Conserved Protein Domain Family
mRING-HC-C3HC5_MGRN1
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cd16816: mRING-HC-C3HC5_MGRN1 
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 (MGRN1) and similar proteins
MGRN1, also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. MGRN1 interacts with cytosolic prion proteins (PrPs) that are linked with neurodegeneration. It also interacts with expanded polyglutamine proteins, and suppresses misfolded polyglutamine aggregation and cytotoxicity. Moreover, MGRN1 inhibits melanocortin receptor signaling by competition with Galphas, suggesting a novel pathway for melanocortin signaling from the cell surface to the nucleus. Furthermore, MGRN1 interacts with and ubiquitylates TSG101, a key component of the endosomal sorting complex required for transport (ESCRT)-I, and regulates endosomal trafficking. A null mutation in the gene encoding MGRN1 causes spongiform neurodegeneration, suggesting a link between dysregulation of endosomal trafficking and spongiform neurodegeneration. MGRN1 contains a modified C3HC5-type RING-HC finger, a conserved PSAP motif necessary for interaction between MGRN1 and TSG101. In addition, MGRN1 harbors a functionally uncharacterized region, as known as the domain associated with RING2 (DAR2), N-terminal to the RING finger. The C3HC5-type RING-HC finger is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.
Links
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Statistics
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PSSM-Id: 438465
Aligned: 6 rows
Threshold Bit Score: 119.398
Created: 27-Mar-2015
Updated: 17-Oct-2022
Structure
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Aligned Rows:
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Zn binding site
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:C C C H C C C CClick to see conserved feature residue pattern help
Evidence:
  • Comment:based on the structures of other RING-HC fingers with bound zinc
  • Comment:modified RING-HC finger (C3HC5-type), extra conserved cysteine is not involved in Zn binding
  • Comment:The C3HC5-type RING finger is distinguished from typical C3HC4 RING-HC finger and C3H2C3 RING-H2 finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.
  • Comment:C3HC4-type RING-HC finger consensus motif: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-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.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                  #  #           # #   #  #          #  #         
O60291       268 DDENSDNSNECVVCLSDLRDTLILPCRHLCLCTSCADTLRYQANNCPICRLPFRALLQ 325 human
XP_007906584 266 DDENSDNSNECVVCLSDLRDTLILPCRHLCLCSTCADTLRYQANNCPICRLPFRALLQ 323 elephant shark
Q7ZUL9       266 EDENSDNSSECVVCLSDLRDTLILPCRHLCLCNACADTLRYQANNCPICRLPFRALLQ 323 zebrafish
XP_005990869 266 DDENSDNSNECVVCLSDLRDTLILPCRHLCLCNSCADTLRYQANNCPICRLPFRALLQ 323 coelacanth
NP_001083558 228 DDENSDNSNECVVCLSDLRDTLILPCRHLCLCNSCADTLRYQANNCPICRLPFRALLQ 285 African clawed frog
XP_015150120 269 DDENSDNSNECVVCLSDLRDTLILPCRHLCLCNSCADTLRYQANNCPICRLPFRALLQ 326 chicken

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