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Q05787 (HRD3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ERAD-associated E3 ubiquitin-protein ligase component HRD3
Alternative name(s):
HMG-CoA reductase degradation protein 3
Gene names
Name:HRD3
Ordered Locus Names:YLR207W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length833 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subunit structure

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. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein Potential Ref.6.

Sequence similarities

Belongs to the sel-1 family.

Contains 7 Sel1-like repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRC1P007292EBI-31647,EBI-4153
YOS9Q992208EBI-31647,EBI-34938

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 833813ERAD-associated E3 ubiquitin-protein ligase component HRD3
PRO_0000240369

Regions

Transmembrane768 – 78821Helical; Potential
Repeat103 – 13937Sel1-like 1
Repeat143 – 18644Sel1-like 2
Repeat187 – 22236Sel1-like 3
Repeat413 – 44533Sel1-like 4
Repeat552 – 59544Sel1-like 5
Repeat596 – 62732Sel1-like 6
Repeat628 – 66336Sel1-like 7
Compositional bias809 – 81911Poly-Gln

Amino acid modifications

Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1231N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Glycosylation6111N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q05787 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E7DB29FBA16D9BFD

FASTA83395,481
        10         20         30         40         50         60 
MITLLLYLCV ICNAIVLIRA DSIADPWPEA RHLLNTIAKS RDPMKEAAME PNADEFVGFY 

        70         80         90        100        110        120 
VPMDYSPRNE EKNYQSIWQN EITDSQRHIY ELLVQSSEQF NNSEATYTLS QIHLWSQYNF 

       130        140        150        160        170        180 
PHNMTLAHKY LEKFNDLTHF TNHSAIFDLA VMYATGGCAS GNDQTVIPQD SAKALLYYQR 

       190        200        210        220        230        240 
AAQLGNLKAK QVLAYKYYSG FNVPRNFHKS LVLYRDIAEQ LRKSYSRDEW DIVFPYWESY 

       250        260        270        280        290        300 
NVRISDFESG LLGKGLNSVP SSTVRKRTTR PDIGSPFIAQ VNGVQMTLQI EPMGRFAFNG 

       310        320        330        340        350        360 
NDGNINGDED DEDASERRII RIYYAALNDY KGTYSQSRNC ERAKNLLELT YKEFQPHVDN 

       370        380        390        400        410        420 
LDPLQVFYYV RCLQLLGHMY FTGEGSSKPN IHMAEEILTT SLEISRRAQG PIGRACIDLG 

       430        440        450        460        470        480 
LINQYITNNI SQAISYYMKA MKTQANNGIV EFQLSKLATS FPEEKIGDPF NLMETAYLNG 

       490        500        510        520        530        540 
FIPAIYEFAV MIESGMNSKS SVENTAYLFK TFVDKNEAIM APKLRTAFAA LINDRSEVAL 

       550        560        570        580        590        600 
WAYSQLAEQG YETAQVSAAY LMYQLPYEFE DPPRTTDQRK TLAISYYTRA FKQGNIDAGV 

       610        620        630        640        650        660 
VAGDIYFQMQ NYSKAMALYQ GAALKYSIQA IWNLGYMHEH GLGVNRDFHL AKRYYDQVSE 

       670        680        690        700        710        720 
HDHRFYLASK LSVLKLHLKS WLTWITREKV NYWKPSSPLN PNEDTQHSKT SWYKQLTKIL 

       730        740        750        760        770        780 
QRMRHKEDSD KAAEDSHKHR TVVQNGANHR GDDQEEASEI LGFQMEDLVT MGCILGIFLL 

       790        800        810        820        830 
SILMSTLAAR RGWNVRFNGA QLNANGNRQQ EQQQQQQAQG PPGWDFNVQI FAI

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U14913 Genomic DNA. Translation: AAB67427.1.
BK006945 Genomic DNA. Translation: DAA09524.1.
PIRS48558.
RefSeqNP_013308.1. NM_001182094.1.

3D structure databases

ProteinModelPortalQ05787.
SMRQ05787. Positions 371-404, 416-443, 579-664.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2843N.
IntActQ05787. 10 interactions.
MINTMINT-1722064.
STRING4932.YLR207W.

Proteomic databases

PaxDbQ05787.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR207W; YLR207W; YLR207W.
GeneID850904.
KEGGsce:YLR207W.

Organism-specific databases

CYGDYLR207w.
SGDS000004197. HRD3.

Phylogenomic databases

eggNOGCOG0790.
GeneTreeENSGT00530000063170.
HOGENOMHOG000112949.
KOK14023.
OMAAGDIYFQ.
OrthoDBEOG46T694.

Enzyme and pathway databases

BioCycYEAST:G3O-32325-MONOMER.

Gene expression databases

GenevestigatorQ05787.
GermOnlineYLR207W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D1.25.40.10. 4 hits.
InterProIPR006597. Sel1-like.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF08238. Sel1. 6 hits.
[Graphical view]
SMARTSM00671. SEL1. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio967296.

Entry information

Entry nameHRD3_YEAST
AccessionPrimary (citable) accession number: Q05787
Secondary accession number(s): D6VYK8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 1, 1996
Last modified: May 29, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents