HRD1_YEAST
ID HRD1_YEAST Reviewed; 551 AA.
AC Q08109; D6W254;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=ERAD-associated E3 ubiquitin-protein ligase HRD1;
DE EC=2.3.2.27;
DE AltName: Full=HMG-CoA reductase degradation protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase HRD1 {ECO:0000305};
GN Name=HRD1; Synonyms=DER3; OrderedLocusNames=YOL013C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=8970163; DOI=10.1091/mbc.7.12.2029;
RA Hampton R.Y., Gardner R.G., Rine J.;
RT "Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-
RT methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane
RT protein.";
RL Mol. Biol. Cell 7:2029-2044(1996).
RN [4]
RP FUNCTION.
RX PubMed=9437001; DOI=10.1091/mbc.9.1.209;
RA Bordallo J., Plemper R.K., Finger A., Wolf D.H.;
RT "Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation
RT of misfolded lumenal and integral membrane proteins.";
RL Mol. Biol. Cell 9:209-222(1998).
RN [5]
RP FUNCTION.
RX PubMed=10218484; DOI=10.1016/s0014-5793(99)00362-2;
RA Bordallo J., Wolf D.H.;
RT "A RING-H2 finger motif is essential for the function of Der3/Hrd1 in
RT endoplasmic reticulum associated protein degradation in the yeast
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 448:244-248(1999).
RN [6]
RP FUNCTION.
RX PubMed=10547371; DOI=10.1242/jcs.112.22.4123;
RA Plemper R.K., Bordallo J., Deak P.M., Taxis C., Hitt R., Wolf D.H.;
RT "Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-
RT translocation complex mediating protein transport for ER degradation.";
RL J. Cell Sci. 112:4123-4134(1999).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HRD3, TOPOLOGY, AND
RP MUTAGENESIS OF CYS-399.
RX PubMed=11018054; DOI=10.1083/jcb.151.1.69;
RA Gardner R.G., Swarbrick G.M., Bays N.W., Cronin S.R., Wilhovsky S.,
RA Seelig L.P., Kim C., Hampton R.Y.;
RT "Endoplasmic reticulum degradation requires lumen to cytosol signaling.
RT Transmembrane control of Hrd1p by Hrd3p.";
RL J. Cell Biol. 151:69-82(2000).
RN [8]
RP FUNCTION.
RX PubMed=10793145; DOI=10.1091/mbc.11.5.1697;
RA Wilhovsky S., Gardner R.G., Hampton R.Y.;
RT "HRD gene dependence of endoplasmic reticulum-associated degradation.";
RL Mol. Biol. Cell 11:1697-1708(2000).
RN [9]
RP FUNCTION, MUTAGENESIS OF CYS-399, AND TOPOLOGY.
RX PubMed=11139575; DOI=10.1074/jbc.m008608200;
RA Deak P.M., Wolf D.H.;
RT "Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase
RT (E3) involved in endoplasmic reticulum degradation.";
RL J. Biol. Chem. 276:10663-10669(2001).
RN [10]
RP FUNCTION, AND INTERACTION WITH HMG1 AND HMG2.
RX PubMed=11390656; DOI=10.1128/mcb.21.13.4276-4291.2001;
RA Gardner R.G., Shearer A.G., Hampton R.Y.;
RT "In vivo action of the HRD ubiquitin ligase complex: mechanisms of
RT endoplasmic reticulum quality control and sterol regulation.";
RL Mol. Cell. Biol. 21:4276-4291(2001).
RN [11]
RP FUNCTION, INTERACTION WITH UBC1 AND UBC7, AND MUTAGENESIS OF CYS-399.
RX PubMed=11146622; DOI=10.1038/35050524;
RA Bays N.W., Gardner R.G., Seelig L.P., Joazeiro C.A., Hampton R.Y.;
RT "Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-
RT associated degradation.";
RL Nat. Cell Biol. 3:24-29(2001).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [13]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [14]
RP FUNCTION, IDENTIFICATION IN THE HRD1 COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=16873066; DOI=10.1016/j.cell.2006.05.043;
RA Carvalho P., Goder V., Rapoport T.A.;
RT "Distinct ubiquitin-ligase complexes define convergent pathways for the
RT degradation of ER proteins.";
RL Cell 126:361-373(2006).
RN [15]
RP FUNCTION, AND INTERACTION WITH CDC48 AND DER1.
