RNF5_CAEEL
ID RNF5_CAEEL Reviewed; 235 AA.
AC Q09463;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=E3 ubiquitin ligase rnf-5 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:20385102};
DE AltName: Full=RING finger protein 5;
GN Name=rnf-5; ORFNames=C16C10.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 38-VAL--VAL-235.
RX PubMed=15210732; DOI=10.1083/jcb.200401133;
RA Broday L., Kolotuev I., Didier C., Bhoumik A., Podbilewicz B., Ronai Z.;
RT "The LIM domain protein UNC-95 is required for the assembly of muscle
RT attachment structures and is regulated by the RING finger protein RNF-5 in
RT C. elegans.";
RL J. Cell Biol. 165:857-867(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DEVELOPMENTAL STAGE.
RX PubMed=20385102; DOI=10.1016/j.bbrc.2010.04.049;
RA Zaidel-Bar R., Miller S., Kaminsky R., Broday L.;
RT "Molting-specific downregulation of C. elegans body-wall muscle attachment
RT sites: the role of RNF-5 E3 ligase.";
RL Biochem. Biophys. Res. Commun. 395:509-514(2010).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF 38-VAL--VAL-235.
RX PubMed=22285439; DOI=10.1016/j.mod.2012.01.003;
RA Kovacevic I., Ho R., Cram E.J.;
RT "CCDC-55 is required for larval development and distal tip cell migration
RT in Caenorhabditis elegans.";
RL Mech. Dev. 128:548-559(2012).
RN [5]
RP FUNCTION.
RX PubMed=23093945; DOI=10.1371/journal.pgen.1003007;
RA Kuang E., Okumura C.Y., Sheffy-Levin S., Varsano T., Shu V.C., Qi J.,
RA Niesman I.R., Yang H.J., Lopez-Otin C., Yang W.Y., Reed J.C., Broday L.,
RA Nizet V., Ronai Z.A.;
RT "Regulation of ATG4B stability by RNF5 limits basal levels of autophagy and
RT influences susceptibility to bacterial infection.";
RL PLoS Genet. 8:e1003007-e1003007(2012).
CC -!- FUNCTION: E3 ubiquitin ligase that plays a role in the maintenance of
CC muscle cell boundaries and muscle dense bodies, which establish the
CC adhesion sites of the muscle cells to the extracellular matrix
CC (PubMed:15210732). Ubiquitinates the LIM domain protein unc-95, thereby
CC regulating its dislocalization from muscle dense bodies and weakening
CC the link between the muscle cells and the hypodermis (PubMed:20385102,
CC PubMed:15210732). Regulation of unc-95 dissociation from muscle dense
CC bodies by ubiquitination plays an important role in ecdysis during
CC molting (PubMed:20385102). Plays a role in the cessation of distal tip
CC cell migration at the end of larval morphogenesis (PubMed:22285439).
CC Acts as a negative regulator of autophagy (PubMed:23093945).
CC {ECO:0000269|PubMed:15210732, ECO:0000269|PubMed:20385102,
CC ECO:0000269|PubMed:22285439, ECO:0000269|PubMed:23093945}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:20385102};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:20385102}.
CC -!- INTERACTION:
CC Q09463; P49023: PXN; Xeno; NbExp=2; IntAct=EBI-963421, EBI-702209;
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:15210732}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:15210732}. Cell membrane
CC {ECO:0000269|PubMed:15210732}. Note=Colocalizes with deb-1/vinculin in
CC muscle dense bodies. {ECO:0000269|PubMed:15210732}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles.
CC {ECO:0000269|PubMed:15210732}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larval stages L1, L2 and L3 and in
CC adult animals with high expression during molting (at protein level).
CC {ECO:0000269|PubMed:15210732, ECO:0000269|PubMed:20385102}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown leads to disorganized
CC muscle dense bodies and abnormal muscle-muscle cell boundaries.
CC Accumulation of unc-95 in the muscle cell bodies.
CC {ECO:0000269|PubMed:15210732}.
CC -!- SIMILARITY: Belongs to the RNF5 family. {ECO:0000305}.
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DR EMBL; Z46787; CAA86745.1; -; Genomic_DNA.
DR PIR; T19328; T19328.
DR RefSeq; NP_497830.1; NM_065429.3.
DR AlphaFoldDB; Q09463; -.
DR SMR; Q09463; -.
DR BioGRID; 40769; 3.
DR IntAct; Q09463; 1.
DR STRING; 6239.C16C10.7; -.
DR EPD; Q09463; -.
DR PaxDb; Q09463; -.
DR PeptideAtlas; Q09463; -.
DR EnsemblMetazoa; C16C10.7a.1; C16C10.7a.1; WBGene00004381.
DR GeneID; 175532; -.
DR UCSC; C16C10.7; c. elegans.
DR CTD; 175532; -.
DR WormBase; C16C10.7a; CE01498; WBGene00004381; rnf-5.
DR eggNOG; KOG0823; Eukaryota.
DR GeneTree; ENSGT00390000014107; -.
DR HOGENOM; CLU_055198_2_2_1; -.
DR InParanoid; Q09463; -.
DR OMA; PLMFMLP; -.
DR OrthoDB; 1510545at2759; -.
DR PhylomeDB; Q09463; -.
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR SignaLink; Q09463; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q09463; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004381; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q09463; baseline and differential.
DR GO; GO:0030054; C:cell junction; IDA:WormBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:WormBase.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0040039; P:inductive cell migration; IMP:WormBase.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
DR GO; GO:0055002; P:striated muscle cell development; IMP:WormBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:WormBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045103; RNF5/RNF185-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12313; PTHR12313; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Membrane; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..235
FT /note="E3 ubiquitin ligase rnf-5"
FT /id="PRO_0000056046"
FT ZN_FING 26..67
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 77..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 38..235
FT /note="Missing: In tm794; irregular structure of the dense
FT bodies, aberrant muscle-muscle cell contacts and irregular
FT deb-1/vinculin localization to muscle cell contacts.
FT Increase of unc-95 localization to the muscle dense bodies.
FT Continuous distal tip cell migration in the posterior gonad
FT past the midline during adulthood. When associated with
FT RNAi-mediated knockdown of cdcc-55, increased severity of
FT the distal tip cell migration defects."
FT /evidence="ECO:0000269|PubMed:15210732,
FT ECO:0000269|PubMed:22285439"
SQ SEQUENCE 235 AA; 24915 MW; 21A04AE951F6382A CRC64;
MASETKAPSE EPTSSSNKDE SARFECNICL DAAKDAVVSL CGHLFCWPCL SQWLDTRPNN
QVCPVCKSAI DGNKVVPIYG RGGDSSDPRK KVPPRPKGQR SEPPPQSFAG FNWGGDGGMM
GGGGPNVHFS FGIGTVNGLF PLMFMLPFIQ GIFPLSFVAS FFGNGNQGAA AAGGGNGGGN
DGNDGTHAHT HGHTHGPRGH GESAAPGSRM AQEEEYLSNI FKYIGFFMLF WLLFV
