HRD1B_ARATH
ID HRD1B_ARATH Reviewed; 460 AA.
AC Q6NPT7; Q3ECI3; Q9SS55;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ERAD-associated E3 ubiquitin-protein ligase HRD1B {ECO:0000305};
DE Short=AtHrd1B {ECO:0000303|PubMed:21187394};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase HRD1B {ECO:0000305};
GN Name=HRD1B {ECO:0000303|PubMed:21187394};
GN OrderedLocusNames=At1g65040 {ECO:0000312|Araport:AT1G65040};
GN ORFNames=F16G16.4 {ECO:0000312|EMBL:AAF06038.1};
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].
RX PubMed=15978049; DOI=10.1111/j.1742-4658.2005.04770.x;
RA Kamauchi S., Nakatani H., Nakano C., Urade R.;
RT "Gene expression in response to endoplasmic reticulum stress in Arabidopsis
RT thaliana.";
RL FEBS J. 272:3461-3476(2005).
RN [2]
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 [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] {ECO:0000312|EMBL:AAR23700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 HRD3A. {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q6NPT7-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the HRD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF06038.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB189470; BAD42325.1; -; mRNA.
DR EMBL; AC009360; AAF06038.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34319.1; -; Genomic_DNA.
DR EMBL; BT010730; AAR23700.1; -; mRNA.
DR EMBL; AK228264; BAF00212.1; -; mRNA.
DR PIR; B96674; B96674.
DR RefSeq; NP_849843.3; NM_179512.4. [Q6NPT7-1]
DR AlphaFoldDB; Q6NPT7; -.
DR SMR; Q6NPT7; -.
DR STRING; 3702.AT1G65040.2; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PaxDb; Q6NPT7; -.
DR PRIDE; Q6NPT7; -.
DR EnsemblPlants; AT1G65040.2; AT1G65040.2; AT1G65040. [Q6NPT7-1]
DR GeneID; 842812; -.
DR Gramene; AT1G65040.2; AT1G65040.2; AT1G65040. [Q6NPT7-1]
DR KEGG; ath:AT1G65040; -.
DR Araport; AT1G65040; -.
DR TAIR; locus:2014993; AT1G65040.
DR eggNOG; KOG0802; Eukaryota.
DR HOGENOM; CLU_009169_4_2_1; -.
DR InParanoid; Q6NPT7; -.
DR OMA; LYFYTFP; -.
DR OrthoDB; 897451at2759; -.
DR PhylomeDB; Q6NPT7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6NPT7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NPT7; baseline and differential.
DR Genevisible; Q6NPT7; 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 Alternative splicing; Endoplasmic reticulum; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..460
FT /note="ERAD-associated E3 ubiquitin-protein ligase HRD1B"
FT /id="PRO_0000431271"
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..140
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..161
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..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..225
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 226..246
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..460
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..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 52127 MW; FA44A226654FD5D0 CRC64;
MIQLKVYAGL STLATLVVIY HAFSSRGQFY PATVYLSTSK INLVVLLNMG LVLMLSLWNL
VKIVFLGSLR EAEVERLNEQ AWRELMEILF AITIFRQDFS VGFISLVVTL LLIKGLHWMA
QKRVEYIETT PSVTLLSHVR IVSFMVFLLI LDCLLTYSSI QQLIQSRKAS MSVFFTFEYM
ILATTTVSII VKYAFYVTDM LKEGQWEGKP VYTFYLELVR DLLHLSMYLC FFLMIFMNYG
LPLHLIRELY ETFRNFKIRV TDYLRYRKIT SNMNDRFPDA TPEELSSNDA TCIICREEMT
SAKKLVCGHL FHVHCLRSWL ERQNTCPTCR ALVVPAENAT STASGNRGPH QESLQQGTGT
SSSDGQGSSV SAAASENMSR HEARFQAAAS AASIYGRSIV YPSSANTLVW SQGNSLLPQT
EVEAQRRFLE SQIEVLTNQL RLLEKPTTVD TKGKSVADTA