RX PubMed=16619026; DOI=10.1038/sj.emboj.7601088;
RA Gauss R., Sommer T., Jarosch E.;
RT "The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate
RT selection and Cdc48p recruitment.";
RL EMBO J. 25:1827-1835(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [18]
RP FUNCTION, SUBUNIT, INTERACTION WITH DER1 AND USA1, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF CYS-399.
RX PubMed=20005842; DOI=10.1016/j.molcel.2009.10.015;
RA Horn S.C., Hanna J., Hirsch C., Volkwein C., Schutz A., Heinemann U.,
RA Sommer T., Jarosch E.;
RT "Usa1 functions as a scaffold of the HRD-ubiquitin ligase.";
RL Mol. Cell 36:782-793(2009).
RN [19]
RP FUNCTION, SUBUNIT, INTERACTION WITH USA1, AND MUTAGENESIS OF CYS-399.
RX PubMed=21074049; DOI=10.1016/j.cell.2010.10.028;
RA Carvalho P., Stanley A.M., Rapoport T.A.;
RT "Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-
RT ligase Hrd1p.";
RL Cell 143:579-591(2010).
RN [20] {ECO:0007744|PDB:5V6P}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS) OF 1-407 IN COMPLEX WITH
RP HRD3.
RX PubMed=28682307; DOI=10.1038/nature23314;
RA Schoebel S., Mi W., Stein A., Ovchinnikov S., Pavlovicz R., DiMaio F.,
RA Baker D., Chambers M.G., Su H., Li D., Rapoport T.A., Liao M.;
RT "Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex
RT with Hrd3.";
RL Nature 548:352-355(2017).
RN [21] {ECO:0007744|PDB:6VJY, ECO:0007744|PDB:6VJZ, ECO:0007744|PDB:6VK0, ECO:0007744|PDB:6VK1}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 1-480 IN COMPLEX WITH
RP DER1; HRD3 AND USA1, FUNCTION, SUBUNIT, AND TRANSMEMBRANE DOMAINS.
RX PubMed=32327568; DOI=10.1126/science.aaz2449;
RA Wu X., Siggel M., Ovchinnikov S., Mi W., Svetlov V., Nudler E., Liao M.,
RA Hummer G., Rapoport T.A.;
RT "Structural basis of ER-associated protein degradation mediated by the Hrd1
RT ubiquitin ligase complex.";
RL Science 368:0-0(2020).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin
CC specifically from endoplasmic reticulum-associated UBC1 and UBC7 E2
CC ligases, and transfers it to substrates promoting their degradation.
CC Mediates the degradation of endoplasmic reticulum proteins (ERQC), also
CC called ER-associated degradation (ERAD). Component of the HRD1
CC ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M
CC pathways responsible for the rapid degradation of soluble lumenal and
CC membrane proteins with misfolded lumenal domains (ERAD-L), or ER-
CC membrane proteins with misfolded transmembrane domains (ERAD-M). In
CC ERAD-L, facilitates retrotranslocation of misfolded proteins from the
CC ER lumen through the ER membrane in conjunction with DER1
CC (PubMed:32327568). Both proteins have lateral gates facing each other
CC which form a channel through the ER membrane and which distort the
CC membrane region between the lateral gates, making it much thinner than
CC a normal phospholipid bilayer (PubMed:32327568). Substrates insert into
CC the membrane as a hairpin loop with one strand interacting with DER1
CC and the other with HRD1. ERAD-L substrates are ubiquitinated through
CC HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and
CC UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via
CC the action of the CDC48-NPL4-UFD1 ATPase complex and targeted to the
CC proteasome. ERAD-M substrates are processed by the same HRD1-HRD3 core
CC complex, but only a subset of the other components is required for
CC ERAD-M. {ECO:0000269|PubMed:10218484, ECO:0000269|PubMed:10547371,
CC ECO:0000269|PubMed:10793145, ECO:0000269|PubMed:11018054,
CC ECO:0000269|PubMed:11139575, ECO:0000269|PubMed:11146622,
CC ECO:0000269|PubMed:11390656, ECO:0000269|PubMed:16619026,
CC ECO:0000269|PubMed:16873066, ECO:0000269|PubMed:20005842,
CC ECO:0000269|PubMed:21074049, ECO:0000269|PubMed:32327568,
CC ECO:0000269|PubMed:8970163, ECO:0000269|PubMed:9437001}.
