PSL4_ARATH
ID PSL4_ARATH Reviewed; 647 AA.
AC Q9FM96; Q8LDD0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Glucosidase 2 subunit beta;
DE AltName: Full=Glucosidase II subunit beta;
DE AltName: Full=Protein PRIORITY IN SWEET LIFE 4;
DE Flags: Precursor;
GN Name=PSL4; OrderedLocusNames=At5g56360; ORFNames=MCD7.9;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
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 DISRUPTION PHENOTYPE.
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: Regulatory subunit of glucosidase II (By similarity).
CC Essential for stable accumulation of the receptor EFR that determines
CC the specific perception of bacterial elongation factor Tu (EF-Tu), a
CC potent elicitor of the defense response to pathogen-associated
CC molecular patterns (PAMPs). Required for sustained activation of EFR-
CC mediated signaling, but not receptor FLS2-mediated signaling elicited
CC by the bacterial flagellin flg22. {ECO:0000250,
CC ECO:0000269|PubMed:20007779}.
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:0000255|PROSITE-
CC ProRule:PRU10138}.
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, but mutant plants have compromised defense response induced
CC by the bacterial elicitor elongation factor Tu (EF-Tu).
CC {ECO:0000269|PubMed:20007779}.
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DR EMBL; AB009049; BAB11263.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96753.1; -; Genomic_DNA.
DR EMBL; AY086076; AAM63282.1; -; mRNA.
DR RefSeq; NP_568840.3; NM_125019.5.
DR AlphaFoldDB; Q9FM96; -.
DR SMR; Q9FM96; -.
DR BioGRID; 20980; 5.
DR STRING; 3702.AT5G56360.1; -.
DR iPTMnet; Q9FM96; -.
DR PaxDb; Q9FM96; -.
DR PRIDE; Q9FM96; -.
DR ProteomicsDB; 249362; -.
DR EnsemblPlants; AT5G56360.1; AT5G56360.1; AT5G56360.
DR GeneID; 835736; -.
DR Gramene; AT5G56360.1; AT5G56360.1; AT5G56360.
DR KEGG; ath:AT5G56360; -.
DR Araport; AT5G56360; -.
DR TAIR; locus:2161078; AT5G56360.
DR eggNOG; KOG2397; Eukaryota.
DR HOGENOM; CLU_016834_3_0_1; -.
DR InParanoid; Q9FM96; -.
DR OMA; KCVYRME; -.
DR OrthoDB; 632472at2759; -.
DR PhylomeDB; Q9FM96; -.
DR UniPathway; UPA00957; -.
DR PRO; PR:Q9FM96; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FM96; baseline and differential.
DR Genevisible; Q9FM96; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0017177; C:glucosidase II complex; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR039794; Gtb1-like.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR036607; PRKCSH.
DR InterPro; IPR028146; PRKCSH_N.
DR PANTHER; PTHR12630; PTHR12630; 1.
DR Pfam; PF12999; PRKCSH-like; 1.
DR Pfam; PF13015; PRKCSH_1; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51914; MRH; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Disulfide bond; Endoplasmic reticulum; Plant defense;
KW Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..647
FT /note="Glucosidase 2 subunit beta"
FT /id="PRO_0000425976"
FT DOMAIN 527..622
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 206..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 155..235
FT /evidence="ECO:0000255"
FT MOTIF 644..647
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 206..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 529..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 579..608
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 593..620
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT CONFLICT 126
FT /note="H -> Q (in Ref. 3; AAM63282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 73214 MW; 49CC4F6DF7026472 CRC64;
MRVVVISSFV SVSLQLSFLL LLASAIRSSS SPPNDPFLGI SPQDEKYYKS SSEIKCKDGS
KKFTKAQLND DFCDCSDGTD EPGTSACPTG KFYCRNAGHS PVILFSSRVN DGICDCCDGS
DEYDGHVSCQ NTCWEAGKAA RENLKKKIET YNQGLVIRRQ EIEQAKVGLE KDAAELKKLK
SEQKILKGLV DQLKDRKEQI EKVEEKERLQ KEKEEKEKKE AELAAQQGKG DAEEKTDDSE
KVEESSHDEG TPAVSQHDET THHDEIGNYK DYPSDEEPAA EGEPTSILDE ATHTNPADEH
VVERKEESTS SEDSSSPTDE SQNDGSAEKE ESDEVKKVED FVTEKKEELS KEELGRLVAS
RWTGEKSDKP TEADDIPKAD DQENHEHTPI TAHEADEDDG FVSDGDEDTS DDGKYSDHEP
EDDSYEEEYR HDSSSSYKSD ADDDVDFSET TSNPTWLEKI QKTVKNILLA VNLFQTTPVD
KSEADRVRKE YDESSSKLNK IQSRISSLEK KLKQDFGPEK EFYSFHGRCF ESKQGKYTYK
VCAYKEATQE EGYSKTRLGE WDKFENSYQF MSYTNGEKCW NGPDRSLKVK LRCGLKNELM
DVDEPSRCEY AAILSTPARC LEDKLKELQQ KLEKLMNQDK PQNHDEL
