RN135_RAT
ID RN135_RAT Reviewed; 415 AA.
AC Q5M929;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=E3 ubiquitin-protein ligase RNF135 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8IUD6};
DE AltName: Full=RING finger protein 135;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF135 {ECO:0000305};
GN Name=Rnf135 {ECO:0000312|RGD:1305252};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: E2-dependent E3 ubiquitin-protein ligase that functions as a
CC RIG-I/DDX58 coreceptor in the sensing of viral RNAs in cell cytoplasm
CC and the activation of the antiviral innate immune response. Together
CC with the UBE2D3, UBE2N and UB2V1 E2 ligases, catalyzes the 'Lys-63'-
CC linked polyubiquitination of RIG-I/DDX58 oligomerized on viral RNAs, an
CC essential step in the activation of the RIG-I signaling pathway.
CC Through a ubiquitin-independent parallel mechanism, which consists in
CC bridging RIG-I/DDX58 filaments forming on longer viral RNAs, further
CC activates the RIG-I signaling pathway. This second mechanism that
CC synergizes with the ubiquitin-dependent one would thereby allow an RNA
CC length-dependent regulation of the RIG-I signaling pathway. Associated
CC with the E2 ligase UBE2N, also constitutively synthesizes unanchored
CC 'Lys-63'-linked polyubiquitin chains that may also activate the RIG-I
CC signaling pathway. {ECO:0000250|UniProtKB:Q8IUD6}.
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:0000250|UniProtKB:Q8IUD6};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q8IUD6}.
CC -!- SUBUNIT: Homodimer. Interacts (homodimer) with DDX58 (double-stranded
CC RNA-bound oligomeric form); involved in both DDX58 ubiquitination,
CC oligomerization into filaments associated with viral RNAs and the
CC bridging of these filaments. Interacts with UBE2D3 and UBE2N; E2
CC ubiquitin ligases involved in RNF135-mediated ubiquitination of DDX58
CC and activation of the RIG-I signaling pathway. Interacts with PCBP2.
CC {ECO:0000250|UniProtKB:Q8IUD6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IUD6}.
CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q8IUD6}.
CC -!- DOMAIN: The B30.2/SPRY domain mediates the interaction with the
CC substrate RIG-I/DDX58. {ECO:0000250|UniProtKB:Q8IUD6}.
CC -!- DOMAIN: The coiled-coil domains mediate homodimerization and the
CC bridging of viral RNA-associated RIG-I/DDX58 filaments.
CC {ECO:0000250|UniProtKB:Q8IUD6}.
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DR EMBL; BC087718; AAH87718.1; -; mRNA.
DR RefSeq; NP_001012010.1; NM_001012010.1.
DR AlphaFoldDB; Q5M929; -.
DR SMR; Q5M929; -.
DR STRING; 10116.ENSRNOP00000005428; -.
DR PhosphoSitePlus; Q5M929; -.
DR PaxDb; Q5M929; -.
DR PRIDE; Q5M929; -.
DR Ensembl; ENSRNOT00000113280; ENSRNOP00000088068; ENSRNOG00000004093.
DR GeneID; 303350; -.
DR KEGG; rno:303350; -.
DR CTD; 84282; -.
DR RGD; 1305252; Rnf135.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000155641; -.
DR HOGENOM; CLU_032372_2_0_1; -.
DR InParanoid; Q5M929; -.
DR OrthoDB; 751018at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5M929; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISS:UniProtKB.
DR GO; GO:0039552; F:RIG-I binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0140374; P:antiviral innate immune response; ISS:UniProtKB.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; ISS:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; ISS:UniProtKB.
DR GO; GO:0039529; P:RIG-I signaling pathway; ISS:UniProtKB.
DR CDD; cd12902; SPRY_PRY_RNF135; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR042723; RNF135_SPRY_PRY_dom.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00622; SPRY; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Immunity; Innate immunity; Metal-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..415
FT /note="E3 ubiquitin-protein ligase RNF135"
FT /id="PRO_0000280559"
FT DOMAIN 228..415
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 21..67
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 181..206
FT /evidence="ECO:0000255"
SQ SEQUENCE 415 AA; 46012 MW; EE4FE96A74586AB8 CRC64;
MAAACPGTAV PVWLSEEDLS CIICQGLLDW PTTLPCGHSF CLQCLKDLWV SKRAGVDSCP
WACPICRKGP SAKPVLHKNP LLQDLVDKYR QAALELEAGP EPAPVPRSLC TPTPPQVTVQ
KSTTQVVQEL TELVGQLVDI VKSLQTQRPS LASGLDNALG ILHMDSSSEE EYPLDSPKLV
TFSASQKKIQ EILRDLEKIQ ETLQGSVTGN EAPKKQVEEM ASSVGLLPDQ RYPVSRKASQ
FSLWAISPTF DLRSLSCNLE VSNNCRMVTV SRALQPYHWS SERFSISQVL CSQAFSSGQK
YWEVDTRNCS HWAVGVASWG MKRDKMLGRT MDSWCIEWRG PSQFSAWAMM KKTDLSSGPP
EVVGVWLDLE LGKLAFYSVA DQERPLYECE VSSSSPLHPA FWLYGLTPGN YLEIL
