ERD2B_ARATH
ID ERD2B_ARATH Reviewed; 215 AA.
AC Q8VWI1; Q8LD09; Q9LJR8;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=ER lumen protein-retaining receptor B;
GN Name=ERD2B; Synonyms=ERD2.2; OrderedLocusNames=At3g25040;
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 [MRNA].
RA Mahon P.;
RL Thesis (2000), Cambridge University, United Kingdom.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, MUTAGENESIS OF GLY-8; ARG-161 AND ALA-186, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19717464; DOI=10.1073/pnas.0905532106;
RA Li J., Zhao-Hui C., Batoux M., Nekrasov V., Roux M., Chinchilla D.,
RA Zipfel C., Jones J.D.;
RT "Specific ER quality control components required for biogenesis of the
RT plant innate immune receptor EFR.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15973-15978(2009).
CC -!- FUNCTION: Determines the specificity of the luminal endoplasmic
CC reticulum protein retention system. Required for the retro-transport of
CC calreticulin-3 (CRT3) from the Golgi to the ER. Specifically required
CC for elongation factor Tu receptor (EFR) function in response to the
CC pathogen-associated molecular pattern (PAMP) elf18.
CC {ECO:0000269|PubMed:19717464}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:19717464}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19717464}. Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:19717464}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:19717464}.
CC -!- SIMILARITY: Belongs to the ERD2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01889.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ271475; CAC81064.1; -; mRNA.
DR EMBL; AP000412; BAB01889.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76971.1; -; Genomic_DNA.
DR EMBL; AY063921; AAL36277.1; -; mRNA.
DR EMBL; AY142602; AAN13171.1; -; mRNA.
DR EMBL; AY086280; AAM64352.1; -; mRNA.
DR RefSeq; NP_566758.1; NM_113408.4.
DR AlphaFoldDB; Q8VWI1; -.
DR SMR; Q8VWI1; -.
DR STRING; 3702.AT3G25040.1; -.
DR PaxDb; Q8VWI1; -.
DR PRIDE; Q8VWI1; -.
DR ProteomicsDB; 220668; -.
DR EnsemblPlants; AT3G25040.1; AT3G25040.1; AT3G25040.
DR GeneID; 822095; -.
DR Gramene; AT3G25040.1; AT3G25040.1; AT3G25040.
DR KEGG; ath:AT3G25040; -.
DR Araport; AT3G25040; -.
DR TAIR; locus:2086954; AT3G25040.
DR eggNOG; KOG3106; Eukaryota.
DR HOGENOM; CLU_057784_0_0_1; -.
DR InParanoid; Q8VWI1; -.
DR OMA; AYTVYLM; -.
DR OrthoDB; 1186269at2759; -.
DR PhylomeDB; Q8VWI1; -.
DR PRO; PR:Q8VWI1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VWI1; baseline and differential.
DR Genevisible; Q8VWI1; AT.
DR GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046923; F:ER retention sequence binding; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006621; P:protein retention in ER lumen; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR000133; ER_ret_rcpt.
DR PANTHER; PTHR10585; PTHR10585; 1.
DR Pfam; PF00810; ER_lumen_recept; 1.
DR PRINTS; PR00660; ERLUMENR.
DR PROSITE; PS00951; ER_LUMEN_RECEPTOR_1; 1.
DR PROSITE; PS00952; ER_LUMEN_RECEPTOR_2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Protein transport; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..215
FT /note="ER lumen protein-retaining receptor B"
FT /id="PRO_0000429318"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 8
FT /note="G->D: In erd2b-1; strongly reduced response to the
FT PAMP elf18, but no effect on the response to PAMP flg22."
FT /evidence="ECO:0000269|PubMed:19717464"
FT MUTAGEN 161
FT /note="R->H: In erd2b-4; strongly reduced response to the
FT PAMP elf18, but no effect on the response to PAMP flg22."
FT /evidence="ECO:0000269|PubMed:19717464"
FT MUTAGEN 186
FT /note="A->V: In erd2b-5; strongly reduced response to the
FT PAMP elf18, but no effect on the response to PAMP flg22."
FT /evidence="ECO:0000269|PubMed:19717464"
FT CONFLICT 124
FT /note="S -> F (in Ref. 5; AAM64352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 215 AA; 25563 MW; 89674213A8C87E64 CRC64;
MNIFRLAGDM THLASVLVLL LKIHTIKSCA GVSLKTQELY AIVFATRYLD IFTSFVSLYN
TSMKLVFLGS SFSIVWYMKY HKAVHRTYDR EQDTFRHWFL VLPCFLLALL IHEKFTFLEV
LWTSSLYLEA VAILPQLVLL QRTRNIDNLT GQYIFLLGGY RGLYILNWIY RYFTEPHFVH
WITWIAGFVQ TLLYADFFYY YFLSWKNNKK LQLPA
