6A3Z,6F98


Conserved Protein Domain Family
RING-H2_synoviolin

?
cd16479: RING-H2_synoviolin 
Click on image for an interactive view with Cn3D
RING finger, H2 subclass, found in synoviolin and similar proteins
Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of synoviolin may represent a protective response against neurodegeneration in Parkinson's disease (PD). In addition, synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger.
Statistics
?
PSSM-Id: 438142
Aligned: 37 rows
Threshold Bit Score: 74.6998
Created: 2-May-2013
Updated: 17-Oct-2022
Structure
?
Program:
Drawing:
Aligned Rows:
 
Zn binding site
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:C C C H H C C CClick to see conserved feature residue pattern help
Evidence:
  • Structure:6A3Z; Homo sapiens synoviolin binds two Zn2+ ions
    View structure with Cn3D
  • Comment:C3H2C3-type RING-H2 finger consensus motif: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, where X is any amino acid and the number of X residues varies in different fingers
  • Comment:A RING finger typically binds two zinc atoms, with its Cys and/or His side chains in a unique "cross-brace" arrangement.

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
Feature 1           #  #                                # #  #  #          #  # 
6A3Z_A        10 DNVCIICREEMvt--------------------gaKRLPCNHIFHTSCLRSWFQRQQtCPTCR 52  human
EAL63570     263 DKICIVCREDMts---------------------gKKLPCGHILHLHCLRSWLERQQtCPICR 304 Dictyostelium discoideum AX4
O74757       289 DRTCTICREEMfhpdhppentdemeplprgldmtpKRLPCGHILHFHCLRNWLERQQtCPICR 351 Schizosaccharomyces pombe 972h-
XP_004363922 290 DNVCIICREEMta---------------------aKRLPCGHVFHLHCLRSWLERQQtCPTCR 331 Capsaspora owczarzaki ATCC 30864
EMR08944     287 DKTCIICREEMvhssikkldkn--nksqsrinstpKKLPCNHILHFNCLKNWLERQQsCPTCR 347 Pneumocystis murina B123
EIE18516     287 DGICIICREDLapg------------------arnKKLPCNHVFHMHCLRSWLERQQnCPTCR 331 Coccomyxa sp. C-169
EKX31973     288 DHTCIICREEMqpp-------------------haKKLPCGHIFHFDCLRSWLEEHSqCPTCR 331 Guillardia theta CCMP2712
CAL56130     287 DDVCIICRENMevgaq--------------ggnkpKKLPCGHSFHLHCLRSWLERQQaCPTCR 335 Ostreococcus tauri
CAD37003     338 DDTCIICREEMrpwdphdp--------vrlertraKKLPCGHILHQGCLKSWLERQQvCPTCR 392 Neurospora crassa OR74A
XP_014159718 185 DSTCIICREDMea--------------------gsKKLPCGHIFHLTCLRSWLERQRtCPTCR 227 Sphaeroforma arctica JP610

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap