ID   HRD1_CAEBR              Reviewed;         622 AA.
AC   A8Y4B2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=E3 ubiquitin-protein ligase hrd-1 {ECO:0000250|UniProtKB:Q20798};
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 {ECO:0000250|UniProtKB:Q20798};
DE   Flags: Precursor;
GN   Name=sel-11 {ECO:0000250|UniProtKB:Q20798};
GN   Synonyms=hrd-1 {ECO:0000312|EMBL:CAP39732.2}; ORFNames=CBG23271;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP39732.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP39732.2};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q86TM6}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q86TM6}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q86TM6}.
CC   -!- DOMAIN: The RING-type zinc finger is required for E3 ligase activity.
CC       {ECO:0000250|UniProtKB:Q86TM6}.
CC   -!- SIMILARITY: Belongs to the HRD1 family. {ECO:0000255}.
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DR   EMBL; HE601533; CAP39732.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8Y4B2; -.
DR   SMR; A8Y4B2; -.
DR   STRING; 6238.CBG23271; -.
DR   EnsemblMetazoa; CBG23271.1; CBG23271.1; WBGene00041655.
DR   WormBase; CBG23271; CBP35436; WBGene00041655; Cbr-sel-11.
DR   eggNOG; KOG0802; Eukaryota.
DR   HOGENOM; CLU_009169_3_1_1; -.
DR   InParanoid; A8Y4B2; -.
DR   OMA; NILMQQY; -.
DR   OrthoDB; 897451at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008549; Chromosome V.
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; IEA:EnsemblMetazoa.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:EnsemblMetazoa.
DR   GO; GO:0008593; P:regulation of Notch signaling pathway; IEA:EnsemblMetazoa.
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..622
FT                   /note="E3 ubiquitin-protein ligase hrd-1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370205"
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..141
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..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..622
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          436..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  68088 MW;  D0C072B328EC1C15 CRC64;
     MRVSAGLMIG GSCVATAATV LNAFVINKQF YPSIVYLSKS NASMAVLYFQ GIVLVYLMFQ
     LLKSILFGDL RAAEAEHLSE RTWHAVLETC LAFTVFRDDF SAMFVMQFIG LLFIKCFHWL
     ADDRVDMMER SPVITLRFHL RMMTVLAALG FADSYFVSSA YFSTITKGAS SQIVFGFEYA
     ILLALVLHVT IKYLLHMHDL RNPQSWDNKA VYLLYAELLI NLIRCVLYGF FAVIMLRVHT
     FPLFSVRPFY QSVRALHKAF LDVILSRRAI NAMNSQFPVV SNDELSAMDA TCIICREEMT
     VESSPKRLPC SHVFHAHCLR SWFQRQQTCP TCRTDIWQGR NGAAGGANAG GAAENNAAGA
     PPAAGIPPFL PFLGHQFGFP QAAAGAQVGG AQAGGHPGPF PHQIFYAPAP ANRPEFMNLA
     PPPMPMAGPP GMFPMMPPPP IPQPNAAPGE SSNAEPPGRP NFDRFSVEEL HRMEGDMRDA
     ILARIQAMEN IMVILESAQV QMVQLAAITP LRRPVPTAEA SEEETATASS VPTSVPSEEP
     SPAPSTPETA SAPRSMFRGN LFNDTQSTST PSTSAGPQPS LTPSTSSVPS TSSVRTPEAD
     EVRQRRLAHL NARFPPPNPE HE