RN19B_XENLA
ID RN19B_XENLA Reviewed; 687 AA.
AC Q08B84; A1L3L5; Q32NH7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=E3 ubiquitin-protein ligase RNF19B;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:O60260};
DE AltName: Full=RING finger protein 19B;
GN Name=rnf19b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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=AAI24835.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC108619; AAI08620.1; -; mRNA.
DR EMBL; BC124834; AAI24835.1; ALT_INIT; mRNA.
DR EMBL; BC130177; AAI30178.1; -; mRNA.
DR AlphaFoldDB; Q08B84; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Genome assembly.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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 PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome; Repeat;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..687
FT /note="E3 ubiquitin-protein ligase RNF19B"
FT /id="PRO_0000307190"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 95..144
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 161..227
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 263..294
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 1..294
FT /note="Required for ubiquitin ligase activity and for
FT protection against staurosporin-induced cell death"
FT /evidence="ECO:0000250|UniProtKB:Q6ZMZ0"
FT REGION 53..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..313
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 618..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT CONFLICT 22
FT /note="Y -> S (in Ref. 1; AAI30178)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="Missing (in Ref. 1; AAI30178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 74541 MW; E44E752BA0BDFC6E CRC64;
MRLRNDCLVR LLTSWFGIFC LYEMTEGSAE PPPCPGARRR RLLLSLPNVF PGRTRAAPEP
SVPSPPPSPP PPPPPPVSVP PPPSSPGGSE SLIECPLCLV RQPPEEIPEL LSCRHRSCLR
CLRQYLRIEI CESRVNLRCP ECAERLSPQH VRAILRDPLL TRKYEEFLLR RCLAADPDCR
WCPAPDCGYA VIAYGCASCP KLTCEREGCR TEFCYHCKHV WHPNQTCDMA RQQRAPSLGV
RRKHPSGISY GQESGSADDM KSCPRCSAYI IKMNDGSCNH MTCSVCGCEF CWLCMKEISD
LHYLSPSGCT FWGKKPWSRK KKIIWQLSTL IGAPVGISLI AGIAIPAMVI GIPVYVGRKI
HGRFENKKTS RHKKNLAVTG GVILSVIASP VVAAVSVGIG VPIMLAYVYG VVPVSLCRGG
GCGVTTANGK GVKIDFEEDG PITVADAWRA LKNPSIGESS MEGLTSVLST SGSPTDGLSV
LQGNYSETAS FAALAGGTLT GGMLSGGRAK YCRLEVQADV QKETCQKDSV SLGAVSDSAS
TRAMAGSIIS SYNPQEREVN NMEIQVHIEA KPSRYQLMSE SSTEESLHAS APLVESEDAE
ACRNQVAACD ITLAQPESIR SDLESSDAQS DDVPDLASEE YDSPHLFPPS PSNALQESPP
HRMCAQEEGL CAHEESLSKV EIIELRV
