ID A0A6P8F2J8_CLUHA Unreviewed; 877 AA.
AC A0A6P8F2J8;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE SubName: Full=Uncharacterized protein si:dkey-181m9.8 isoform X2 {ECO:0000313|RefSeq:XP_031419004.1};
GN Name=si:dkey-181m9.8 {ECO:0000313|RefSeq:XP_031419004.1};
OS Clupea harengus (Atlantic herring).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Clupei; Clupeiformes; Clupeoidei;
OC Clupeidae; Clupea.
OX NCBI_TaxID=7950 {ECO:0000313|Proteomes:UP000515152, ECO:0000313|RefSeq:XP_031419004.1};
RN [1] {ECO:0000313|RefSeq:XP_031419004.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
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DR RefSeq; XP_031419004.1; XM_031563144.2.
DR AlphaFoldDB; A0A6P8F2J8; -.
DR GeneID; 105900621; -.
DR Proteomes; UP000515152; Chromosome 25.
DR GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR GO; GO:1990450; F:linear polyubiquitin binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097039; P:protein linear polyubiquitination; IEA:TreeGrafter.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR CDD; cd20337; BRcat_RBR_HOIP; 1.
DR CDD; cd16631; mRING-HC-C4C4_RBR_HOIP; 1.
DR CDD; cd20351; Rcat_RBR_HOIP; 1.
DR CDD; cd11685; UEV_TSG101-like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047540; BRcat_RBR_RNF31-like.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR057051; PARP14_RPM_1.
DR InterPro; IPR047542; Rcat_RBR_RNF31-like.
DR InterPro; IPR026254; RNF31-like.
DR InterPro; IPR041031; RNF31_C.
DR InterPro; IPR047541; RNF31_RBR_mRING-HC-like.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR008883; UEV_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16004:SF3; E3 UBIQUITIN-PROTEIN LIGASE RNF31; 1.
DR PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR Pfam; PF18091; E3_UbLigase_RBR; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF23222; RRM_PARP14_1; 1.
DR Pfam; PF05743; UEV; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS51322; UEV; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000515152};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 DOMAIN 5..149
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT DOMAIN 455..692
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 459..508
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 175..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..856
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 99105 MW; 70D18F111464385D CRC64;
MARVTAGQEY DTLAECNYCS PNEVLADVRS ATATYTDLNL HVDFYCYPNN EKKKLVYLGG
TIPVVYEGNV YNIPIRIWIH ETHPKSPPKC SVCPSVFMVI NAKSSFVDAS GHVHLHCLNN
WKIGWSSLSI VLEEMRAAFQ RETPLFTAFP VGSVTLSTPP LPPLPGSADA NASPYDSWPY
SDSMSSQQNT SDLNRMSSSC AVQPDSNTLP KSSKSSQSLA TREPVSVVRR SYTQELLDMG
ITFEEPVVRT HHPTNPFLSS ASVPNITPSN VEDVDNLFKS LQLEKVVNIY QLGTKDTDIN
EAWERPGFGE QPHEVAGLLD DTHTVVIDHL PRGVSPSRMK NKLTIYFQRK HNGGGEVVDV
TYPTAHPDQA YVTFRNRRDV RQVLRQPSRA IAVNEQQFPI QVKKFDRSQV PEGIVGEKAA
MFKSLLTMEG HTFSPTDVLE AVQACRDLPS ALKYLSHECP ICQEQVCFSK IITMTHCSCA
FCESCFKAYF SSVIKEKSIV HAVCPLCNHP DVRGAQCLEE SVEYFSLLDT QIRHYLDPET
YELFQRKLRD RALQEMPNFR WCAHCCFGLL HEAERLRMDC PSCGKSTCFK CKSAWAPQHE
GLSCEKFKEW QLHNSPEYQN TRLEHLMSRN KIDCPKCKFR FYLSKGGCLH FKCTQCQHEF
CGGCGRPFKL GSACGFSAEC SAKGLHAHHP RDCLYHLRDW SVHRLQRLLQ LHRVSLPLLI
RHKHGAAGRD WRGVCGVLEH KESGATKDEP CGRPALQEDN GYCSFHYKEC LVELVNQKHL
DPALLFDIQE MVAELQRWRV RFPQQQPQES DQLYRERLRK ILTETVGLST GALGRSKRME
PSSSSPSISV RNPWSSPQAS PARGLSEDSQ LLLLLND
//
