ID A0A2Y9SQV4_PHYMC Unreviewed; 732 AA.
AC A0A2Y9SQV4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 18-JUN-2025, entry version 32.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=RNF19B {ECO:0000313|RefSeq:XP_023981056.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023981056.1};
RN [1] {ECO:0000313|RefSeq:XP_023981056.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023981056.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
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:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily.
CC {ECO:0000256|ARBA:ARBA00061087}.
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DR RefSeq; XP_023981056.1; XM_024125288.3.
DR AlphaFoldDB; A0A2Y9SQV4; -.
DR FunCoup; A0A2Y9SQV4; 1262.
DR GeneID; 102973447; -.
DR KEGG; pcad:102973447; -.
DR InParanoid; A0A2Y9SQV4; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000248484; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20363; BRcat-RBR_RNF19B; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR CDD; cd16776; RING-HC_RBR_RNF19B; 1.
DR FunFam; 1.20.120.1750:FF:000001; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 2.20.25.20:FF:000004; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000052; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 346..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 114..336
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 118..166
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..99
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..682
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 77905 MW; D811FB1DC23384D2 CRC64;
MGSEKDSESP RSTSLHAAAP DPKCRSGGRR RRLTFHSVFS ASARGRHARA KPQAEPPPPA
APPPPAPAPA AAQAPPPEAL PAEPAAEAEA EAAATAGPGL DDEEAAEGGG SGPEEVECPL
CLVRLPPERA PRLLSCPHRS CRDCLRHYLR LEISESRVPI SCPECSERLN PHDIRLLLGD
PPLMHKYEEF MLRRYLASDP DCRWCPAPDC GYAVIAYGCA SCPKLTCERE GCQTEFCYHC
KQIWHPNQTC DMARQQRAQT LRVRTKHTSG LSYGQESGPA DDIKPCPRCS AYIIKMNDGS
CNHMTCAVCG CEFCWLCMKE ISDLHYLSPS GCTFWGKKPW SRKKKILWQL GTLIGAPVGI
SLIAGIAIPA MVIGIPVYVG RKIHSRYEGR KTSKHKRNLA ITGGVTLSVI ASPVIAAVSV
GIGVPIMLAY VYGVVPISLC RGGGCGVSTA NGKGVKIEFD EDDGPITVAD AWRALKNPSI
GESSIEGLTS VLSTSGSPTD GLSVMQGPYS ETASFAALSG GTLSGGILSS GKGKYSRLEV
QADVQKEIFP KDTASLGAIS DNASTRAMAG SIISSYNPQD RECNNMEIQV DIEAKPSHYQ
LVSGSSTEDS LHVHAQMVEN EEEGGGGSGS NEEDPPCKHQ SCEQKDCQAS RPWDISLAQP
ESIRSDLESS DTQSDDVPDI TSDECGSPHS QAAACPSTPR APGAPSPSAH MNLSAPAEGT
TVLKPEDAEA RV
//
