MNS5_ARATH
ID MNS5_ARATH Reviewed; 574 AA.
AC Q9SXC9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Alpha-mannosidase I MNS5;
DE EC=3.2.1.- {ECO:0000269|PubMed:24737672};
GN Name=MNS5; OrderedLocusNames=At1g27520; ORFNames=T17H3.2;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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).
RN [4]
RP IDENTIFICATION.
RX PubMed=20023195; DOI=10.1105/tpc.109.072363;
RA Liebminger E., Huttner S., Vavra U., Fischl R., Schoberer J., Grass J.,
RA Blaukopf C., Seifert G.J., Altmann F., Mach L., Strasser R.;
RT "Class I alpha-mannosidases are required for N-glycan processing and root
RT development in Arabidopsis thaliana.";
RL Plant Cell 21:3850-3867(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-388.
RX PubMed=24737672; DOI=10.1105/tpc.114.123216;
RA Huettner S., Veit C., Vavra U., Schoberer J., Liebminger E., Maresch D.,
RA Grass J., Altmann F., Mach L., Strasser R.;
RT "Arabidopsis class I alpha-mannosidases MNS4 and MNS5 are involved in
RT endoplasmic reticulum-associated degradation of misfolded glycoproteins.";
RL Plant Cell 26:1712-1728(2014).
CC -!- FUNCTION: Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N-
CC glycans with a terminal alpha-1,6-linked Man residue in the C-branch.
CC Functions in the formation of unique N-glycan structures that are
CC specifically recognized by components of the endoplasmic reticulum-
CC associated degradation (ERAD) machinery, which leads to the degradation
CC of misfolded glycoproteins. Most likely generates N-glycan signal on
CC misfolded glycoproteins that is subsequently recognized by OS9.
CC Required for ERAD of the heavily glycosylated and misfolded BRI1
CC variants BRI1-5 and BRI1-9. Does not seem to play role in N-glycan
CC processing of correctly folded proteins destined for secretion.
CC {ECO:0000269|PubMed:24737672}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P45700};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24737672}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR EMBL; AC005916; AAD45990.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30841.1; -; Genomic_DNA.
DR EMBL; AY056382; AAL08238.1; -; mRNA.
DR PIR; C86400; C86400.
DR RefSeq; NP_564288.1; NM_102516.4.
DR AlphaFoldDB; Q9SXC9; -.
DR SMR; Q9SXC9; -.
DR STRING; 3702.AT1G27520.1; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PaxDb; Q9SXC9; -.
DR PRIDE; Q9SXC9; -.
DR ProteomicsDB; 238256; -.
DR EnsemblPlants; AT1G27520.1; AT1G27520.1; AT1G27520.
DR GeneID; 839643; -.
DR Gramene; AT1G27520.1; AT1G27520.1; AT1G27520.
DR KEGG; ath:AT1G27520; -.
DR Araport; AT1G27520; -.
DR TAIR; locus:2196874; AT1G27520.
DR eggNOG; KOG2429; Eukaryota.
DR HOGENOM; CLU_003818_5_6_1; -.
DR InParanoid; Q9SXC9; -.
DR OMA; NWTFVKD; -.
DR OrthoDB; 434316at2759; -.
DR PhylomeDB; Q9SXC9; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9SXC9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SXC9; baseline and differential.
DR Genevisible; Q9SXC9; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004559; F:alpha-mannosidase activity; IMP:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; IBA:GO_Central.
DR GO; GO:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:TAIR.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR044674; EDEM1/2/3.
DR InterPro; IPR001382; Glyco_hydro_47.
DR InterPro; IPR036026; Seven-hairpin_glycosidases.
DR PANTHER; PTHR45679; PTHR45679; 1.
DR Pfam; PF01532; Glyco_hydro_47; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF48225; SSF48225; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..574
FT /note="Alpha-mannosidase I MNS5"
FT /id="PRO_0000397937"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..574
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 274
FT /evidence="ECO:0000250"
FT ACT_SITE 367
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT ACT_SITE 388
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 388
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24737672"
SQ SEQUENCE 574 AA; 65708 MW; 4ACC456DE487EA93 CRC64;
MSCPIHPRRL FLCLLISLTF FVVDPSSQHI EVKKKQMREK VREMFYHAYD NYMTYAFPHD
ELKPLTKSFT DSLSELGNLK LEHLPTDYNG SAVTLVESLS SLAILGNSTE FEKGVLWLSE
NLTFDIDARV NLFECNIRVL GGLISAHLLA IDPNNRLIQG SYNNQLLRLA EDLGKRFLPA
FETPTGLPYA WINLKNGVME NETTETSTSG CGSLVLEMGA LSRLTGDPRF ESAALRALRQ
LWRMRSSLDL LGTTLDVVTG EWIEYSSSIG AGVDSFYEYL LKAYILFGKE DYWRMFHSAY
LASQKYFRHG PWYHEANMWS GKPTYWQLTS LQAFWPGLQV LVGDIAAANS SHREFFHVWE
KFGVLPERYL LDHQIIHPTM KYYPLRPELA ESTFYLYQAT KDPWYLDVGE SMVKSLNLYT
KVPGGFASVR DVTTMQLEDH QHSFFLAETC KYLYLLFDDS FVAKRNYIFT TEGHPIQVVS
SWHEKLPETY FSGNWTLSKS GAWESRASAL SLQVCPLISL NSRHPEQQRE SACHVLDEQI
NHKCWSNKEC GVDATTCRLR TCSGVGYCGL WNPL
