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Protein

Alpha-mannosidase 2

Gene

GMII

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -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

Man5GlcNAc3-[protein] + 2 H2O = Man3GlcNAc3-[protein] + 2 alpha-D-mannopyranose.1 Publication

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)DescriptionActionsGraphical viewLength
Metal bindingi162ZincBy similarity1
Metal bindingi164ZincBy similarity1
Active sitei276NucleophileBy similarity1
Metal bindingi276ZincBy similarity1
Metal bindingi564ZincBy similarity1

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

Keywordsi

Molecular functionGlycosidase, Hydrolase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT5G14950-MONOMER
MetaCyc: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

AraportiAT5G14950
TAIRilocus:2147855 AT5G14950

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 50CytoplasmicCuratedAdd BLAST50
Transmembranei51 – 71Helical; Signal-anchorSequence analysisAdd BLAST21
Topological domaini72 – 1173LumenalCuratedAdd BLAST1102

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004321151 – 1173Alpha-mannosidase 2Add BLAST1173

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi106N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi262N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi467N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi675N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi772N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi782N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi991N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi1098N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi1108N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

Post-translational modificationi

Glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9LFR0

PTM databases

iPTMnetiQ9LFR0
SwissPalmiQ9LFR0

Expressioni

Gene expression databases

ExpressionAtlasiQ9LFR0 baseline and differential
GenevisibleiQ9LFR0 AT

Interactioni

Subunit structurei

Homodimer; disulfide-linked (By similarity). Interacts with GALT1 (PubMed:23400704).By similarity1 Publication

Protein-protein interaction databases

STRINGi3702.AT5G14950.1

Structurei

3D structure databases

ProteinModelPortaliQ9LFR0
SMRiQ9LFR0
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
OMAiWRQNWDL
OrthoDBiEOG093600KX
PhylomeDBiQ9LFR0

Family and domain databases

Gene3Di1.20.1270.50, 1 hit
2.60.40.1180, 1 hit
3.20.110.10, 1 hit
InterProiView protein in InterPro
IPR011013 Gal_mutarotase_sf_dom
IPR011330 Glyco_hydro/deAcase_b/a-brl
IPR011682 Glyco_hydro_38_C
IPR015341 Glyco_hydro_38_cen
IPR037094 Glyco_hydro_38_cen_sf
IPR000602 Glyco_hydro_38_N
IPR027291 Glyco_hydro_38_N_sf
IPR028995 Glyco_hydro_57/38_cen_sf
IPR013780 Glyco_hydro_b
PfamiView protein in Pfam
PF09261 Alpha-mann_mid, 1 hit
PF01074 Glyco_hydro_38, 1 hit
PF07748 Glyco_hydro_38C, 1 hit
SMARTiView protein in SMART
SM00872 Alpha-mann_mid, 1 hit
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_121499.3
UniGeneiAt.22883
At.68063

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiGMAN2_ARATH
AccessioniPrimary (citable) accession number: Q9LFR0
Secondary accession number(s): Q940T6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 4, 2015
Last sequence update: October 1, 2000
Last modified: May 23, 2018
This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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