HOIL1_DANRE
ID HOIL1_DANRE Reviewed; 714 AA.
AC A9JTG5;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=zgc:175152;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) 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; BC155331; AAI55332.1; -; mRNA.
DR RefSeq; NP_001104670.1; NM_001111200.1.
DR AlphaFoldDB; A9JTG5; -.
DR SMR; A9JTG5; -.
DR STRING; 7955.ENSDARP00000078154; -.
DR PaxDb; A9JTG5; -.
DR PRIDE; A9JTG5; -.
DR Ensembl; ENSDART00000083719; ENSDARP00000078154; ENSDARG00000059871.
DR GeneID; 569903; -.
DR KEGG; dre:569903; -.
DR CTD; 569903; -.
DR ZFIN; ZDB-GENE-080220-52; shrprbck1r.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000164582; -.
DR HOGENOM; CLU_014998_1_0_1; -.
DR InParanoid; A9JTG5; -.
DR OMA; CRICYVD; -.
DR OrthoDB; 1086223at2759; -.
DR PhylomeDB; A9JTG5; -.
DR TreeFam; TF323486; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:A9JTG5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000059871; Expressed in muscle tissue and 31 other tissues.
DR ExpressionAtlas; A9JTG5; baseline and differential.
DR GO; GO:0071797; C:LUBAC complex; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:ZFIN.
DR GO; GO:0071600; P:otic vesicle morphogenesis; IMP:ZFIN.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; 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 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 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..714
FT /note="RanBP-type and C3HC4-type zinc finger-containing
FT protein 1"
FT /id="PRO_0000409509"
FT DOMAIN 225..301
FT /note="Ubiquitin-like"
FT ZN_FING 394..426
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 486..536
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 555..615
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 651..680
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..710
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ACT_SITE 664
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 489
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 509
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 580
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 595
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
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 606
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 610
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 651
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 654
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ SEQUENCE 714 AA; 78912 MW; A4748B995E29979C CRC64;
MSLSSGGWTR ASPPAQSSSS HLGHEASQSA CSTVLMSVKV SVCHSGIRPL CLPGAGDESL
RLQLSMDPGK AGEFRLALRD ISATAAGRSV FIAEFDLKTV QYEVKTPLCH ELSLATPPHD
RISFKFRCEQ EAQEWATVVM SSLREAHRVA ISSSTEEGRL PPPPLATQSK APMPRTEEIC
AELVSAIEAG DVRSASVCAS SLAKQKAALS IQPSKRNYTD SEVCLAVVVE DASSSCCVSV
KVFPHSTIGA LKQQVFSDYG FHPRVQRWVI GQSLCSDHRS LASYGVQRDG DTAFLYLISA
RQARLSRGIY QQDQESALLM VPTTHQAHQE AVSNGPAALN TASRPYSTLP TRLHNSHNTL
SNNAGGSERL GLSDIRDLIN LELPQLNEAL GPNRTSIQPG WACPTCTYIN KPTRPGCEMC
SADRPEGYTV PGNYRPDALE LRRIQQEKEA IRQYQQARET ERRENFARLV QMDGQDLVPN
PERVECRICY VELESGEGVL LRECLHCFCK ECLRSVILMS EDPQVACPYR DESYACDCVL
QEREIRALVS VDDYQHWLQR GLSVAESRCE GSYHCATADC PGWCVYEDTV NTFHCPVCKK
QNCLLCKAIH EGMNCKQYQD DLTARAINDS AARRTRDLLK TLVNSGEAMH CPQCGIIVQK
KEGCDWLRCT VCHTEICWVT RGPRWGPKGP GDISGGCRCN VNKQRCHPKC QNCH
