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Q05787

- HRD3_YEAST

UniProt

Q05787 - HRD3_YEAST

Protein

ERAD-associated E3 ubiquitin-protein ligase component HRD3

Gene

HRD3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Component of the endoplasmic reticulum quality control (ERQC) system involved in ubiquitin-dependent degradation of missfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome. ERAD-M substrates are processed by the same HRD1-HRD3 core complex, but only a subset of the other components is required for ERAD-M. Stabilizes the HRD1 ubiquitin-protein ligase. Has also a function in recruiting misfolded protein substrates.10 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. ER-associated ubiquitin-dependent protein catabolic process Source: SGD
    2. protein ubiquitination Source: GOC
    3. retrograde protein transport, ER to cytosol Source: SGD

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32325-MONOMER.

    Protein family/group databases

    TCDBi3.A.16.1.2. the endoplasmic reticular retrotranslocon (er-rt) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ERAD-associated E3 ubiquitin-protein ligase component HRD3
    Alternative name(s):
    HMG-CoA reductase degradation protein 3
    Gene namesi
    Name:HRD3
    Ordered Locus Names:YLR207W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR207w.
    SGDiS000004197. HRD3.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: SGD
    2. Hrd1p ubiquitin ligase ERAD-L complex Source: SGD
    3. Hrd1p ubiquitin ligase ERAD-M complex Source: SGD
    4. integral component of membrane Source: UniProtKB-KW
    5. luminal surveillance complex Source: SGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 833813ERAD-associated E3 ubiquitin-protein ligase component HRD3PRO_0000240369Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi429 – 4291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi611 – 6111N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ05787.
    PaxDbiQ05787.

    Expressioni

    Gene expression databases

    GenevestigatoriQ05787.

    Interactioni

    Subunit structurei

    Component of the HRD1 complex which contains HRD1, HRD3, USA1, DER1, YOS9, KAR2, CDC48, NPL4, UFD1 AND UBX2/SEL1. The complex is composed of the core membrane complex, consisting of the E3 ligase HRD1 and its cofactors HRD3, DER1 and USA1, the substrate recruiting factors KAR2 and YOS9, and the heterotrimeric UFD1-NPL4-CDC48/p97 (UNC) ATPase complex recruited by UBX2/SEL1. The complex interacts with the ERAD substrates HMG1 and HMG2. Interacts with HRD1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC48P256946EBI-31647,EBI-4308
    DER1P383073EBI-31647,EBI-5761
    HRD1Q081099EBI-31647,EBI-37613
    PRC1P007296EBI-31647,EBI-4153
    SEC61P329152EBI-31647,EBI-16400
    YOS9Q992208EBI-31647,EBI-34938

    Protein-protein interaction databases

    BioGridi31475. 70 interactions.
    DIPiDIP-2843N.
    IntActiQ05787. 13 interactions.
    MINTiMINT-1722064.
    STRINGi4932.YLR207W.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05787.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei768 – 78821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati103 – 13937Sel1-like 1Add
    BLAST
    Repeati143 – 18644Sel1-like 2Add
    BLAST
    Repeati187 – 22236Sel1-like 3Add
    BLAST
    Repeati413 – 44533Sel1-like 4Add
    BLAST
    Repeati552 – 59544Sel1-like 5Add
    BLAST
    Repeati596 – 62732Sel1-like 6Add
    BLAST
    Repeati628 – 66336Sel1-like 7Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi809 – 81911Poly-GlnAdd
    BLAST

    Sequence similaritiesi

    Belongs to the sel-1 family.Curated
    Contains 7 Sel1-like repeats.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0790.
    GeneTreeiENSGT00530000063170.
    HOGENOMiHOG000112949.
    KOiK14023.
    OMAiWIANFLE.
    OrthoDBiEOG741Z9S.

    Family and domain databases

    Gene3Di1.25.40.10. 4 hits.
    InterProiIPR006597. Sel1-like.
    IPR011990. TPR-like_helical.
    [Graphical view]
    PfamiPF08238. Sel1. 6 hits.
    [Graphical view]
    SMARTiSM00671. SEL1. 6 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q05787-1 [UniParc]FASTAAdd to Basket

