HRDL1_CAEEL
ID HRDL1_CAEEL Reviewed; 564 AA.
AC P90859; P90852;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=E3 ubiquitin-protein ligase hrd-like protein 1;
GN Name=hrdl-1; ORFNames=F26E4.11;
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 IDENTIFICATION.
RX PubMed=10456327; DOI=10.1016/s0014-5793(99)00966-7;
RA Shimizu K., Tani M., Watanabe H., Nagamachi Y., Niinaka Y., Shiroishi T.,
RA Ohwada S., Raz A., Yokota J.;
RT "The autocrine motility factor receptor gene encodes a novel type of seven
RT transmembrane protein.";
RL FEBS Lett. 456:295-300(1999).
RN [3]
RP IDENTIFICATION.
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).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [5]
RP FUNCTION.
RX PubMed=18182484; DOI=10.1073/pnas.0711018105;
RA Hamamichi S., Rivas R.N., Knight A.L., Cao S., Caldwell K.A.,
RA Caldwell G.A.;
RT "Hypothesis-based RNAi screening identifies neuroprotective genes in a
RT Parkinson's disease model.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:728-733(2008).
CC -!- FUNCTION: Proposed to have a role in neuroprotection.
CC {ECO:0000269|PubMed:18182484}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; Z81070; CAB03009.1; -; Genomic_DNA.
DR EMBL; Z81075; CAB03009.1; JOINED; Genomic_DNA.
DR PIR; T21423; T21423.
DR RefSeq; NP_492602.2; NM_060201.5.
DR AlphaFoldDB; P90859; -.
DR SMR; P90859; -.
DR BioGRID; 38256; 1.
DR STRING; 6239.F26E4.11; -.
DR iPTMnet; P90859; -.
DR EPD; P90859; -.
DR PaxDb; P90859; -.
DR EnsemblMetazoa; F26E4.11.1; F26E4.11.1; WBGene00009164.
DR GeneID; 172833; -.
DR KEGG; cel:CELE_F26E4.11; -.
DR CTD; 172833; -.
DR WormBase; F26E4.11; CE51378; WBGene00009164; hrdl-1.
DR eggNOG; KOG0802; Eukaryota.
DR GeneTree; ENSGT00940000156482; -.
DR HOGENOM; CLU_015061_1_0_1; -.
DR InParanoid; P90859; -.
DR OMA; WAWFTAL; -.
DR OrthoDB; 897451at2759; -.
DR PhylomeDB; P90859; -.
DR Reactome; R-CEL-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR PRO; PR:P90859; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009164; Expressed in adult organism and 4 other tissues.
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; IGI:WormBase.
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; IMP: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 1: Evidence at protein level;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..564
FT /note="E3 ubiquitin-protein ligase hrd-like protein 1"
FT /id="PRO_0000056330"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 432..474
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT ZN_FING 335..373
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
SQ SEQUENCE 564 AA; 64709 MW; 7C790C238207E49B CRC64;
MGVVNLLSRS SFPSVDSYLA LSVLVAIVAS VTVFTTFRSQ PELQKLIEEE LRNNTRLSSA
YGLNIEALSG HTFFQIAHYI LSDTTLIWVA INSYFAILAV CTRLIIKLTF KELARQEENV
ARQAFFCYVL LTIVYLSVVI GPQKGHRVMP WMIWGGICAF LSHLQFITCQ RLKHISPSCD
RGSQKISFLS LFLFFVSIAM TFLISRFQHH LTWQPAVLLY FDCLLAVFRS TYILFRCISS
SRVFSFNPDS VRHFNYWLEL ITNFVCELIQ MLSFAQLLAF SPGLNLTSIF FLYHMKLTYN
CMTEQLSRHR NHKKIFEHIE RSYPSVKCAN GDDRCVVCWE LLGTSRRLPC SHQFHDWCLM
WWLAQDSSCP TCRCTIPSPQ DQIRQPPEVG NSTRLRFNGG SFGFVHFPAF TLEVAANFGP
FFGRAAEPTE EQLQTMLEQV REMFPQMSVD IIMTDLRQSG SAQSTIENIL EGRIGMNASF
MPGGVLDDEL SDESENEIEY EEPAEIVQEP DNGRQRTWTK LSSSSGDEDL SYYEIQRAKM
IETYRRKYLE SDKAADLRAM GITE
