2M6M


Conserved Protein Domain Family
RING_CH-C4HC3_MARCH6

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cd16702: RING_CH-C4HC3_MARCH6 
Click on image for an interactive view with Cn3D
RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated RING-CH6 (MARCH6)
MARCH6, also known as membrane-associated RING finger protein 6, membrane-associated RING-CH protein VI (MARCH-VI), RING finger protein 176 (RNF176), protein TEB-4, or Doa10 homolog, is an endoplasmic reticulum (ER)-localized E3 ubiquitin ligase that ubiquitinates ER-associated proteins with a cytoplasmic domain in a ubiquitin-conjugating enzyme 7 (UBC7)-dependent manner), such as Mps2, UBC6, and Ste6. It also regulates its own UBC7-mediated degradation. MARCH6 interacts with ubiquitin-specific protease USP19, which deubiquitinates and stabilizes MARCH6 and inhibits p97-dependent proteasomal degradation. It is also involved in the cholesterol synthesis pathway through controlling the degradation of squalene monooxygenase (SM), and affects 3-hydroxy-3-methyl-glutaryl coenzyme A reductase (HMGCR). Furthermore, it may be a key regulator of thyroid hormone activation in a number of tissues, since it mediates the proteasomal degradation of type 2 iodothyronine deiodinase (D2). MARCH6 contains 14 transmembrane helices and a conserved N-terminal C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, that catalyzes ubiquitin Lys48-specific ligation.
Statistics
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PSSM-Id: 319616
View PSSM: cd16702
Aligned: 35 rows
Threshold Bit Score: 81.9264
Threshold Setting Gi: 635575668
Created: 20-Mar-2015
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
Zn binding siteRING-CH finger
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Structure:2M6M; Saccharomyces cerevisiae Doa10p binds two Zn2+ ions through its RING-CH finger.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
Feature 1          #  #             # #       #  #                    #  #  
2M6M_A         20 TCRICRgeatednPLFHPCKCRGSIKYMHESCLLEWVAsknidiskpgadvKCDICHY 77
gi 290975103   59 LCRICKqpaadddPLFHPCKCSGSIKYIHESCLNEWMKhsn-------kgkYCEICKH 109
gi 60466638    12 FCRVCRngstpdnPLSYPCKCSGSIKYIHQNCLLEWIQhsk--------ssSCELCGH 61
gi 28919721    65 QCRICRgdaspddPLYHPCKCSGSIKWVHQECLMQWLAqtq--------rkHCELCKT 114
gi 262106362   19 ECRVCRgeaepdrRLFAPCKCSGSIRFTHSDCLEQWLEhsg--------ksFCELCGH 68
gi 507112806    9 ECRICRgdsepgrPLLHPCRCSGSIKFTHEDCLLNWLAqsg--------ssRCELCNH 58
gi 219109961  131 ECRVCRgpeeegrPLFKPCKCSGSIGLTHQDCLQSWLEvqr-------gdgRCELCHT 181
gi 551676877  133 ECRICRggv-ecgVLLYPCKCSGSIRYVHQECLDAWLArtg--------stKCELCHQ 181
gi 730835      38 TCRICRgeatednPLFHPCKCRGSIKYMHESCLLEWVAsknidiskpgadvKCDICHY 95
gi 857974585   34 ECRVCRggsfddePLYNPCLCRGSIKWVHQSCLQDWLAhrpr------tdgRCELCRH 85

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