    « Hide

    MITLLLYLCV ICNAIVLIRA DSIADPWPEA RHLLNTIAKS RDPMKEAAME    50
    PNADEFVGFY VPMDYSPRNE EKNYQSIWQN EITDSQRHIY ELLVQSSEQF 100
    NNSEATYTLS QIHLWSQYNF PHNMTLAHKY LEKFNDLTHF TNHSAIFDLA 150
    VMYATGGCAS GNDQTVIPQD SAKALLYYQR AAQLGNLKAK QVLAYKYYSG 200
    FNVPRNFHKS LVLYRDIAEQ LRKSYSRDEW DIVFPYWESY NVRISDFESG 250
    LLGKGLNSVP SSTVRKRTTR PDIGSPFIAQ VNGVQMTLQI EPMGRFAFNG 300
    NDGNINGDED DEDASERRII RIYYAALNDY KGTYSQSRNC ERAKNLLELT 350
    YKEFQPHVDN LDPLQVFYYV RCLQLLGHMY FTGEGSSKPN IHMAEEILTT 400
    SLEISRRAQG PIGRACIDLG LINQYITNNI SQAISYYMKA MKTQANNGIV 450
    EFQLSKLATS FPEEKIGDPF NLMETAYLNG FIPAIYEFAV MIESGMNSKS 500
    SVENTAYLFK TFVDKNEAIM APKLRTAFAA LINDRSEVAL WAYSQLAEQG 550
    YETAQVSAAY LMYQLPYEFE DPPRTTDQRK TLAISYYTRA FKQGNIDAGV 600
    VAGDIYFQMQ NYSKAMALYQ GAALKYSIQA IWNLGYMHEH GLGVNRDFHL 650
    AKRYYDQVSE HDHRFYLASK LSVLKLHLKS WLTWITREKV NYWKPSSPLN 700
    PNEDTQHSKT SWYKQLTKIL QRMRHKEDSD KAAEDSHKHR TVVQNGANHR 750
    GDDQEEASEI LGFQMEDLVT MGCILGIFLL SILMSTLAAR RGWNVRFNGA 800
    QLNANGNRQQ EQQQQQQAQG PPGWDFNVQI FAI 833
    Length:833
    Mass (Da):95,481
    Last modified:November 1, 1996 - v1
    Checksum:iE7DB29FBA16D9BFD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14913 Genomic DNA. Translation: AAB67427.1.
    BK006945 Genomic DNA. Translation: DAA09524.1.
    PIRiS48558.
    RefSeqiNP_013308.1. NM_001182094.1.

    Genome annotation databases

    EnsemblFungiiYLR207W; YLR207W; YLR207W.
    GeneIDi850904.
    KEGGisce:YLR207W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14913 Genomic DNA. Translation: AAB67427.1 .
    BK006945 Genomic DNA. Translation: DAA09524.1 .
    PIRi S48558.
    RefSeqi NP_013308.1. NM_001182094.1.

    3D structure databases

    ProteinModelPortali Q05787.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31475. 70 interactions.
    DIPi DIP-2843N.
    IntActi Q05787. 13 interactions.
    MINTi MINT-1722064.
    STRINGi 4932.YLR207W.

    Protein family/group databases

    TCDBi 3.A.16.1.2. the endoplasmic reticular retrotranslocon (er-rt) family.

    Proteomic databases

    MaxQBi Q05787.
    PaxDbi Q05787.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR207W ; YLR207W ; YLR207W .
    GeneIDi 850904.
    KEGGi sce:YLR207W.

    Organism-specific databases

    CYGDi YLR207w.
    SGDi S000004197. HRD3.

    Phylogenomic databases

    eggNOGi COG0790.
    GeneTreei ENSGT00530000063170.
    HOGENOMi HOG000112949.
    KOi K14023.
    OMAi WIANFLE.
    OrthoDBi EOG741Z9S.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32325-MONOMER.

    Miscellaneous databases

    NextBioi 967296.
    PROi Q05787.

    Gene expression databases

    Genevestigatori Q05787.

    Family and domain databases

    Gene3Di 1.25.40.10. 4 hits.
    InterProi IPR006597. Sel1-like.
    IPR011990. TPR-like_helical.
    [Graphical view ]
    Pfami PF08238. Sel1. 6 hits.
    [Graphical view ]
    SMARTi SM00671. SEL1. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein."
      Hampton R.Y., Gardner R.G., Rine J.
      Mol. Biol. Cell 7:2029-2044(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "A RING-H2 finger motif is essential for the function of Der3/Hrd1 in endoplasmic reticulum associated protein degradation in the yeast Saccharomyces cerevisiae."
      Bordallo J., Wolf D.H.
      FEBS Lett. 448:244-248(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation."
      Plemper R.K., Bordallo J., Deak P.M., Taxis C., Hitt R., Wolf D.H.
      J. Cell Sci. 112:4123-4134(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p."
      Gardner R.G., Swarbrick G.M., Bays N.W., Cronin S.R., Wilhovsky S., Seelig L.P., Kim C., Hampton R.Y.
      J. Cell Biol. 151:69-82(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HRD1.
    7. "HRD gene dependence of endoplasmic reticulum-associated degradation."
      Wilhovsky S., Gardner R.G., Hampton R.Y.
      Mol. Biol. Cell 11:1697-1708(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation."
      Gardner R.G., Shearer A.G., Hampton R.Y.
      Mol. Cell. Biol. 21:4276-4291(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HMG1 AND HMG2.
    9. "A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation."
      Denic V., Quan E.M., Weissman J.S.
      Cell 126:349-359(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH KAR2 AND YOS9.
    10. "Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins."
      Carvalho P., Goder V., Rapoport T.A.
      Cell 126:361-373(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE HRD1 COMPLEX WITH UBX2; HRD1; USA1; DER1; YOS9; KAR2; CDC48; NPL4 AND UFD1.
    11. "The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment."
      Gauss R., Sommer T., Jarosch E.
      EMBO J. 25:1827-1835(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDC48 AND DER1.
    12. "A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery."
      Gauss R., Jarosch E., Sommer T., Hirsch C.
      Nat. Cell Biol. 8:849-854(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HRD1 AND YOS9.

    Entry informationi

    Entry nameiHRD3_YEAST
    AccessioniPrimary (citable) accession number: Q05787
    Secondary accession number(s): D6VYK8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3