RN19B_MOUSE
ID RN19B_MOUSE Reviewed; 732 AA.
AC A2A7Q9; A0AUN9; Q7TT05;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=E3 ubiquitin-protein ligase RNF19B;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:O60260};
DE AltName: Full=IBR domain-containing protein 3;
DE AltName: Full=Natural killer lytic-associated molecule;
DE AltName: Full=RING finger protein 19B;
GN Name=Rnf19b; Synonyms=Ibrdc3, Nklam;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY CYTOKINES.
RX PubMed=10912506; DOI=10.1007/s002510000182;
RA Portis T., Anderson J., Esposito A., Kornbluth J.;
RT "Gene structure of human and mouse NKLAM, a gene associated with cellular
RT cytotoxicity.";
RL Immunogenetics 51:546-555(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-732.
RC STRAIN=Czech II; TISSUE=Lung;
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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=27485036; DOI=10.1038/srep30955;
RA Kaneko M., Iwase I., Yamasaki Y., Takai T., Wu Y., Kanemoto S.,
RA Matsuhisa K., Asada R., Okuma Y., Watanabe T., Imaizumi K., Nomura Y.;
RT "Genome-wide identification and gene expression profiling of ubiquitin
RT ligases for endoplasmic reticulum protein degradation.";
RL Sci. Rep. 6:30955-30955(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2
CC ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a
CC thioester and then directly transfers the ubiquitin to targeted
CC substrates, such as UCKL1. Involved in the cytolytic activity of
CC natural killer cells and cytotoxic T-cells. Protects against
CC staurosporin-induced cell death (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZMZ0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:O60260};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with UBE2L3, UBE2L6 and UCKL1.
CC {ECO:0000250|UniProtKB:Q6ZMZ0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane
CC {ECO:0000250|UniProtKB:Q6ZMZ0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q6ZMZ0}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q6ZMZ0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q6ZMZ0}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in natural killer cells,
CC activated macrophages and cytotoxic T-cells (PubMed:10912506). Present
CC in macrophages (at protein level) (PubMed:10912506). Ubiquitously
CC expressed with high expression in testis (PubMed:27485036).
CC {ECO:0000269|PubMed:10912506, ECO:0000269|PubMed:27485036}.
CC -!- INDUCTION: By IFNG and LPS in macrophages. By IL2 in natural killer
CC cells and cytotoxic T-cells. {ECO:0000269|PubMed:10912506}.
CC -!- DOMAIN: The first IBR-type zinc finger is the most crucial for
CC interaction with UBE2L3, UBE2L6 and UCKL1.
CC {ECO:0000250|UniProtKB:Q6ZMZ0}.
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC type E3 enzymes: they bind E2s via the first RING domain, but require
CC an obligate trans-thiolation step during the ubiquitin transfer,
CC requiring a conserved cysteine residue in the second RING domain.
CC {ECO:0000250|UniProtKB:O60260}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52529.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM19707.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL606977; CAM19707.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC052529; AAH52529.1; ALT_INIT; mRNA.
DR EMBL; BC117807; AAI17808.1; -; mRNA.
DR CCDS; CCDS89829.1; -.
DR RefSeq; XP_006503521.1; XM_006503458.3.
DR AlphaFoldDB; A2A7Q9; -.
DR BioGRID; 217322; 2.
DR STRING; 10090.ENSMUSP00000030584; -.
DR iPTMnet; A2A7Q9; -.
DR PhosphoSitePlus; A2A7Q9; -.
DR PaxDb; A2A7Q9; -.
DR PRIDE; A2A7Q9; -.
DR ProteomicsDB; 300537; -.
DR Antibodypedia; 57831; 117 antibodies from 15 providers.
DR Ensembl; ENSMUST00000030584; ENSMUSP00000030584; ENSMUSG00000028793.
DR UCSC; uc008uvx.2; mouse.
DR MGI; MGI:1922484; Rnf19b.
DR VEuPathDB; HostDB:ENSMUSG00000028793; -.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000158451; -.
DR InParanoid; A2A7Q9; -.
DR OMA; LPDRDCT; -.
DR OrthoDB; 257621at2759; -.
DR PhylomeDB; A2A7Q9; -.
DR TreeFam; TF324777; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 75234; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Rnf19b; mouse.
DR PRO; PR:A2A7Q9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2A7Q9; protein.
DR Bgee; ENSMUSG00000028793; Expressed in seminiferous tubule of testis and 234 other tissues.
DR ExpressionAtlas; A2A7Q9; baseline and differential.
DR Genevisible; A2A7Q9; MM.
DR GO; GO:0044194; C:cytolytic granule; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Endoplasmic reticulum; Immunity; Membrane;
KW Metal-binding; Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..732
FT /note="E3 ubiquitin-protein ligase RNF19B"
FT /id="PRO_0000307188"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 116..165
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 183..248
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 284..315
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 1..315
FT /note="Required for ubiquitin ligase activity and for
FT protection against staurosporin-induced cell death"
FT /evidence="ECO:0000250|UniProtKB:Q6ZMZ0"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..334
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 598..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT CONFLICT 278
FT /note="Missing (in Ref. 1 and 3; AAI17808)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="Q -> P (in Ref. 3; AAH52529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 78127 MW; 81AAF64F9AE566F7 CRC64;
MGSEKDSESP RSTSLHAAAP DPKCRSGGRR RRLTFHSVFS ASARGRRART KPQAEPPPPA
APPPPPPPAP APVEAQAPPV EALPSEPAAE AEAEAVAAGP EEDEAAEGGG AEEVECPLCL
VRLPPERAPR LLSCPHRSCR DCLRHYLRLE ISESRVPISC PECSERLNPH DIRLLLADPP
LMHKYEEFML RRYLASDPDC RWCPAPDCGY AVIAYGCASC PKLTCEREGC QTEFCYHCKQ
IWHPNQTCDM ARQQRAQTLR VRTKHTSGLS YGQESGPADD IKPCPRCSAY IIKMNDGSCN
HMTCAVCGCE FCWLCMKEIS DLHYLSPSGC TFWGKKPWSR KKKILWQLGT LIGAPVGISL
IAGIAIPAMV IGIPVYVGRK IHSRYEGRKT SKHKRNLAIT GGVTLSVIAS PVIAAVSVGI
GVPIMLAYVY GVVPISLCRG GGCGVSTANG KGVKIEFDED DGPITVADAW RALKNPSIGE
SSIEGLTSVL STSGSPTDGL SVMQGPYSET ASFAALSGGT LSGGILSSGK GKYSRLEVQA
DVQKEIFPKD TASLGAISDS ASTRAMAGSI ISSYNPQDRE CNNMEIQVDI EAKPSHYQLV
SGSSTEDSLH VHAQVAEKEE EGNGAGGGSG GSEDDPPYKH QSCEQKDCLA SKAWDISLAQ
PESIRSDLES SDTQSDDVPD ITSDECGSPR SHAAACPSTP QVHGAPSPSA HKNLAAPAEG
QTVLKSEEYE VE
