Conserved Protein Domain Family
RING_CH-C4HC3_MARCH7-like
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cd16703: RING_CH-C4HC3_MARCH7-like 
RING-CH finger, H2 subclass (C4HC3-type), found in membrane-associated MARCH7, MARCH10, and similar proteins
This subfamily includes two closely related membrane-associated RING-CH proteins, MARCH7 and MARCH10, both of which are predicted to have no transmembrane spanning region, but do harbor a C4HC3-type RING-CH finger, also known as vRING or RINGv, a variant of C3H2C3-type RING-H2 finger, that is responsible for E3 activity. MARCH7, also known as MARCH-VII, RNF177, or axotrophin, is a ubiquitin E3 ligase expressed in multiple types of cells and tissues, including stem cells and precursor cells, and is predominantly localized on the plasma membrane, and cytoplasm. MARCH7 is involved in T cell proliferation and neuronal development. It also participates in the regulation of cytoskeleton re-organization, cellular migration and invasion, cell proliferation, and tumorigenesis in ovarian carcinoma cells. Moreover, MARCH7 modulates nuclear factor kappaB (NF-kappaB) and Wnt/beta-catenin pathways. It has been identified as an authentic target of miR-101. It ubiquitinates tau protein in vitro, impairing microtubule binding. MARCH10, also known as MARCH-X or RNF190, is a microtubule-associated E3 ubiquitin ligase of developing spermatids and is involved in spermiogenesis by regulating the formation and maintenance of the flagella. It is localized to the principal piece of elongating spermatids. in developing spermatids.
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Statistics
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PSSM-Id: 438363
Aligned: 3 rows
Threshold Bit Score: 123.519
Created: 20-Mar-2015
Updated: 17-Oct-2022
Structure
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Aligned Rows:
Download Cn3D
 
Zn binding site
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:C C C C H C C CClick to see conserved feature residue pattern help
Evidence:
  • Comment:based on the structure of human MARCH8 with bound Zn2+ ions through its RING-CH finger
  • Comment:RING-CH finger (C4HC3-type)
  • Comment:A RING finger typically binds two zinc atoms, with its Cys and/or His side chains in a unique "cross-brace" arrangement.
  • Comment:The RING fingers found in MARCH proteins have an unusual arrangement of zinc-coordinating residues: The conserved helix complete with tryptophan at the C-terminal end is present but the cysteines and histidines are arranged in the sequence as C4HC3-type, rather than the typical C3H2C3-type in RING-H2 finger.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1            #  #              # #       #  #                    #  # 
Q8NA82       655 EGDLCRICQIaggspsNPLLEPCGCVGSLQFVHQECLKKWLKVKITSGADLgAVKTCEMCK 715 human
Q9H992       548 EGDLCRICQMaaasssNLLIEPCKCTGSLQYVHQDCMKKWLQAKINSGSSLeAVTTCELCK 608 human
XP_018090360 582 DGDSCRICLTrgdtteNQLISPCQCTGSLQLVHQECLKRWLISKIQSGAELdAVKTCEMCR 642 African clawed frog

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