ID A0A8C4E4Y7_DICLA Unreviewed; 852 AA.
AC A0A8C4E4Y7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 2.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=RNF19A {ECO:0000313|Ensembl:ENSDLAP00005013839.2};
OS Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489 {ECO:0000313|Ensembl:ENSDLAP00005013839.2, ECO:0000313|Proteomes:UP000694389};
RN [1] {ECO:0000313|Ensembl:ENSDLAP00005013839.2}
RP IDENTIFICATION.
RG Ensembl;
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 Ensembl; ENSDLAT00005015084.2; ENSDLAP00005013839.2; ENSDLAG00005006890.2.
DR GeneTree; ENSGT00940000158703; -.
DR Proteomes; UP000694389; Unassembled WGS sequence.
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; cd20355; Rcat_RBR_RNF19; 1.
DR CDD; cd16775; RING-HC_RBR_RNF19A; 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; 2.
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:UP000694389};
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 339..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 106..329
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 110..158
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..483
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..669
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..788
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..843
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 90821 MW; 874A2247A847FED9 CRC64;
ILQKHQQLGG GSGGVMGSDR DLQSTASSIS LPSVKKAPKK RRLSLASLFR RRGRESKSGR
QRSRELQHTG PGGLGGVDGI ASIESIHSEM CNDKNSAFFS VAGTGALLEC PLCLLRHSRE
SFPDIMTCHH RSCIDCLRQY LRIEISESRV NISCPECSER FNPHDIRMIL GDRALMDKYE
EFMLRRWLVA DPDCRWCPAP DCGYAVIAFG CASCPKITCG REGCGTEFCY HCKQLWHPNQ
TCDAARQQRA QSLRLRTVRS SSLSYSQESG AAADDIKPCP RCAAYIIKMN DGSCNHMTCA
VCGCEFCWLC MKEISDLHYL SPSGCTFWGK KPWSRKKKIL WQLGTLVGAP VGIALIAGIA
IPAMIIGIPV YVGRKIHNRY EGKDISNHKR NLVIAGGVTL SVIVSPVVAA VTVGIGVPIM
LAYVYGVVPI SLCRSGGCGV SAGNGKGVRI EFDDENDMNV GSGAAATDTT SVADTRNNPS
IGEGSVGGLT GSLSASGSHM DRLGAIRDNL SETASTMALA GASITGSLSG SAMVNYLNRL
EVQADVQKER CSLSGESGTV SLGTISDNAS TKAMAGSILN AYMPLDRDGN SMEVQVDIES
KPGKLRHHSG SSSVDDGSHV GRCGWTCPSN GCTSSEGKGT STKWAKEASC SSSSSSGGKK
SKGKLRKKGG GGTKINETRE DMDAQLLEQR STNSSEFDSP SLSGSLPSVA DSHSSHFSEF
SCSDLESMKT SCSHGSGGGD YHTRFATVSP LPEVENDRLE TCPASSSSSS QGQGAVITPH
SPTSTTSSLG HGAELSPLCF ITEENVNLVC PAELDSHSNT RELLKETNNN HQPQHPTQTQ
QQPKNSCIQT DI
//
