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Q05787

- HRD3_YEAST

UniProt

Q05787 - HRD3_YEAST

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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

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 - 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
Complete GO annotation...

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

Topology

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

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
Complete GO annotation...

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.
SMRiQ05787. Positions 428-454.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ05787.
KOiK14023.
OMAiWIANFLE.
OrthoDBiEOG741Z9S.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR006597. Sel1-like.
IPR011990. TPR-like_helical_dom.
[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

        10         20         30         40         50
MITLLLYLCV ICNAIVLIRA DSIADPWPEA RHLLNTIAKS RDPMKEAAME
60 70 80 90 100
PNADEFVGFY VPMDYSPRNE EKNYQSIWQN EITDSQRHIY ELLVQSSEQF
110 120 130 140 150
NNSEATYTLS QIHLWSQYNF PHNMTLAHKY LEKFNDLTHF TNHSAIFDLA
160 170 180 190 200
VMYATGGCAS GNDQTVIPQD SAKALLYYQR AAQLGNLKAK QVLAYKYYSG
210 220 230 240 250
FNVPRNFHKS LVLYRDIAEQ LRKSYSRDEW DIVFPYWESY NVRISDFESG
260 270 280 290 300
LLGKGLNSVP SSTVRKRTTR PDIGSPFIAQ VNGVQMTLQI EPMGRFAFNG
310 320 330 340 350
NDGNINGDED DEDASERRII RIYYAALNDY KGTYSQSRNC ERAKNLLELT
360 370 380 390 400
YKEFQPHVDN LDPLQVFYYV RCLQLLGHMY FTGEGSSKPN IHMAEEILTT
410 420 430 440 450
SLEISRRAQG PIGRACIDLG LINQYITNNI SQAISYYMKA MKTQANNGIV
460 470 480 490 500
EFQLSKLATS FPEEKIGDPF NLMETAYLNG FIPAIYEFAV MIESGMNSKS
510 520 530 540 550
SVENTAYLFK TFVDKNEAIM APKLRTAFAA LINDRSEVAL WAYSQLAEQG
560 570 580 590 600
YETAQVSAAY LMYQLPYEFE DPPRTTDQRK TLAISYYTRA FKQGNIDAGV
610 620 630 640 650
VAGDIYFQMQ NYSKAMALYQ GAALKYSIQA IWNLGYMHEH GLGVNRDFHL
660 670 680 690 700
AKRYYDQVSE HDHRFYLASK LSVLKLHLKS WLTWITREKV NYWKPSSPLN
710 720 730 740 750
PNEDTQHSKT SWYKQLTKIL QRMRHKEDSD KAAEDSHKHR TVVQNGANHR
760 770 780 790 800
GDDQEEASEI LGFQMEDLVT MGCILGIFLL SILMSTLAAR RGWNVRFNGA
810 820 830
QLNANGNRQQ EQQQQQQAQG PPGWDFNVQI FAI
Length:833
Mass (Da):95,481
Last modified:November 1, 1996 - v1
Checksum:iE7DB29FBA16D9BFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
SMRi Q05787. Positions 428-454.
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.
InParanoidi Q05787.
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_dom.
[Graphical view ]
Pfami PF08238. Sel1. 6 hits.
[Graphical view ]
SMARTi SM00671. SEL1. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 106 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