HRD3_YEAST » ERAD-associated E3 ubiquitin-protein ligase component HRD3

HRD3_YEAST » ERAD-associated E3 ubiquitin-protein ligase component HRD3
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Topology in Endoplasmic reticulum membrane
Topologylumenal side
cytoplasmic side
HRD3_YEAST » ERAD-associated E3 ubiquitin-protein ligase component HRD3 » HMG-CoA reductase degradation protein 3;
Hydrophobic Thickness 30.8 ± 1.6 Å
Tilt Angle 0 ± 0°
ΔGtransfer -33.2 kcal/mol
ΔGfold -17.1 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING
Topology Out
TM Segments 766-788 (766-791)
Pathways

Protein processing in endoplasmic reticulum (KEGG)

PDB none
OPM none
Complexes none
Interactions

ALG5, Complex: HRD3:ALG5

BIG1, Complex: HRD3:BIG1

CALX, Complex: HRD3:CALX

CD4, Complex: CD4:HRD3, PubMed

CUE1, Complex: HRD3:CUE1

CWH41, Complex: HRD3:CWH41

EMP47, Complex: HRD1:UBX2:OS9:EMP47:USA1:CBPY:HRD3:CDC48:GRP78, PubMed

GDA1, Complex: GDA1:HRD3

GPI8, Complex: HRD3:GPI8

IRE1, Complex: HRD3:IRE1

SEC22, Complex: HRD3:SEC22

TSC3, Complex: TSC3:HRD3

UBX2, Complex: UBX2:HRD3, PubMed

YUR1, Complex: YUR1:HRD3

Domains

AA: 143-186, PDBID: 1OUV, Subunit A, Seq Identity:30%, Sel1 repeat

AA: 628-663, PDBID: 1OUV, Subunit A, Seq Identity:32%, Sel1 repeat

UniProt annotation for HRD3_YEAST » ERAD-associated E3 ubiquitin-protein ligase component HRD3
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.

SUBUNIT: 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.

UniProt features for HRD3_YEAST » ERAD-associated E3 ubiquitin-protein ligase component HRD3
SIGNAL 1 20 Potential.
CHAIN 21 833 ERAD-associated E3 ubiquitin-protein ligase component HRD3.
REPEAT 103 139 Sel1-like 1.
REPEAT 143 186 Sel1-like 2.
REPEAT 187 222 Sel1-like 3.
REPEAT 413 445 Sel1-like 4.
REPEAT 552 595 Sel1-like 5.
REPEAT 596 627 Sel1-like 6.
REPEAT 628 663 Sel1-like 7.
Amino Acid Sequence for HRD3_YEAST » ERAD-associated E3 ubiquitin-protein ligase component HRD3
MITLLLYLCV ICNAIVLIRA DSIADPWPEA RHLLNTIAKS RDPMKEAAME PNADEFVGFY VPMDYSPRNE EKNYQSIWQN EITDSQRHIY ELLVQSSEQF NNSEATYTLS QIHLWSQYNF PHNMTLAHKY LEKFNDLTHF TNHSAIFDLA VMYATGGCAS GNDQTVIPQD SAKALLYYQR AAQLGNLKAK QVLAYKYYSG FNVPRNFHKS LVLYRDIAEQ LRKSYSRDEW DIVFPYWESY NVRISDFESG LLGKGLNSVP SSTVRKRTTR PDIGSPFIAQ VNGVQMTLQI EPMGRFAFNG NDGNINGDED DEDASERRII RIYYAALNDY KGTYSQSRNC ERAKNLLELT YKEFQPHVDN LDPLQVFYYV RCLQLLGHMY FTGEGSSKPN IHMAEEILTT SLEISRRAQG PIGRACIDLG LINQYITNNI SQAISYYMKA MKTQANNGIV EFQLSKLATS FPEEKIGDPF NLMETAYLNG FIPAIYEFAV MIESGMNSKS SVENTAYLFK TFVDKNEAIM APKLRTAFAA LINDRSEVAL WAYSQLAEQG YETAQVSAAY LMYQLPYEFE DPPRTTDQRK TLAISYYTRA FKQGNIDAGV VAGDIYFQMQ NYSKAMALYQ GAALKYSIQA IWNLGYMHEH GLGVNRDFHL AKRYYDQVSE HDHRFYLASK LSVLKLHLKS WLTWITREKV NYWKPSSPLN PNEDTQHSKT SWYKQLTKIL QRMRHKEDSD KAAEDSHKHR TVVQNGANHR GDDQEEASEI LGFQMEDLVT MGCILGIFLL SILMSTLAAR RGWNVRFNGA QLNANGNRQQ EQQQQQQAQG PPGWDFNVQI FAI