HRD1_CAEEL
ID HRD1_CAEEL Reviewed; 610 AA.
AC Q20798;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=E3 ubiquitin-protein ligase hrd-1;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase hrd-1 {ECO:0000305};
DE AltName: Full=Suppressor/enhancer of lin-12;
DE Flags: Precursor;
GN Name=sel-11; Synonyms=hrd-1; ORFNames=F55A11.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=8293978; DOI=10.1093/genetics/135.3.765;
RA Sundaram M., Greenwald I.;
RT "Suppressors of a lin-12 hypomorph define genes that interact with both
RT lin-12 and glp-1 in Caenorhabditis elegans.";
RL Genetics 135:765-783(1993).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17825049; DOI=10.1111/j.1365-2443.2007.01108.x;
RA Sasagawa Y., Yamanaka K., Ogura T.;
RT "ER E3 ubiquitin ligase HRD-1 and its specific partner chaperone BiP play
RT important roles in ERAD and developmental growth in Caenorhabditis
RT elegans.";
RL Genes Cells 12:1063-1073(2007).
CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase which accepts
CC ubiquitin specifically from endoplasmic reticulum-associated ubc-7 E2
CC ligase and transfers it to substrates, promoting their degradation.
CC Component of the endoplasmic reticulum quality control (ERQC) system,
CC which is also called the ER-associated degradation (ERAD) system,
CC involved in ubiquitin-dependent degradation of misfolded endoplasmic
CC reticulum proteins. Also promotes the degradation of normal but
CC naturally short-lived proteins. Protects cells from ER stress-induced
CC apoptosis. Thought to play a role together with hsp-3 in developmental
CC growth and function of intestinal cells and to play a role together
CC with hsp-4 in gonad formation. {ECO:0000269|PubMed:17825049,
CC ECO:0000269|PubMed:8293978}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The RING-type zinc finger is required for E3 ligase activity.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth rate.
CC {ECO:0000269|PubMed:17825049}.
CC -!- SIMILARITY: Belongs to the HRD1 family. {ECO:0000305}.
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DR EMBL; Z72511; CAA96657.1; -; Genomic_DNA.
DR PIR; T22687; T22687.
DR RefSeq; NP_505969.1; NM_073568.4.
DR AlphaFoldDB; Q20798; -.
DR SMR; Q20798; -.
DR BioGRID; 44637; 9.
DR DIP; DIP-26690N; -.
DR IntAct; Q20798; 4.
DR STRING; 6239.F55A11.3; -.
DR iPTMnet; Q20798; -.
DR EPD; Q20798; -.
DR PaxDb; Q20798; -.
DR PeptideAtlas; Q20798; -.
DR EnsemblMetazoa; F55A11.3.1; F55A11.3.1; WBGene00004768.
DR GeneID; 179612; -.
DR KEGG; cel:CELE_F55A11.3; -.
DR UCSC; F55A11.3; c. elegans.
DR CTD; 179612; -.
DR WormBase; F55A11.3; CE05945; WBGene00004768; sel-11.
DR eggNOG; KOG0802; Eukaryota.
DR GeneTree; ENSGT00940000172216; -.
DR HOGENOM; CLU_009169_3_1_1; -.
DR InParanoid; Q20798; -.
DR OMA; PGMGAPF; -.
DR OrthoDB; 897451at2759; -.
DR PhylomeDB; Q20798; -.
DR Reactome; R-CEL-5358346; Hedgehog ligand biogenesis.
DR SignaLink; Q20798; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q20798; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004768; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; IEA:InterPro.
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:0035264; P:multicellular organism growth; IGI:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:WormBase.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IGI:WormBase.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032832; E3_lig_synoviolin/Hrd1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22763:SF169; PTHR22763:SF169; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..610
FT /note="E3 ubiquitin-protein ligase hrd-1"
FT /id="PRO_0000280553"
FT TOPO_DOM 24..41
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..144
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..215
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 292..333
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 386..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 66814 MW; 42BE294F4A554F50 CRC64;
MRVSAGLMIG GSCVATAATI LNAFLINKQF YPSIVYLSKS NASMAVIYVQ GIVLVYLMFQ
LLKSILFGDL RAAEAEHLSE RTWHAVLETC LAFTVFRDDF SAIFVMQFIG LLFIKCFHWL
ADDRVDMMER SPVITLRFHL RMMTVLAALG FADSYFVSSA YFTTITRGAS AQIVFGFEYA
ILLALVLHVT IKYLLHMHDL RNPQSWDNKA VYLLYAELFI NLIRCLLYGF FAVVMLRVHT
FPLFSVRPFY QSVRALHKAF LDVILSRRAI NAMNSQFPVV SAEDLAAMDA TCIICREEMT
VDASPKRLPC SHVFHAHCLR SWFQRQQTCP TCRTDIWQGR NGAAAGGNAA DAAANVADAN
VAGAQIGAGM PPFLPFLGHQ FGFPQQPAGA GGAQPGAAQA GGQPGPFPHQ IFYAPAPANR
PEFMNLIPPP PLPMAGPPGM FPMMPPPPLP QVNTTQGTSS ETPPVNPSYS QLSTEELRRM
EGESREALLA RLQAMDNIMV LLESAQMQMI QLATVTPIRP RPVVPSDESE QEAPGPSTDQ
VTSEEQEIPA TSSAPSIFRT ESPSTSSTAP STSSPVTASS TPTTSSTRTP EAEEVRQRRL
ARLLGENANQ
