ID   HRD3_CANGA              Reviewed;         833 AA.
AC   Q6FNV5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=ERAD-associated E3 ubiquitin-protein ligase component HRD3;
DE   Flags: Precursor;
GN   Name=HRD3; OrderedLocusNames=CAGL0J08756g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Component of the endoplasmic reticulum quality control (ERQC)
CC       system involved in ubiquitin-dependent degradation of missfolded
CC       endoplasmic reticulum proteins. 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). ERAD-L substrates are
CC       ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-
CC       conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are
CC       then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97
CC       (UNC) AAA ATPase complex and targeted to the proteasome. ERAD-M
CC       substrates are processed by the same HRD1-HRD3 core complex, but only a
CC       subset of the other components is required for ERAD-M. Stabilizes the
CC       HRD1 ubiquitin-protein ligase. Has also a function in recruiting
CC       misfolded protein substrates (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with HRD1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sel-1 family. {ECO:0000305}.
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DR   EMBL; CR380956; CAG61040.1; -; Genomic_DNA.
DR   RefSeq; XP_448089.1; XM_448089.1.
DR   AlphaFoldDB; Q6FNV5; -.
DR   SMR; Q6FNV5; -.
DR   STRING; 5478.XP_448089.1; -.
DR   EnsemblFungi; CAG61040; CAG61040; CAGL0J08756g.
DR   GeneID; 2889675; -.
DR   KEGG; cgr:CAGL0J08756g; -.
DR   CGD; CAL0133178; CAGL0J08756g.
DR   VEuPathDB; FungiDB:CAGL0J08756g; -.
DR   eggNOG; KOG1550; Eukaryota.
DR   HOGENOM; CLU_348239_0_0_1; -.
DR   InParanoid; Q6FNV5; -.
DR   OMA; DMLAKPR; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IEA:EnsemblFungi.
DR   GO; GO:0000838; C:Hrd1p ubiquitin ligase ERAD-M complex; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0034099; C:luminal surveillance complex; IEA:EnsemblFungi.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:EnsemblFungi.
DR   GO; GO:1905524; P:negative regulation of protein autoubiquitination; IEA:EnsemblFungi.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:EnsemblFungi.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR   Gene3D; 1.25.40.10; -; 2.
DR   InterPro; IPR006597; Sel1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF08238; Sel1; 7.
DR   SMART; SM00671; SEL1; 5.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..833
FT                   /note="ERAD-associated E3 ubiquitin-protein ligase
FT                   component HRD3"
FT                   /id="PRO_0000240368"
FT   TRANSMEM        752..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          107..143
FT                   /note="Sel1-like 1"
FT   REPEAT          147..184
FT                   /note="Sel1-like 2"
FT   REPEAT          185..220
FT                   /note="Sel1-like 3"
FT   REPEAT          592..623
FT                   /note="Sel1-like 4"
FT   REPEAT          624..659
FT                   /note="Sel1-like 5"
FT   REGION          789..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        607
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        688
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        713
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   833 AA;  95778 MW;  7DFEC44E92F4BBB5 CRC64;
     MLLSTYLNWA SVLLTIAGAE SNIDPWDEVS SFLQGKLRKL DVTNPNAYDM NDNEQDATFY
     VSMDYHEEEE RSEYESVWQY YNENSDQDWH KSVYDKLQVS ADQFNNTEAM YKLSQINLWG
     QYGYPHNKSV AFQYLQKFND MTSYENSSAL FDLAVAYSTG LFGTLPVDVA RGLLYFQRSA
     RLGDLKAKQV LAYRYFSGYS VARDVDKALL LYKEIAEEIK KKYSEEQWNM VFPYIESYIV
     RIPDFDEGLL GKGLSTVPQS VRRKKTTRPP FAGSSNLKPI GDVGYGEVVM QFKFNAGNGN
     PGSFVISDSE HEDRLVELFY TAWDLYKGTY TRGRDCDKAK RLLLQVYKTY DAEVKYMDNL
     QKFFYVKSLD LLAHMYFTGE GFERPNVQAA LDLFDRSEKI LEGAEISRTA SEVDKGLISQ
     YYFNNTLGAL KHYKKAKESG NAHGILFYQL GKLSEKNPEL KIGDPYLYMQ EASSQQYLPA
     QYEFAKMVES NELRKYSVED ITRLYKAFVE ENENIMAPHL RLGFSELLGG SSEVSLYAYA
     QAAEQGYEAA QISAAYLLYQ LPYKFDDPPE TTIERKTMAI SYYTRAFKQG NTDAAVVAGD
     IYFQMKNYTK ALSLYQSAAL KFSAQALWNI GYMYEHGLGV EKDFHLAKRF YDQILEHNQK
     LYFAVKASVM KLQLKSWFMW LNGKELDNIS IDQEQESTVV RPFFDRLVQL LKNLSRETRG
     DNKKKNQHRI LKEKKTPSQG IMERFGLQTE DLLTMVCVLI IFAISMFFRT VAPRGQWNVR
     INGVNIAGGN ALGEEGNPEN ENEEDDENDD EGRARARNNF GFGNNFDVQV FAI