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: Monomer (PubMed:32327568). Has also been shown to form
CC homodimers (PubMed:28682307). However, dimer assembly is likely to be
CC non-physiological (PubMed:32327568). Forms homooligomers in a USA1-
CC dependent manner (PubMed:20005842, PubMed:21074049). However, can
CC function as a monomer in ERAD-L so the role of USA1-dependent
CC oligomerization remains unclear (PubMed:32327568). Component of the
CC HRD1 ubiquitin ligase complex which contains the E3 ligase HRD1, its
CC cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and
CC CDC48-binding protein UBX2 (PubMed:16873066). Within the complex,
CC interacts directly with HRD3 and USA1 and indirectly with DER1
CC (PubMed:11018054, PubMed:16619026, PubMed:20005842, PubMed:21074049,
CC PubMed:28682307). In ERAD-L, HRD3 and YOS9 jointly bind misfolded
CC glycoproteins in the endoplasmic reticulum (ER) lumen
CC (PubMed:32327568). Movement of ERAD-L substrates through the ER
CC membrane is facilitated by HRD1 and DER1 which have lateral gates
CC facing each other and which distort the membrane region between the
CC lateral gates, making it much thinner than a normal phospholipid
CC bilayer (PubMed:32327568). Substrates insert into the membrane as a
CC hairpin loop with one strand interacting with DER1 and the other with
CC HRD1 (PubMed:32327568). The HRD1 complex interacts with the
CC heterotrimeric CDC48-NPL4-UFD1 ATPase complex which is recruited by
CC UBX2 via its interaction with CDC48 and which moves ubiquitinated
CC substrates to the cytosol for targeting to the proteasome
CC (PubMed:16873066, PubMed:16619026). The HRD1 complex interacts with the
CC ERAD substrates HMG1 and HMG2 (PubMed:11390656). Interacts with the
CC associated E2 ubiquitin conjugating enzymes UBC1 and UBC7 with its
CC membrane anchor CUE1 (PubMed:11146622). {ECO:0000269|PubMed:11018054,
CC ECO:0000269|PubMed:11146622, ECO:0000269|PubMed:11390656,
CC ECO:0000269|PubMed:16619026, ECO:0000269|PubMed:16873066,
CC ECO:0000269|PubMed:20005842, ECO:0000269|PubMed:21074049,
CC ECO:0000269|PubMed:28682307, ECO:0000269|PubMed:32327568}.
CC -!- INTERACTION:
CC Q08109; P25694: CDC48; NbExp=8; IntAct=EBI-37613, EBI-4308;
CC Q08109; P38307: DER1; NbExp=5; IntAct=EBI-37613, EBI-5761;
CC Q08109; Q08109: HRD1; NbExp=5; IntAct=EBI-37613, EBI-37613;
CC Q08109; Q05787: HRD3; NbExp=11; IntAct=EBI-37613, EBI-31647;
CC Q08109; P00729: PRC1; NbExp=11; IntAct=EBI-37613, EBI-4153;
CC Q08109; Q04228: UBX2; NbExp=7; IntAct=EBI-37613, EBI-27730;
CC Q08109; Q99220: YOS9; NbExp=6; IntAct=EBI-37613, EBI-34938;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11018054, ECO:0000269|PubMed:14562095}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11018054,
CC ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Impaired degradation of proteins with misfolded
CC intramembrane or lumenal domains. {ECO:0000269|PubMed:16873066,
CC ECO:0000269|PubMed:20005842}.
CC -!- MISCELLANEOUS: Present with 2660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HRD1 family. {ECO:0000305}.
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DR EMBL; Z74755; CAA99012.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10770.1; -; Genomic_DNA.
DR PIR; S66695; S66695.
DR RefSeq; NP_014630.1; NM_001183267.1.
DR PDB; 5V6P; EM; 4.10 A; A/B=1-407.
DR PDB; 6VJY; EM; 4.30 A; B=1-430.
DR PDB; 6VJZ; EM; 4.30 A; B=1-480.
DR PDB; 6VK0; EM; 4.10 A; B=1-480.
DR PDB; 6VK1; EM; 3.90 A; B=1-480.
DR PDBsum; 5V6P; -.
DR PDBsum; 6VJY; -.
