HOIL1_DICLA
ID HOIL1_DICLA Reviewed; 707 AA.
AC E6ZIJ1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:Q9BYM8};
DE AltName: Full=Heme-oxidized IRP2 ubiquitin ligase 1 homolog;
DE Short=HOIL-1;
DE AltName: Full=Heme-oxidized IRP2 ubiquitin transferase 1 homolog {ECO:0000305};
GN Name=rbck1; ORFNames=DLA_XVIII01330;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kuhl H., Tine M., Beck A., Timmermann B., Reinhardt R.;
RT "Chromosome directed sequencing of European seabass (Dicentrarchus labrax
RT L.) by comparatively mapped BAC clones.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the LUBAC complex which conjugates linear ('Met-
CC 1'-linked) polyubiquitin chains to substrates and plays a key role in
CC NF-kappa-B activation and regulation of inflammation (By similarity).
CC LUBAC conjugates linear polyubiquitin to ikbkg and RIPK1 and is
CC involved in activation of the canonical NF-kappa-B and the JNK
CC signaling pathways (By similarity). Linear ubiquitination mediated by
CC the LUBAC complex interferes with TNF-induced cell death and thereby
CC prevents inflammation (By similarity). LUBAC is recruited to the TNF-R1
CC signaling complex (TNF-RSC) to conjugate linear polyubiquitin to ikbkg
CC and possibly other components contributing to the stability of the
CC complex (By similarity). The LUBAC complex is also involved in innate
CC immunity by conjugating linear polyubiquitin chains at the surface of
CC bacteria invading the cytosol to form the ubiquitin coat surrounding
CC bacteria (By similarity). LUBAC is not able to initiate formation of
CC the bacterial ubiquitin coat, and can only promote formation of linear
CC polyubiquitins on pre-existing ubiquitin (By similarity). The bacterial
CC ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes
CC NF-kappa-B activation (By similarity). Binds polyubiquitin of different
CC linkage types (By similarity). {ECO:0000250|UniProtKB:Q9BYM8}.
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:Q9BYM8};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9BYM8}.
CC -!- SUBUNIT: Component of the LUBAC complex (linear ubiquitin chain
CC assembly complex). {ECO:0000250|UniProtKB:Q9BYM8}.
CC -!- DOMAIN: The RanBP2-type zinc finger, also called Npl4 zinc finger
CC (NZF), mediates binding to 'Met-1'-linked polyubiquitins.
CC {ECO:0000250|UniProtKB:Q9WUB0}.
CC -!- DOMAIN: The UBL domain mediates association with RNF31 via interaction
CC with its UBA domain. {ECO:0000250|UniProtKB:Q9BYM8}.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000305}.
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DR EMBL; FQ310508; CBN81875.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZIJ1; -.
DR SMR; E6ZIJ1; -.
DR Ensembl; ENSDLAT00005043979; ENSDLAP00005041183; ENSDLAG00005018422.
DR GeneTree; ENSGT00940000164582; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000694389; Unassembled WGS sequence.
DR GO; GO:0071797; C:LUBAC complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0097039; P:protein linear polyubiquitination; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR026261; RBCK1/SHARPIN.
DR InterPro; IPR031912; Sharpin_PH.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22770:SF43; PTHR22770:SF43; 1.
DR Pfam; PF16764; Sharpin_PH; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..707
FT /note="RanBP-type and C3HC4-type zinc finger-containing
FT protein 1"
FT /id="PRO_0000409510"
FT DOMAIN 223..286
FT /note="Ubiquitin-like"
FT ZN_FING 390..419
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 479..529
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 548..608
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 644..673
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..703
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT COMPBIAS 336..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 657
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 479
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 482
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 497
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 529
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 573
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 588
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 591
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 596
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 599
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 608
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 644
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 665
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ SEQUENCE 707 AA; 78715 MW; 87A9DC41F3791D5C CRC64;
MSLSSGGWTP TPGFTPDQSA ALPTHYGASQ SQLGCQTVLM SVRVSVCHSG IRPLCLPGAG
DESLRLQLSM DPGKSGEFRL SLQDSSGTGR SVTIAEFDLG TVNYEVKSPK CHELSLVAPP
HDRISFNFRC EQEAQEWATV VLSSLREAQR VAPQDNGPQR PLDGLNLQNT MILQRTEETC
IELTRAIEAG DMQAASAFAA TLARQHATLK IQPSAGEYED TEISLAVVVE DSSSSCCVTV
KVFPHMTTAA LKQQMFLEYG FHPRVQRWVI GQCLCTDQRS LASYGVHQDG DTAFLYLLSA
RHARLTLQVL QQDQESALLL SSPSLSLPTP PLPATSANGP SSLDQRPYTT LPPRLHTSSS
TERRNISEIK DLINLEMPQL NEALSPNTAS TQGWSCPSCT YINKPTRPGC EICSTNRPEN
YIIPGGYRPD QLELRRIQQE KEAIRQYQQA REEERRENFA RLVMMDSQDL LPNPEPVDCR
ICYMDLQPGE GVLLRECLHC FCRECLRSVI MLSEEPEVSC PYRDDTYSCA CSLQEREIRA
LVPAEEYERW LQRGLSVAES RCEGSYHCAT PDCLGWCVYE DTVNVFHCPV CRKHNCLICK
SIHEGMNCKQ YQDDLAARAI NDSAARRTTQ LLKTLVQSGE AMHCPQCGII VQKRDGCDWL
RCTVCHTEIC WVTRGPRWGP KGPGDTSGGC RCNVNNQKCH PKCQNCH
