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   24-JAN-2024, entry version 137.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.Q9FM96; -.
DR   iPTMnet; Q9FM96; -.
DR   PaxDb; 3702-AT5G56360-1; -.
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; AT5G56360; PSL4.
DR   eggNOG; KOG2397; Eukaryota.
DR   HOGENOM; CLU_016834_3_0_1; -.
DR   InParanoid; Q9FM96; -.
DR   OMA; YENGQHC; -.
DR   OrthoDB; 103990at2759; -.
DR   PhylomeDB; Q9FM96; -.
DR   UniPathway; UPA00957; -.
DR   PRO; PR:Q9FM96; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FM96; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR   Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 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:SF1; GLUCOSIDASE 2 SUBUNIT BETA; 1.
DR   PANTHER; PTHR12630; N-LINKED OLIGOSACCHARIDE PROCESSING; 1.
DR   Pfam; PF12999; PRKCSH-like; 1.
DR   Pfam; PF13015; PRKCSH_1; 1.
DR   SUPFAM; SSF50911; Mannose 6-phosphate receptor domain; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS51914; MRH; 1.
DR   Genevisible; Q9FM96; AT.
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
//