DR PDBsum; 6VJZ; -.
DR PDBsum; 6VK0; -.
DR PDBsum; 6VK1; -.
DR AlphaFoldDB; Q08109; -.
DR SMR; Q08109; -.
DR BioGRID; 34391; 178.
DR ComplexPortal; CPX-3070; HRD1 ubiquitin ligase complex.
DR DIP; DIP-8850N; -.
DR IntAct; Q08109; 13.
DR MINT; Q08109; -.
DR STRING; 4932.YOL013C; -.
DR TCDB; 3.A.16.1.2; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; Q08109; -.
DR MaxQB; Q08109; -.
DR PaxDb; Q08109; -.
DR PRIDE; Q08109; -.
DR EnsemblFungi; YOL013C_mRNA; YOL013C; YOL013C.
DR GeneID; 854149; -.
DR KEGG; sce:YOL013C; -.
DR SGD; S000005373; HRD1.
DR VEuPathDB; FungiDB:YOL013C; -.
DR eggNOG; KOG0802; Eukaryota.
DR GeneTree; ENSGT00940000172216; -.
DR HOGENOM; CLU_026577_0_0_1; -.
DR InParanoid; Q08109; -.
DR OMA; MEFTMLL; -.
DR BioCyc; YEAST:G3O-33429-MON; -.
DR BRENDA; 2.3.2.27; 984.
DR Reactome; R-SCE-5358346; Hedgehog ligand biogenesis.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q08109; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08109; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; IPI:ComplexPortal.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IDA:SGD.
DR GO; GO:0000838; C:Hrd1p ubiquitin ligase ERAD-M complex; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:SGD.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IDA:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:ParkinsonsUK-UCL.
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 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..551
FT /note="ERAD-associated E3 ubiquitin-protein ligase HRD1"
FT /id="PRO_0000240367"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TRANSMEM 9..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TOPO_DOM 31..43
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TRANSMEM 44..71
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TOPO_DOM 72..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TRANSMEM 85..101
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TOPO_DOM 102..103
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TRANSMEM 104..126
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TOPO_DOM 127..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TRANSMEM 148..169
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TOPO_DOM 170..183
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TRANSMEM 184..208
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TOPO_DOM 209..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TRANSMEM 272..292
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TOPO_DOM 293..296
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TRANSMEM 297..314
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:32327568"
FT TOPO_DOM 315..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32327568"
FT ZN_FING 349..400
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 226..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..551
FT /note="Interaction with USA1"
FT MUTAGEN 399
FT /note="C->S: Stabilizes HRD1. Reduced interaction with
FT substrate. Formation of oligomer with or without USA1."
FT /evidence="ECO:0000269|PubMed:11018054,
FT ECO:0000269|PubMed:11139575, ECO:0000269|PubMed:11146622,
FT ECO:0000269|PubMed:20005842, ECO:0000269|PubMed:21074049"
SQ SEQUENCE 551 AA; 63535 MW; CAA6341E7A94DB0B CRC64;
MVPENRRKQL AIFVVVTYLL TFYCVYSATK TSVSFLQVTL KLNEGFNLMV LSIFILLNST
LLWQLLTKLL FGELRLIEHE HIFERLPFTI INTLFMSSLF HERYFFTVAF FGLLLLYLKV
FHWILKDRLE ALLQSINDST TMKTLIFSRF SFNLVLLAVV DYQIITRCIS SIYTNQKSDI
ESTSLYLIQV MEFTMLLIDL LNLFLQTCLN FWEFYRSQQS LSNENNHIVH GDPTDENTVE
SDQSQPVLND DDDDDDDDRQ FTGLEGKFMY EKAIDVFTRF LKTALHLSML IPFRMPMMLL
KDVVWDILAL YQSGTSLWKI WRNNKQLDDT LVTVTVEQLQ NSANDDNICI ICMDELIHSP
NQQTWKNKNK KPKRLPCGHI LHLSCLKNWM ERSQTCPICR LPVFDEKGNV VQTTFTSNSD
ITTQTTVTDS TGIATDQQGF ANEVDLLPTR TTSPDIRIVP TQNIDTLAMR TRSTSTPSPT
WYTFPLHKTG DNSVGSSRSA YEFLITNSDE KENGIPVKLT IENHEVNSLH GDGGEQIAKK
IVIPDKFIQH I
