5ZBU


Conserved Protein Domain Family
RING-H2_RNF13-like

?
cd16665: RING-H2_RNF13-like 
Click on image for an interactive view with Cn3D
RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), and similar proteins
This subfamily includes RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), Zinc/RING finger protein 4 (ZNRF4), and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane domain (TM), and a C-terminal C3H2C3-type RING-H2 finger followed by a putative PEST sequence. RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that functions in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in the ubiquitination of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR). It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. ZNRF4, also known as RING finger protein 204 (RNF204), or Nixin, is an endoplasmic reticulum (ER) membrane-anchored ubiquitin ligase that physically interacts with the ER-localized chaperone calnexin in a glycosylation-independent manner, inducing calnexin ubiquitination, and p97-dependent degradation. The murine protein sperizin (spermatid-specific ring zinc finger) is a homolog of human ZNRF4. It is specifically expressed in Haploid germ cells and is involved in spermatogenesis.
Statistics
?
PSSM-Id: 438327
Aligned: 12 rows
Threshold Bit Score: 84.0198
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:5ZBU; Homo sapiens RNF13 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          #  #              # #  #  #            #  #  
5ZBU_A        24 DVCAICLDEYeDGDKLRILPCSHAYHCKCVDPWLTkt-kKTCPVCKQ 69  human
AAF54124     233 DTCVICLEDFiEDDKLRVLPCSHPYHTHCIDPWLTen-rRVCPICKR 278 fruit fly
EFX76866     231 DTCAICLEDYvDGDKLRILPCSHAYHTKCIDPWLTrn-rRVCPVCKR 276 common water flea
Q9H6Y7       228 DVCAICLDEYeDGDKLRVLPCAHAYHSRCVDPWLTqt-rKTCPICKQ 273 human
KFM58066     234 DVCAICLEDYnEGDKLRLLPCSHAYHAKCIDPWLMnn-rRNCPLCKR 279 Stegodyphus mimosarum
Q8WWF5       307 DLCAICLDEYeEGDQLKILPCSHTYHCKCIDPWFSqaprRSCPVCKQ 353 human
EDV21872     209 DMCAICIDDFaLKDRIRILPCKHAYHCKCIDPWFLvegkRNCPLCKL 255 Trichoplax adhaerens
XP_009023635 233 EVCAVCLEDYsFFDKLRILPCSHAFHQKCIDPWLTrn-kQTCPLCNK 278 Helobdella robusta
EDO36379     264 DVCAICLDEYkEGDKLRILPCDHAYHCKCVDPWLTeg-kRTCPVCKR 309 starlet sea anemone
KOF98358     235 DVCAICLDEYeEGDKLRVLPCAHAYHCKCIDPWLTkn-kRTCPVCKR 280 Octopus bimaculoides
XP_013412372 328 DTCAICLDDYeDGEKLRLLPCQHAYHQQCVDPWLTkn-kRVCPVCKA 373 Lingula anatina
XP_002115508 237 DVCAVCLEDYeDNDKLRLLPCNHAFHARCIDPWILgqdkSTCPLCKQ 283 Trichoplax adhaerens

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