PSL5_ARATH
ID PSL5_ARATH Reviewed; 921 AA.
AC Q9FN05;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Probable glucan 1,3-alpha-glucosidase;
DE EC=3.2.1.84;
DE AltName: Full=Glucosidase II subunit alpha;
DE AltName: Full=Protein PRIORITY IN SWEET LIFE 5;
DE AltName: Full=Protein RADIAL SWELLING 3;
DE Flags: Precursor;
GN Name=PSL5; Synonyms=RSW3; OrderedLocusNames=At5g63840; ORFNames=MGI19.5;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP SER-599.
RX PubMed=12492837; DOI=10.1046/j.1365-313x.2002.01483.x;
RA Burn J.E., Hurley U.A., Birch R.J., Arioli T., Cork A., Williamson R.E.;
RT "The cellulose-deficient Arabidopsis mutant rsw3 is defective in a gene
RT encoding a putative glucosidase II, an enzyme processing N-glycans during
RT ER quality control.";
RL Plant J. 32:949-960(2002).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF SER-517.
RX PubMed=20007779; DOI=10.1073/pnas.0907711106;
RA Lu X., Tintor N., Mentzel T., Kombrink E., Boller T., Robatzek S.,
RA Schulze-Lefert P., Saijo Y.;
RT "Uncoupling of sustained MAMP receptor signaling from early outputs in an
RT Arabidopsis endoplasmic reticulum glucosidase II allele.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:22522-22527(2009).
CC -!- FUNCTION: Cleaves sequentially the 2 innermost alpha-1,3-linked glucose
CC residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of
CC immature glycoproteins (By similarity). Essential for stable
CC accumulation of the receptor EFR that determines the specific
CC perception of bacterial elongation factor Tu (EF-Tu), a potent elicitor
CC of the defense response to pathogen-associated molecular patterns
CC (PAMPs). Required for sustained activation of EFR-mediated signaling,
CC but not receptor FLS2-mediated signaling elicited by the bacterial
CC flagellin flg22. {ECO:0000250, ECO:0000269|PubMed:12492837,
CC ECO:0000269|PubMed:20007779}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal (1->3)-alpha-D-glucosidic links in
CC (1->3)-alpha-D-glucans.; EC=3.2.1.84;
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC -!- SUBUNIT: Heterodimer of a catalytic alpha subunit (PSL5) and a beta
CC subunit (PSL4). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, leaf blades,
CC mature stems, cauline leaves, flower buds, flowers and siliques.
CC {ECO:0000269|PubMed:12492837}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (permissive temperature of 21 degrees Celsius), but mutant
CC plants have a temperature-sensitive phenotype (when transferred to 30
CC degrees Celsius) showing radially swollen roots and reduction in
CC cellulose production. {ECO:0000269|PubMed:12492837}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK226927; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB007646; BAB11032.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97803.1; -; Genomic_DNA.
DR EMBL; AK226927; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_201189.1; NM_125779.3.
DR AlphaFoldDB; Q9FN05; -.
DR SMR; Q9FN05; -.
DR BioGRID; 21746; 7.
DR STRING; 3702.AT5G63840.1; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR iPTMnet; Q9FN05; -.
DR PaxDb; Q9FN05; -.
DR PRIDE; Q9FN05; -.
DR EnsemblPlants; AT5G63840.1; AT5G63840.1; AT5G63840.
DR GeneID; 836504; -.
DR Gramene; AT5G63840.1; AT5G63840.1; AT5G63840.
DR KEGG; ath:AT5G63840; -.
DR Araport; AT5G63840; -.
DR TAIR; locus:2163976; AT5G63840.
DR eggNOG; KOG1066; Eukaryota.
DR HOGENOM; CLU_000631_7_0_1; -.
DR InParanoid; Q9FN05; -.
DR OMA; QAGIWYP; -.
DR PhylomeDB; Q9FN05; -.
DR BRENDA; 3.2.1.207; 399.
DR UniPathway; UPA00957; -.
DR PRO; PR:Q9FN05; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN05; baseline and differential.
DR Genevisible; Q9FN05; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0090599; F:alpha-glucosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; IGI:TAIR.
DR GO; GO:0015926; F:glucosidase activity; IMP:TAIR.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0006491; P:N-glycan processing; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase; Plant defense;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..921
FT /note="Probable glucan 1,3-alpha-glucosidase"
FT /id="PRO_0000425975"
FT ACT_SITE 512
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 515
FT /evidence="ECO:0000250"
FT ACT_SITE 588
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 517
FT /note="S->F: In psl5-1; Compromised defense response
FT induced by the bacterial elicitor elongation factor Tu (EF-
FT Tu)."
FT /evidence="ECO:0000269|PubMed:20007779"
FT MUTAGEN 599
FT /note="S->F: In rsw3; temperature-sensitive radial swelling
FT of roots and reduction in cellulose production."
FT /evidence="ECO:0000269|PubMed:12492837"
SQ SEQUENCE 921 AA; 104275 MW; C0BA0808C6FC27B6 CRC64;
MRSLLFVLSL ICFCSQTALS WKKEEFRSCD QTPFCKRARS RTPGACSLIV GDVSITDGDL
VAKLLPKAPN QGDGDQIKPL ILSLSVYKDG IVRLKIDEDH SLNPPKKRFQ VPDVVVSEFE
EKKIWLQKVA TETISGDTSP SSVVYVSDGY EAVVRHDPFE VYVREKSGDR RRVVSLNSHG
LFDFEQLGRK TEGDNWEEKF RTHTDSRPSG PQSISFDVSF YDSSFVYGIP EHATSFALKP
TKGPGVEESE PYRLFNLDVF EYDHESPFGL YGSIPFMVSH GKSGKTSGFF WLNAAEMQID
VLANGWDAES GISLPSSHSR IDTFWMSEAG IVDTFFFVGP EPKDVVKQYA SVTGTSAMPQ
LFATGYHQCR WNYKDEEDVA QVDSKFDEHD IPYDVLWLDI EHTDGKRYFT WDSVLFPHPE
EMQKKLAAKG RKMVTIVDPH IKRDDSYFLH KEATQMGYYV KDSSGKDFDG WCWPGSSSYI
DMLSPEIRKW WGGRFSYKNY VGSTPSLYTW NDMNEPSVFN GPEVTMPRDA LHVGGVEHRE
VHNAYGYYFH MATSDGLVMR EEGKDRPFVL SRAIFPGTQR YGAIWTGDNT AEWEHLRVSI
PMILTLGLTG ITFSGADIGG FFGNPEPELL VRWYQVGAYY PFFRGHAHHD TKRREPWLFG
ERNTELMRDA IHTRYTLLPY FYTLFREANV TGVPVVRPLW MEFPQDEATF SNDEAFMVGS
GLLVQGVYTK GTTQASVYLP GKESWYDLRN GKTYVGGKTH KMDAPEESIP AFQKAGTIIP
RKDRFRRSSS QMDNDPYTLV VALNSSQEAE GELYIDDGKS FEFRRGSYIH RRFVFSKGVL
TSTNLAPPEA RLSSQCLIDR IILLGHSSGP KSALVEPLNQ KAEIEMGPLR MGGLVASSGT
KVLTIRKPGV RVDQDWTVKI L
