MANA1_ARATH
ID MANA1_ARATH Reviewed; 1019 AA.
AC P94078; Q96239;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Alpha-mannosidase At3g26720 {ECO:0000305};
DE EC=3.2.1.24 {ECO:0000269|PubMed:16233119};
DE Flags: Precursor;
GN OrderedLocusNames=At3g26720 {ECO:0000312|Araport:AT3G26720};
GN ORFNames=MLJ15.11 {ECO:0000312|EMBL:BAB01735.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8932388; DOI=10.1093/nar/24.21.4313;
RA Quigley F., Dao P., Cottet A., Mache R.;
RT "Sequence analysis of an 81 kb contig from Arabidopsis thaliana chromosome
RT III.";
RL Nucleic Acids Res. 24:4313-4318(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 CATALYTIC ACTIVITY.
RX PubMed=16233119; DOI=10.1263/jbb.92.401;
RA Fujiyama K., Kira Y., Iizuka M., Kimura Y., Seki T.;
RT "Identification of putative gene encoded on ORF16 of the 81 kb contig of
RT Arabidopsis thaliana chromosome III as alpha-mannosidase.";
RL J. Biosci. Bioeng. 92:401-404(2001).
CC -!- FUNCTION: Liberates mannose from p-nitrophenyl-alpha-D-mannoside in
CC vitro. {ECO:0000269|PubMed:16233119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC in alpha-D-mannosides.; EC=3.2.1.24;
CC Evidence={ECO:0000269|PubMed:16233119};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q29451};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q29451};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q29451}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=P94078-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR EMBL; X98130; CAA66821.1; -; Genomic_DNA.
DR EMBL; Y11767; CAA72432.1; -; mRNA.
DR EMBL; AB026648; BAB01735.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77203.1; -; Genomic_DNA.
DR EMBL; AY039536; AAK62592.1; -; mRNA.
DR EMBL; AY113006; AAM47314.1; -; mRNA.
DR RefSeq; NP_189306.1; NM_113583.4. [P94078-1]
DR AlphaFoldDB; P94078; -.
DR SMR; P94078; -.
DR STRING; 3702.AT3G26720.1; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR PaxDb; P94078; -.
DR PRIDE; P94078; -.
DR ProteomicsDB; 238582; -. [P94078-1]
DR EnsemblPlants; AT3G26720.1; AT3G26720.1; AT3G26720. [P94078-1]
DR GeneID; 822284; -.
DR Gramene; AT3G26720.1; AT3G26720.1; AT3G26720. [P94078-1]
DR KEGG; ath:AT3G26720; -.
DR Araport; AT3G26720; -.
DR TAIR; locus:2090817; AT3G26720.
DR eggNOG; KOG1959; Eukaryota.
DR InParanoid; P94078; -.
DR OMA; SEAACGY; -.
DR OrthoDB; 201312at2759; -.
DR PhylomeDB; P94078; -.
DR BioCyc; ARA:AT3G26720-MON; -.
DR PRO; PR:P94078; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P94078; baseline and differential.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004559; F:alpha-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR Gene3D; 1.20.1270.50; -; 2.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041147; GH38_C.
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; PF17677; Glyco_hydro38C2; 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 Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Metal-binding; Reference proteome; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1019
FT /note="Alpha-mannosidase At3g26720"
FT /evidence="ECO:0000255"
FT /id="PRO_5006739397"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 466..474
FT /evidence="ECO:0000250|UniProtKB:C0HJB3"
FT DISULFID 824..829
FT /evidence="ECO:0000250|UniProtKB:C0HJB3"
SQ SEQUENCE 1019 AA; 115220 MW; 4F764F2359F9FBEC CRC64;
MAVKCFSLYL ILAAIVIGGV TSEYIEYNTK PRIVPEKINV HLVPHSHDDV GWLKTVDQYY
VGSNNSIRGA CVQNVLDSVI ASLLDDENRK FIYVEMAFFQ RWWRQQSNAK KVKVKKLVDS
GQLEFINGGM CMHDEATPHY IDMIDQTTLG HQFIKTEFGQ VPRVGWQIDP FGHSAVQAYL
LGAEFGFDSL FFARIDYQDR AKRLREKTLE VIWQGSKSLG SSSQIFTGVF PRHYDPPEGF
TFEINDVSAP IQDDPLLFDY NVQERVNDFV AAALAQVNVT RTNHIMWLMG TDFRYQYAYS
WFRQIDKFIH YVNKDGRLNV LYSTPSIYTD AKYAANESWP LKTDDFFPYA DKPNAYWTGY
FTSRPAFKKY VRDLSGYYLA ARQLEFLRGR DSSGPTTDML ADALAIAQHH DAVSGTQRQH
VAADYALRLS MGYLQAEKLV ASSLSFLSAA KSSTEKKNPG TKFQQCPLLN ISYCPASEAR
LLSGKSLVVV VYNSLGWKRE EVVRVPVSSE NVIVKDASGK EVVFQLLPLS EIALRIRNEY
VKAYLGRSPR DTAKHVLAFT ASVPPLGFSS YVISDTGRTA RGLSASYVTS GSMNQNVEVG
QGNLKLRYSE EGVKITRHLS TKNQVTAEQS YAYYIGSNGT DKDPQASGAY VFRPDGVLPI
KSKEEAQLTI VQGPLFDEVH QELNSWISQI TRVYKGKNHA EIEFTIGPIP ADDGISKEII
TKLTTTMKTN GTFYTDSNGR DFIKRIRDFR TDWDLQVYQP VAGNYYPLNL GIYMQDKTSE
LSVLVDRAVG GSSLENGQIE LMLHRRMQHD DIRGVGEILN ETVCLPEGCK GLTIQGKFYV
QIDKPGDGAK WRRTFGQEIY SPLLIAFTEQ EGDSWINSHK TTFSAFEPSY SLPKNVALLT
LQELENGEVL LRLAHLFEVG EDSEYSVMAK VELKKLFHNK KIREVKETSL SGNQEKAEME
KRRLIWKVEG SAGEEVKRGE AVDAEKLVVE LVPMEIRTLL IKFDDQIEMV GDKEQQHRL
