ID   HRDL1_CAEBR             Reviewed;         578 AA.
AC   A8WWR3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=E3 ubiquitin-protein ligase hrd-like protein 1;
GN   Name=hrdl-1 {ECO:0000312|EMBL:CAP24624.1}; ORFNames=CBG03795;
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:CAP24624.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP24624.1};
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: Proposed to have a role in neuroprotection.
CC       {ECO:0000250|UniProtKB:P90859}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
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DR   EMBL; HE600906; CAP24624.1; -; Genomic_DNA.
DR   RefSeq; XP_002639237.1; XM_002639191.1.
DR   AlphaFoldDB; A8WWR3; -.
DR   SMR; A8WWR3; -.
DR   STRING; 6238.CBG03795; -.
DR   EnsemblMetazoa; CBG03795.1; CBG03795.1; WBGene00026578.
DR   GeneID; 8581231; -.
DR   KEGG; cbr:CBG_03795; -.
DR   CTD; 8581231; -.
DR   WormBase; CBG03795; CBP14918; WBGene00026578; Cbr-hrdl-1.
DR   eggNOG; KOG0802; Eukaryota.
DR   HOGENOM; CLU_015061_1_0_1; -.
DR   InParanoid; A8WWR3; -.
DR   OMA; WAWFTAL; -.
DR   OrthoDB; 897451at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:EnsemblMetazoa.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:1901214; P:regulation of neuron death; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR003892; CUE.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF02845; CUE; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00546; CUE; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS51140; CUE; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW   Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN           1..578
FT                   /note="E3 ubiquitin-protein ligase hrd-like protein 1"
FT                   /id="PRO_0000370218"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          447..489
FT                   /note="CUE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT   ZN_FING         350..388
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   578 AA;  66025 MW;  0A4E47141A211D27 CRC64;
     MNRGNPQALR HPQVPLGIAN IIGRSTFPSV EGYLALSLCV AFIASASVFT HFHSQPEIKR
     LLEEELRNNT RLTTAFGINI DTIAGSTVFQ MAHYILTDTT LIWVAINSYF AILAMCTKLI
     IKLTFKELSR QEEVAARQAF LSYILLTIVY LSVVTGPQKG HRVMPWMIWG GVCGFLSHLQ
     FVTCQRLKYT SPSCDRGSQR VSFISLFLFF VSIAMTFMVS RFQQHLEWQP AVLLYFDCLL
     AVFRSTYILF RCISSSRVFS FNPDSVRHFN YWLELATNFA CELLQFLSYA QLFVFAPGLN
     LTSIFFLYHM KLTYNCMREQ LGRHRTHKKI FEHIESAYPS VKAANSDDRC IVCWELLGTS
     RRLPCSHQFH DWCLMWWLAQ DSSCPTCRYV IPSPQEEASR TDSGNGNTMF RFNGRTFGFF
     TLPSFTVEVG SSFGNIFGRA AEPTQEQLQS MLETVLEMFP QMSPETILAD LRQSGSAQST
     IENILEGRMG LNASLIPGVL DEDLSDDTDN ELEYEEHVEV VQEPDRTRQR TWTKLSSSSG
     EAELSYYEIQ RANMIETYRR KYLASDKAAD LRAMGITE