HRD1A_ARATH
ID HRD1A_ARATH Reviewed; 492 AA.
AC Q9LW77;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ERAD-associated E3 ubiquitin-protein ligase HRD1A {ECO:0000305};
DE Short=AtHrd1A {ECO:0000303|PubMed:21187394};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase HRD1A {ECO:0000305};
GN Name=HRD1A {ECO:0000303|PubMed:21187394};
GN OrderedLocusNames=At3g16090 {ECO:0000312|Araport:AT3G16090};
GN ORFNames=MSL1.13 {ECO:0000312|EMBL:BAC41836.1};
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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).
CC -!- FUNCTION: Probable component of the HRD1 ubiquitin ligase complex that
CC mediates the rapid degradation of misfolded endoplasmic reticulum (ER)
CC proteins, a process called ER-associated degradation (ERAD). Targets
CC the misfolded LRR receptor kinase BRI1. Functions redundantly with
CC HRD3B. {ECO:0000269|PubMed:21187394}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the HRD1 family. {ECO:0000305}.
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DR EMBL; DQ059113; AAY57599.1; -; mRNA.
DR EMBL; AB012247; BAB02675.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75770.1; -; Genomic_DNA.
DR EMBL; AK117158; BAC41836.1; -; mRNA.
DR RefSeq; NP_188230.1; NM_112479.3.
DR AlphaFoldDB; Q9LW77; -.
DR SMR; Q9LW77; -.
DR BioGRID; 6188; 2.
DR STRING; 3702.AT3G16090.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PaxDb; Q9LW77; -.
DR PRIDE; Q9LW77; -.
DR ProteomicsDB; 232115; -.
DR EnsemblPlants; AT3G16090.1; AT3G16090.1; AT3G16090.
DR GeneID; 820854; -.
DR Gramene; AT3G16090.1; AT3G16090.1; AT3G16090.
DR KEGG; ath:AT3G16090; -.
DR Araport; AT3G16090; -.
DR TAIR; locus:2093422; AT3G16090.
DR eggNOG; KOG0802; Eukaryota.
DR HOGENOM; CLU_009169_4_1_1; -.
DR InParanoid; Q9LW77; -.
DR OMA; MEFTMLL; -.
DR OrthoDB; 897451at2759; -.
DR PhylomeDB; Q9LW77; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LW77; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LW77; baseline and differential.
DR Genevisible; Q9LW77; AT.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..492
FT /note="ERAD-associated E3 ubiquitin-protein ligase HRD1A"
FT /id="PRO_0000431270"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..24
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..40
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 41..61
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..135
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 136..156
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..191
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..221
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 222..242
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ZN_FING 292..330
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 339..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 56037 MW; A7C1C6C96235370B CRC64;
MIRLRTYAGL SFMATLAVIY HAFSSRGQFY PATVYLSTSK ISLVLLLNMC LVLMLSLWHL
VKFVFLGSLR EAEVERLNEQ AWRELMEILF AITIFRQDFS SGFLPLVVTL LLIKALHWLA
QKRVEYIETT PSVSKLSHFR IVSFMGFLLL VDSLFMYSSI RHLIQSRQAS VSLFFSFEYM
ILATTTVAIF VKYVFYVTDM LMDGQWEKKP VYTFYLELIR DLLHLSMYIC FFFVIFMNYG
VPLHLLRELY ETFRNFQIRV SDYLRYRKIT SNMNDRFPDA TPEELTASDA TCIICREEMT
NAKKLICGHL FHVHCLRSWL ERQQTCPTCR ALVVPPENAT SAAPGQRELH QGSQQGTSSS
GNQGSEISSS AGVSNNSLSR HHARLQAAAS AASVYGKSMV YPSANTVAWS SGVPGTEQVS
TEPDQTLPQH NLPVENSHAY ANMSETKLEE MRKSLETHLE ILRNRLHFLE TRKPESAGEP
ENKGKSVADA AE
