Conserved Protein Domain Family
RING-H2_RNF121-like
?
cd16475: RING-H2_RNF121-like 
RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins
This subfamily includes RNF121, RNF175 and similar proteins. RNF121 is an E3-ubiquitin ligase present in the endoplasmic reticulum (ER) and cis-Golgi compartments. It is a novel regulator of apoptosis. It also facilitates the degradation and membrane localization of voltage-gated sodium (NaV) channels, and thus plays a role in the quality control of NaV channels during their synthesis and subsequent transport to the membrane. Moreover, RNF121 acts as a broad regulator of nuclear factor kappaB (NF-kappaB) signaling since its silencing also dampens NF-kappaB activation following stimulation of toll-like receptors (TLRs), nod-like receptors (NLRs), RIG-I-like Receptors (RLRs) or after DNA damage. RNF121 contains five conserved transmembrane (TM) domains and a C3H2C2-type RING-H2 finger. RNF175 is an uncharacterized RING finger protein that shows high sequence similarity with RNF121. This family also includes Arabidopsis RING finger E3 ligase RHA2A, RHA2B, and their homologs. RHA2A is a positive regulator of abscisic acid (ABA) signaling during seed germination and early seedling development. RHA2B may play a role in the ubiquitin-dependent proteolysis pathway that respond to proteasome inhibition. All subfamily members contain a C3H2C3-type RING-H2 finger, which is responsible for E3-ubiquitin ligase activity.
Links
?
Statistics
?
PSSM-Id: 438138
Aligned: 27 rows
Threshold Bit Score: 84.2678
Created: 2-May-2013
Updated: 17-Oct-2022
Structure
?
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 H H C C CClick to see conserved feature residue pattern help
Evidence:
  • Comment:based on the structures of other RING-H2 fingers with bound zinc
  • 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.
Scroll to Sequence Alignment Display
Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection: 

Feature 1          #  #               # #  #  #                #  #   
Q9H920       224 SVCAVCGQ.[12].ENTYRLSCNHVFHEFCIRGWCI.[1].GKKQTCPYCKEK 278 human
Q09251       294 GVCAVCGG.[24].EKLYKLSCGHVFHEFCIRGWVV.[1].GKLQTCPYCKER 360 Caenorhabditis elegans
CBY30697     174 DTCGVCGE.[11].EKQHTLPCGHSFHDYCIRGWVI.[1].GKKQICPVCKEK 227 Oikopleura dioica
EDQ85429     289 DVCAVCGD.[ 9].EKRATLPCGHVMHDFCIRGWCI.[1].GKKQTCPYCKEK 340 Monosiga brevicollis MX1
EKX44945     105 TVCLLCGD.[24].ERTVNLSCGHSFHDFCIRGWTI.[1].GKKDICPFCSEK 171 Guillardia theta CCMP2712
EFN56031     209 RSCGICGG.[23].LGTIQLSCKHLFHMECIRGWCI.[1].GKKDTCPTCWEK 274 Chlorella variabilis
XP_004343440 221 NMCGICTE.[10].TRVVKLECQHHFHEFCIRGWCI.[1].GKKQTCPYCKEK 273 Capsaspora owczarzaki ATCC 30864
EFC48740     211 HVCGICNQ.[44].QETKVLSCQHKFHEFCLYGWLI.[1].GKKDSCPICKEV 297 Naegleria gruberi strain NEG-M
AGE96407     238 SLCMICTK.[ 5].VKIHTLVCSHSFHEDCIKGWCL.[1].GKKPFCPYCKKR 285 Encephalitozoon cuniculi
CEO94280     174 RICALCDQ.[13].RNVHVLACGHRYHDLCLRGWAM.[1].GKKDTCAYCREK 229 Plasmodiophora brassicae

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