MANA2_ARATH
ID MANA2_ARATH Reviewed; 1024 AA.
AC Q8LPJ3; Q3E9H8; Q9FFX7;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable alpha-mannosidase At5g13980 {ECO:0000305};
DE EC=3.2.1.24 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At5g13980 {ECO:0000312|Araport:AT5G13980};
GN ORFNames=MAC12.5 {ECO:0000312|EMBL:BAB11126.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
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 [3]
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).
CC -!- FUNCTION: Liberates mannose from p-nitrophenyl-alpha-D-mannoside in
CC vitro. {ECO:0000250|UniProtKB:P94078}.
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:0000250|UniProtKB:P94078};
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=Q8LPJ3-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11126.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005230; BAB11126.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91968.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91969.1; -; Genomic_DNA.
DR EMBL; AY099704; AAM20555.1; -; mRNA.
DR EMBL; BT000301; AAN15620.1; -; mRNA.
DR RefSeq; NP_196902.2; NM_121401.5. [Q8LPJ3-1]
DR RefSeq; NP_851037.2; NM_180706.3. [Q8LPJ3-1]
DR AlphaFoldDB; Q8LPJ3; -.
DR SMR; Q8LPJ3; -.
DR STRING; 3702.AT5G13980.2; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR MetOSite; Q8LPJ3; -.
DR PaxDb; Q8LPJ3; -.
DR PRIDE; Q8LPJ3; -.
DR ProteomicsDB; 238280; -. [Q8LPJ3-1]
DR EnsemblPlants; AT5G13980.1; AT5G13980.1; AT5G13980. [Q8LPJ3-1]
DR EnsemblPlants; AT5G13980.2; AT5G13980.2; AT5G13980. [Q8LPJ3-1]
DR GeneID; 831246; -.
DR Gramene; AT5G13980.1; AT5G13980.1; AT5G13980. [Q8LPJ3-1]
DR Gramene; AT5G13980.2; AT5G13980.2; AT5G13980. [Q8LPJ3-1]
DR KEGG; ath:AT5G13980; -.
DR Araport; AT5G13980; -.
DR TAIR; locus:2159143; AT5G13980.
DR eggNOG; KOG1959; Eukaryota.
DR InParanoid; Q8LPJ3; -.
DR OrthoDB; 201312at2759; -.
DR PhylomeDB; Q8LPJ3; -.
DR BioCyc; ARA:AT5G13980-MON; -.
DR PRO; PR:Q8LPJ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LPJ3; baseline and differential.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Metal-binding; Reference proteome; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1024
FT /note="Probable alpha-mannosidase At5g13980"
FT /evidence="ECO:0000255"
FT /id="PRO_5006749971"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q29451"
FT BINDING 168
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 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 63
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 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 461..469
FT /evidence="ECO:0000250|UniProtKB:C0HJB3"
FT DISULFID 827..832
FT /evidence="ECO:0000250|UniProtKB:C0HJB3"
SQ SEQUENCE 1024 AA; 115902 MW; 83E0BA831BFC31D3 CRC64;
MDLAKFLCWI VLLLGISLVE SRYMVYNTSH TIVPGKLNVH VVPHSHDDVG WLKTVDQYYV
GSNNSIQVAC VQNVLDSIVP ALLADKNRKF IYVEQAFFQR WWNEQSEEIK RIVKELIHSG
QLELINGGMC MHDEAAPHYI DMIDQTTLGH RFIIREFNVT PRIGWQIDPF GHSAVQAYLL
GAEVGFDSVF FGRIDYQDRE KRYKEKTLEV IWRGSKSLGS SSQIFAGAFP TNYEPPPGGF
YYEITDDSPV VQDDPDLFDY NVQERVNAFV AAALDQANIT RINHIMFTMG TDFRYQYAHT
WYRQMDKLIH YVNLDGRVNA FYSTPSIYTD AKHAANEAWP LKTEDYFPYA DRINAYWTGY
FTSRPALKRY VRVMSAYYLA ARQLEFFKGR SQKGPNTDSL ADALAIAQHH DAVSGTSKQH
VANDYAKRLA IGYVEAESVV ATSLAHLTKV DPTLNPTFQQ CLLLNISYCP SSEVNLSDGK
SLIVLAYNPL GWKRVDIVRL PVVGGDVSVH DSEGHEVESQ LVPFTDEYVA LRKYHVEAYL
GQSPTQVPKY WLVFSVTVPP LGFTTYTIST AKKTDGYSSK SYVSNILKGE QSIINIGHGH
LKLSFSTDQG TAINYVNGRT SMTEPVKQTF SYYSAYNGSN DKEPLIPQNS GAYVFRPNGT
FPINPEGQVP LTVIHGPLVD EVHQQINPWI SQITRVYKGK EHVEVEFIVG NIPIDDGIGK
EVVTQISSSL KSNKTFYTDS SGRDYIKRIR DYRSDWKLDV NQPIAGNYYP INHGIYLQDS
KKEFSVMVDR AFGGSSIVDG QVELMLHRRL LLDDSRGVAE NLNETVCVQD KCTGLTIQGK
YYYRIDPYGE GAKWRRTFGQ EIYSPLLLAF AQQDDGKPMS FGAASFSGID PSYSLPDNVA
LLTLQELDDG NVLLRLAHLY EVEEDKELSG VASVELKKLF PGKKIGKLTE MSLSANQERS
TMEKKRLVWK VEGEGSYGEE KKAKRGREID PRKLEMELYP MEIRTVLIHL ELPSSHSRIN
RFDA
