HRD1_ASHGO
ID HRD1_ASHGO Reviewed; 575 AA.
AC Q75CC8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=ERAD-associated E3 ubiquitin-protein ligase HRD1;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase HRD1 {ECO:0000305};
GN Name=HRD1; OrderedLocusNames=ACL019C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 179.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin
CC specifically from endoplasmic reticulum-associated E2 ligases, and
CC transfers it to substrates promoting their degradation. Mediates the
CC degradation of endoplasmic reticulum proteins (ERQC), also called ER-
CC associated degradation (ERAD). Component of the HRD1 ubiquitin ligase
CC complex, which is part of the ERAD-L and ERAD-M pathways responsible
CC for the rapid degradation of soluble lumenal and membrane proteins with
CC misfolded lumenal domains (ERAD-L), or ER-membrane proteins with
CC misfolded transmembrane domains (ERAD-M) (By similarity).
CC {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.
CC -!- SUBUNIT: Interacts with HRD3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HRD1 family. {ECO:0000305}.
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DR EMBL; AE016816; AAS51209.2; -; Genomic_DNA.
DR RefSeq; NP_983385.2; NM_208738.2.
DR AlphaFoldDB; Q75CC8; -.
DR SMR; Q75CC8; -.
DR STRING; 33169.AAS51209; -.
DR EnsemblFungi; AAS51209; AAS51209; AGOS_ACL019C.
DR GeneID; 4619510; -.
DR KEGG; ago:AGOS_ACL019C; -.
DR eggNOG; KOG0802; Eukaryota.
DR HOGENOM; CLU_026577_0_0_1; -.
DR InParanoid; Q75CC8; -.
DR OMA; DICAVHF; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000591; Chromosome III.
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; IEA:InterPro.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
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;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..575
FT /note="ERAD-associated E3 ubiquitin-protein ligase HRD1"
FT /id="PRO_0000240366"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 5..25
FT /note="Helical; Name=1"
FT TOPO_DOM 26..46
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 47..67
FT /note="Helical; Name=2"
FT TOPO_DOM 68..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 80..100
FT /note="Helical; Name=3"
FT TOPO_DOM 101..103
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 104..124
FT /note="Helical; Name=4"
FT TOPO_DOM 125..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 139..159
FT /note="Helical; Name=5"
FT TOPO_DOM 160..179
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 180..200
FT /note="Helical; Name=6"
FT TOPO_DOM 201..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT ZN_FING 320..368
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 486..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 65420 MW; C4B3C901EBFA5F74 CRC64;
MPREVSWPMW AMFITATYAL AGWSAYSCAT SFDDPLSALF MASSGVHFVI WGNFLIVHYC
LFVWAIIRVL FGQLTAIEYD HIFERLHVVL VTLASIVITM RKTYMAGHMT ILFYTLCLVA
HWVLRDRMDF VFQVHGTDSS LLGILCSRFM FSLLVLGMVD YKMLKFCVQN TNVDGKRHDL
YLMLALSFAQ LILDVLHVVL LTSLNLFEMV RSRRTRSANL VYEGGTTDDD ADDEVFILEG
KYIYETVFDL TITVLKVILD IIQEVFVPWS ITVVYSIFVR SIKAGESFLL VYNYWKNNKK
LYEKLSDVSE EQLDDTDSMC IICMDDMLPT TETTKMNRRA KMLPCGHMLH FGCLKSWMER
SQTCPICRLS VFANDSNSHA TTQAREQTPP DLLQERGIDE HIDVIGMQDM SVQSISLHEG
TAVRRGTTGN CMNQAYDGGL LSHEERDQAG WVAFPIEFRA DNKVFFNLND SQGDRQWMAS
YTSYPRQNMV NSDDPDNASE SHSRIPSPSL PGSLEGTSSQ VDVTVSAKDA PANACFVIAT
SKLEQTKEVE HLKRKVEELE SRVEELSKRI KTDQV
