GMAN2_ARATH
ID GMAN2_ARATH Reviewed; 1173 AA.
AC Q9LFR0; Q940T6;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Alpha-mannosidase 2 {ECO:0000303|PubMed:16460512};
DE EC=3.2.1.114 {ECO:0000269|PubMed:16460512};
DE AltName: Full=Golgi alpha-mannosidase II {ECO:0000303|PubMed:16460512};
DE Short=AMan II;
DE Short=AtGMII {ECO:0000303|PubMed:16460512};
DE Short=Man II;
DE AltName: Full=Protein hybrid glycosylation 1 {ECO:0000303|PubMed:18408158};
GN Name=GMII {ECO:0000303|PubMed:16460512};
GN Synonyms=HGL1 {ECO:0000303|PubMed:18408158};
GN OrderedLocusNames=At5g14950 {ECO:0000312|Araport:AT5G14950};
GN ORFNames=F2G14.70 {ECO:0000312|EMBL:CAC01814.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, PATHWAY, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=16460512; DOI=10.1111/j.1365-313x.2005.02648.x;
RA Strasser R., Schoberer J., Jin C., Glossl J., Mach L., Steinkellner H.;
RT "Molecular cloning and characterization of Arabidopsis thaliana Golgi
RT alpha-mannosidase II, a key enzyme in the formation of complex N-glycans in
RT plants.";
RL Plant J. 45:789-803(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18408158; DOI=10.1073/pnas.0800237105;
RA Kang J.S., Frank J., Kang C.H., Kajiura H., Vikram M., Ueda A., Kim S.,
RA Bahk J.D., Triplett B., Fujiyama K., Lee S.Y., von Schaewen A., Koiwa H.;
RT "Salt tolerance of Arabidopsis thaliana requires maturation of N-
RT glycosylated proteins in the Golgi apparatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5933-5938(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=21478158; DOI=10.1074/jbc.m110.196097;
RA Kaulfurst-Soboll H., Rips S., Koiwa H., Kajiura H., Fujiyama K.,
RA von Schaewen A.;
RT "Reduced immunogenicity of Arabidopsis hgl1 mutant N-glycans caused by
RT altered accessibility of xylose and core fucose epitopes.";
RL J. Biol. Chem. 286:22955-22964(2011).
RN [7]
RP INTERACTION WITH GALT1.
RX PubMed=23400704; DOI=10.1104/pp.112.210757;
RA Schoberer J., Liebminger E., Botchway S.W., Strasser R., Hawes C.;
RT "Time-resolved fluorescence imaging reveals differential interactions of N-
RT glycan processing enzymes across the Golgi stack in planta.";
RL Plant Physiol. 161:1737-1754(2013).
CC -!- FUNCTION: Catalyzes the first committed step in the biosynthesis of
CC complex N-glycans. It controls conversion of high mannose to complex N-
CC glycans; the final hydrolytic step in the N-glycan maturation pathway.
CC Converts GlcNAcMan(5)GlcNAc(2) (Man5Gn) into GlcNAcMan(3)GlcNAc(2)
CC (MGn) by sequential removal of two alpha1,6- and alpha1,3-linked
CC mannose residues from the alpha1,6-mannose branch of the substrate. To
CC a lesser extent, also able to cleave beta1,2-xylosylated Man5Gn-
CC glycopeptide (Man5GnX-GP) and pyridylaminated substrates Man5Gn-PA and
CC Man5GnX-PA, but not active toward Man5-glycopeptide (PubMed:16460512,
CC PubMed:21478158). Required for resistance to salt stress
CC (PubMed:18408158). {ECO:0000269|PubMed:16460512,
CC ECO:0000269|PubMed:18408158, ECO:0000269|PubMed:21478158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-
CC D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] =
CC 2 alpha-D-mannopyranose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-L-asparaginyl-[protein]; Xref=Rhea:RHEA:56052,
CC Rhea:RHEA-COMP:14368, Rhea:RHEA-COMP:14369, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28729, ChEBI:CHEBI:60615, ChEBI:CHEBI:60625;
CC EC=3.2.1.114; Evidence={ECO:0000269|PubMed:16460512};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16460512};
CC Note=Binds 1 zinc ion per subunit. Not sensitive to EDTA and not
CC significantly stimulated by cations such as Ca(2+), Co(2+), Mn(2+),
CC Ni(2+) or Zn(2+) (PubMed:16460512). {ECO:0000269|PubMed:16460512};
CC -!- ACTIVITY REGULATION: Inhibited by 1 mM Cu(2+) and by the class II
CC alpha-mannosidase inhibitor swainsonine. {ECO:0000269|PubMed:16460512}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:16460512, ECO:0000269|PubMed:21478158}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC GALT1 (PubMed:23400704). {ECO:0000250|UniProtKB:P28494,
CC ECO:0000269|PubMed:23400704}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16460512}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:16460512}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P28494}.
CC -!- DISRUPTION PHENOTYPE: Predominant presence of unprocessed hybrid N-
CC glycans (PubMed:16460512). Reduced levels of glycoprotein N-glycans
CC (PubMed:21478158). Increased sensitivity to salt stress
CC (PubMed:18408158). {ECO:0000269|PubMed:16460512,
CC ECO:0000269|PubMed:18408158, ECO:0000269|PubMed:21478158}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK96611.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ029214; AAY90120.1; -; mRNA.
