HRD3A_ARATH
ID HRD3A_ARATH Reviewed; 678 AA.
AC Q9LM25; Q94BN9;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=ERAD-associated E3 ubiquitin-protein ligase component HRD3A {ECO:0000305};
DE AltName: Full=AtSel1A {ECO:0000303|PubMed:21187394};
DE AltName: Full=Protein EMS-MUTAGENIZED BRI1 SUPPRESSOR 5 {ECO:0000303|PubMed:21187394};
DE Flags: Precursor;
GN Name=HRD3A {ECO:0000305}; Synonyms=EBS5 {ECO:0000303|PubMed:21187394};
GN OrderedLocusNames=At1g18260 {ECO:0000312|Araport:AT1G18260};
GN ORFNames=T10O22.22 {ECO:0000312|EMBL:AAF78381.1};
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 FUNCTION.
RX PubMed=21187394; DOI=10.1073/pnas.1013251108;
RA Su W., Liu Y., Xia Y., Hong Z., Li J.;
RT "Conserved endoplasmic reticulum-associated degradation system to eliminate
RT mutated receptor-like kinases in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:870-875(2011).
RN [5]
RP INTERACTION WITH OS9.
RX PubMed=22516478; DOI=10.1093/mp/sss042;
RA Su W., Liu Y., Xia Y., Hong Z., Li J.;
RT "The Arabidopsis homolog of the mammalian OS-9 protein plays a key role in
RT the endoplasmic reticulum-associated degradation of misfolded receptor-like
RT kinases.";
RL Mol. Plant 5:929-940(2012).
RN [6]
RP INTERACTION WITH OS9.
RX PubMed=22328055; DOI=10.1007/s11103-012-9891-4;
RA Huttner S., Veit C., Schoberer J., Grass J., Strasser R.;
RT "Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic
RT reticulum-associated degradation of glycoproteins.";
RL Plant Mol. Biol. 79:21-33(2012).
CC -!- FUNCTION: Component of the endoplasmic reticulum (ER) quality control
CC system called ER-associated degradation (ERAD) and involved in
CC ubiquitin-dependent degradation of misfolded endoplasmic reticulum
CC proteins. Functions as an ERAD substrate-recruiting factor that
CC recognizes misfolded proteins for the HRD1 E3 ubiquitin ligase complex.
CC Targets the misfolded LRR receptor kinase BRI1.
CC {ECO:0000269|PubMed:21187394}.
CC -!- SUBUNIT: Interacts with OS9. {ECO:0000269|PubMed:22328055,
CC ECO:0000269|PubMed:22516478}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the sel-1 family. {ECO:0000305}.
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DR EMBL; AB189471; BAD42326.1; -; mRNA.
DR EMBL; AC069551; AAF78381.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29692.1; -; Genomic_DNA.
DR EMBL; AY039982; AAK64159.1; -; mRNA.
DR RefSeq; NP_564049.1; NM_101684.4.
DR AlphaFoldDB; Q9LM25; -.
DR SMR; Q9LM25; -.
DR BioGRID; 23645; 3.
DR DIP; DIP-59592N; -.
DR IntAct; Q9LM25; 1.
DR STRING; 3702.AT1G18260.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PaxDb; Q9LM25; -.
DR PRIDE; Q9LM25; -.
DR ProteomicsDB; 228747; -.
DR EnsemblPlants; AT1G18260.1; AT1G18260.1; AT1G18260.
DR GeneID; 838406; -.
DR Gramene; AT1G18260.1; AT1G18260.1; AT1G18260.
DR KEGG; ath:AT1G18260; -.
DR Araport; AT1G18260; -.
DR TAIR; locus:2014109; AT1G18260.
DR eggNOG; KOG1550; Eukaryota.
DR HOGENOM; CLU_007931_4_0_1; -.
DR InParanoid; Q9LM25; -.
DR OMA; DMLAKPR; -.
DR OrthoDB; 357553at2759; -.
DR PhylomeDB; Q9LM25; -.
DR PRO; PR:Q9LM25; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LM25; baseline and differential.
DR Genevisible; Q9LM25; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:TAIR.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR044623; HRD3.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR45084; PTHR45084; 1.
DR Pfam; PF08238; Sel1; 8.
DR SMART; SM00671; SEL1; 8.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..678
FT /note="ERAD-associated E3 ubiquitin-protein ligase
FT component HRD3A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431273"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 124..159
FT /note="Sel1-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 242..277
FT /note="Sel1-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 279..313
FT /note="Sel1-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 317..349
FT /note="Sel1-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 353..386
FT /note="Sel1-like 5"
FT /evidence="ECO:0000255"
FT REPEAT 388..422
FT /note="Sel1-like 6"
FT /evidence="ECO:0000255"
FT REPEAT 506..537
FT /note="Sel1-like 7"
FT /evidence="ECO:0000255"
FT REPEAT 540..568
FT /note="Sel1-like 8"
FT /evidence="ECO:0000255"
FT REGION 40..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 248
FT /note="I -> N (in Ref. 3; AAK64159)"
SQ SEQUENCE 678 AA; 75942 MW; 415235B57FC7430D CRC64;
MRILSYGIVI LSLLVFSFIE FGVHARPVVL VLSNDDLNSG GDDNGVGESS DFDEFGESEP
KSEEELDPGS WRSIFEPDDS TVQAASPQYY SGLKKILSAA SEGNFRLMEE AVDEIEAASS
AGDPHAQSIM GFVYGIGMMR EKSKSKSFLH HNFAAAGGNM QSKMALAFTY LRQDMHDKAV
QLYAELAETA VNSFLISKDS PVVEPTRIHS GTEENKGALR KSRGEEDEDF QILEYQAQKG
NANAMYKIGL FYYFGLRGLR RDHTKALHWF LKAVDKGEPR SMELLGEIYA RGAGVERNYT
KALEWLTLAA KEGLYSAFNG IGYLYVKGYG VDKKNYTKAR EYFEKAVDNE DPSGHYNLGV
LYLKGIGVNR DVRQATKYFF VAANAGQPKA FYQLAKMFHT GVGLKKNLEM ATSFYKLVAE
RGPWSSLSRW ALEAYLKGDV GKALILYSRM AEMGYEVAQS NAAWILDKYG ERSMCMGVSG
FCTDKERHER AHSLWWRASE QGNEHAALLI GDAYYYGRGT ERDFVRAAEA YMHAKSQSNA
QAMFNLGYMH EHGQGLPFDL HLAKRYYDES LQSDAAARLP VTLALASLWL RRNYADTVLV
RVVDSLPEVY PKVETWIENV VFEEGNATIL TLFVCLITIL YLRERQRRQV VVVADPVAAD
VAQPLDADVA QHLAAFPR
