDSNS GAVVDITTKD LYDRIEFLDT DGGPWKQGWR VTYKDDEWEK
160 170 180 190 200
EKLKIFVVPH SHNDPGWKLT VEEYYQRQSR HILDTIVETL SKDSRRKFIW
210 220 230 240 250
EEMSYLERWW RDASPNKQEA LTKLVKDGQL EIVGGGWVMN DEANSHYFAI
260 270 280 290 300
IEQIAEGNMW LNDTIGVIPK NSWAIDPFGY SSTMAYLLRR MGFENMLIQR
310 320 330 340 350
THYELKKDLA QHKNLEYIWR QSWDAMETTD IFVHMMPFYS YDIPHTCGPE
360 370 380 390 400
PAICCQFDFA RMRGFKYELC PWGKHPVETT LENVQERALK LLDQYRKKST
410 420 430 440 450
LYRTNTLLIP LGDDFRYISI DEAEAQFRNY QMLFDHINSN PSLNAEAKFG
460 470 480 490 500
TLEDYFRTVR EEADRVNYSR PGEVGSGQVV GFPSLSGDFF TYADRQQDYW
510 520 530 540 550
SGYYVSRPFF KAVDRVLEHT LRGAEIMMSF LLGYCHRIQC EKFPTSFTYK
560 570 580 590 600
LTAARRNLAL FQHHDGVTGT AKDYVVQDYG TRMHTSLQDL QIFMSKAIEV
610 620 630 640 650
LLGIRHEKEK SDQSPSFFEA EQMRSKYDAR PVHKPIAARE GNSHTVILFN
660 670 680 690 700
PSEQTREEVV TVVVNRAEIS VLDSNWTCVP SQISPEVQHD DTKLFTGRHR
710 720 730 740 750
LYWKASIPAL GLRTYFIANG NVECEKATPS KLKYASEFDP FPCPPPYSCS
760 770 780 790 800
KLDNDVTEIR NEHQTLVFDV KNGSLRKIVH RNGSETVVGE EIGMYSSPES
810 820 830 840 850
GAYLFKPDGE AQPIVQPDGH VVTSEGLLVQ EVFSYPKTKW EKSPLSQKTR
860 870 880 890 900
LYTGGNTLQD QVVEIEYHVE LLGNDFDDRE LIVRYKTDVD NKKVFYSDLN
910 920 930 940 950
GFQMSRRETY DKIPLQGNYY PMPSLAFIQG SNGQRFSVHS RQSLGVASLK
960 970 980 990 1000
EGWLEIMLDR RLVRDDGRGL GQGVMDNRAM TVVFHLLAES NISQADPASN
1010 1020 1030 1040 1050
TNPRNPSLLS HLIGAHLNYP INTFIAKKPQ DISVRVPQYG SFAPLAKPLP
1060 1070 1080 1090 1100
CDLHIVNFKV PRPSKYSQQL EEDKPRFALI LNRRAWDSAY CHKGRQVNCT
1110 1120 1130 1140 1150
SMANEPVNFS DMFKDLAASK VKPTSLNLLQ EDMEILGYDD QELPRDSSQP
1160 1170
REGRVSISPM EIRAYKLELR PHK
Length:1,173
Mass (Da):134,726
Last modified:October 1, 2000 - v1
Checksum:iC13CD004D8DE49F9
GO

Sequence cautioni

The sequence AAK96611 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ029214 mRNA. Translation: AAY90120.1.
AL391146 Genomic DNA. Translation: CAC01814.1.
CP002688 Genomic DNA. Translation: AED92095.1.
AY052707 mRNA. Translation: AAK96611.1. Different initiation.
AF446883 mRNA. Translation: AAL38616.1.
PIRiT51440.
RefSeqiNP_196999.1. NM_121499.2.
UniGeneiAt.22883.
At.68063.

Genome annotation databases

EnsemblPlantsiAT5G14950.1; AT5G14950.1; AT5G14950.
GeneIDi831347.
GrameneiAT5G14950.1; AT5G14950.1; AT5G14950.
KEGGiath:AT5G14950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ029214 mRNA. Translation: AAY90120.1.
AL391146 Genomic DNA. Translation: CAC01814.1.
CP002688 Genomic DNA. Translation: AED92095.1.
AY052707 mRNA. Translation: AAK96611.1. Different initiation.
AF446883 mRNA. Translation: AAL38616.1.
PIRiT51440.
RefSeqiNP_196999.1. NM_121499.2.
UniGeneiAt.22883.
At.68063.

3D structure databases

ProteinModelPortaliQ9LFR0.
SMRiQ9LFR0. Positions 114-1047.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G14950.1.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

PTM databases

iPTMnetiQ9LFR0.
SwissPalmiQ9LFR0.

Proteomic databases

PaxDbiQ9LFR0.
PRIDEiQ9LFR0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G14950.1; AT5G14950.1; AT5G14950.
GeneIDi831347.
GrameneiAT5G14950.1; AT5G14950.1; AT5G14950.
KEGGiath:AT5G14950.

Organism-specific databases

TAIRiAT5G14950.

Phylogenomic databases

eggNOGiKOG1958. Eukaryota.
ENOG410XQMZ. LUCA.
HOGENOMiHOG000293253.
KOiK01231.
OMAiASLKDGW.
OrthoDBiEOG093600KX.
PhylomeDBiQ9LFR0.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciARA:AT5G14950-MONOMER.
BRENDAi3.2.1.114. 399.
ReactomeiR-ATH-975578. Reactions specific to the complex N-glycan synthesis pathway.

Miscellaneous databases

PROiQ9LFR0.

Gene expression databases

GenevisibleiQ9LFR0. AT.

Family and domain databases

Gene3Di1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
IPR013780. Glyco_hydro_b.
[Graphical view]
PfamiPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTiSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMiSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGMAN2_ARATH
AccessioniPrimary (citable) accession number: Q9LFR0
Secondary accession number(s): Q940T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 4, 2015
Last sequence update: October 1, 2000
Last modified: September 7, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.