DR EMBL; AL391146; CAC01814.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92095.1; -; Genomic_DNA.
DR EMBL; AY052707; AAK96611.1; ALT_INIT; mRNA.
DR EMBL; AF446883; AAL38616.1; -; mRNA.
DR PIR; T51440; T51440.
DR RefSeq; NP_196999.1; NM_121499.3.
DR AlphaFoldDB; Q9LFR0; -.
DR SMR; Q9LFR0; -.
DR STRING; 3702.AT5G14950.1; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR iPTMnet; Q9LFR0; -.
DR SwissPalm; Q9LFR0; -.
DR PaxDb; Q9LFR0; -.
DR PRIDE; Q9LFR0; -.
DR ProteomicsDB; 247369; -.
DR EnsemblPlants; AT5G14950.1; AT5G14950.1; AT5G14950.
DR GeneID; 831347; -.
DR Gramene; AT5G14950.1; AT5G14950.1; AT5G14950.
DR KEGG; ath:AT5G14950; -.
DR Araport; AT5G14950; -.
DR TAIR; locus:2147855; AT5G14950.
DR eggNOG; KOG1958; Eukaryota.
DR HOGENOM; CLU_004690_1_0_1; -.
DR InParanoid; Q9LFR0; -.
DR OMA; GEMEIMQ; -.
DR OrthoDB; 1101882at2759; -.
DR PhylomeDB; Q9LFR0; -.
DR BioCyc; ARA:AT5G14950-MON; -.
DR BioCyc; MetaCyc:AT5G14950-MON; -.
DR BRENDA; 3.2.1.114; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9LFR0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFR0; baseline and differential.
DR Genevisible; Q9LFR0; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000137; C:Golgi cis cisterna; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0004559; F:alpha-mannosidase activity; IDA:TAIR.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004572; F:mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:UniProtKB.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0006517; P:protein deglycosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:TAIR.
DR Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosidase; Golgi apparatus; Hydrolase;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..1173
FT /note="Alpha-mannosidase 2"
FT /id="PRO_0000432115"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..71
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..1173
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1098
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1173 AA; 134726 MW; C13CD004D8DE49F9 CRC64;
MPFSSYIGNS RRSSTGGGTG GWGQSLLPTA LSKSKLAINR KPRKRTLVVN FIFANFFVIA
LTVSLLFFLL TLFHFGVPGP ISSRFLTSRS NRIVKPRKNI NRRPLNDSNS GAVVDITTKD
LYDRIEFLDT DGGPWKQGWR VTYKDDEWEK EKLKIFVVPH SHNDPGWKLT VEEYYQRQSR
HILDTIVETL SKDSRRKFIW EEMSYLERWW RDASPNKQEA LTKLVKDGQL EIVGGGWVMN
DEANSHYFAI IEQIAEGNMW LNDTIGVIPK NSWAIDPFGY SSTMAYLLRR MGFENMLIQR
THYELKKDLA QHKNLEYIWR QSWDAMETTD IFVHMMPFYS YDIPHTCGPE PAICCQFDFA
RMRGFKYELC PWGKHPVETT LENVQERALK LLDQYRKKST LYRTNTLLIP LGDDFRYISI
DEAEAQFRNY QMLFDHINSN PSLNAEAKFG TLEDYFRTVR EEADRVNYSR PGEVGSGQVV
GFPSLSGDFF TYADRQQDYW SGYYVSRPFF KAVDRVLEHT LRGAEIMMSF LLGYCHRIQC
EKFPTSFTYK LTAARRNLAL FQHHDGVTGT AKDYVVQDYG TRMHTSLQDL QIFMSKAIEV
LLGIRHEKEK SDQSPSFFEA EQMRSKYDAR PVHKPIAARE GNSHTVILFN PSEQTREEVV
TVVVNRAEIS VLDSNWTCVP SQISPEVQHD DTKLFTGRHR LYWKASIPAL GLRTYFIANG
NVECEKATPS KLKYASEFDP FPCPPPYSCS KLDNDVTEIR NEHQTLVFDV KNGSLRKIVH
RNGSETVVGE EIGMYSSPES GAYLFKPDGE AQPIVQPDGH VVTSEGLLVQ EVFSYPKTKW
EKSPLSQKTR LYTGGNTLQD QVVEIEYHVE LLGNDFDDRE LIVRYKTDVD NKKVFYSDLN
GFQMSRRETY DKIPLQGNYY PMPSLAFIQG SNGQRFSVHS RQSLGVASLK EGWLEIMLDR
RLVRDDGRGL GQGVMDNRAM TVVFHLLAES NISQADPASN TNPRNPSLLS HLIGAHLNYP
INTFIAKKPQ DISVRVPQYG SFAPLAKPLP CDLHIVNFKV PRPSKYSQQL EEDKPRFALI
LNRRAWDSAY CHKGRQVNCT SMANEPVNFS DMFKDLAASK VKPTSLNLLQ EDMEILGYDD
QELPRDSSQP REGRVSISPM EIRAYKLELR PHK
