ID F7IDR9_CALJA Unreviewed; 610 AA.
AC F7IDR9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1 {ECO:0000256|ARBA:ARBA00017887};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=RBCK1 {ECO:0000313|Ensembl:ENSCJAP00000038780.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000038780.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000038780.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000038780.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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DR AlphaFoldDB; F7IDR9; -.
DR STRING; 9483.ENSCJAP00000038780; -.
DR Ensembl; ENSCJAT00000040965.4; ENSCJAP00000038780.3; ENSCJAG00000020846.5.
DR GeneTree; ENSGT00940000161130; -.
DR HOGENOM; CLU_1269488_0_0_1; -.
DR InParanoid; F7IDR9; -.
DR OMA; CRCRMNG; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008225; Chromosome 5.
DR Bgee; ENSCJAG00000020846; Expressed in ovary and 6 other cell types or tissues.
DR GO; GO:0071797; C:LUBAC complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:1990757; F:ubiquitin ligase activator activity; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0097039; P:protein linear polyubiquitination; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR CDD; cd20345; BRcat_RBR_HOIL1; 1.
DR CDD; cd16633; mRING-HC-C3HC3D_RBR_HOIL1; 1.
DR CDD; cd20358; Rcat_RBR_HOIL1; 1.
DR CDD; cd01799; Ubl_HOIL1; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR047558; BRcat_RBR_HOIL1.
DR InterPro; IPR047559; HOIL1_RBR_mRING-HC-C3HC3D.
DR InterPro; IPR047557; Rcat_RBR_HOIL1.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR027370; Znf-RING_euk.
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:SF35; RANBP-TYPE AND C3HC4-TYPE ZINC FINGER-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
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:PRU00322}.
FT DOMAIN 155..222
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 297..322
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 378..606
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 382..424
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..360
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 32..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 67743 MW; 03B0AEF80571BBD0 CRC64;
MLGWAGAGLA GHAPNQSPAA QRCGSRCPPS GDPAPAQGPA PAPGSAQPAY RPRPSPRLRP
TRLPAPPPGA ALQRDRQGDP EVAFPRSHGP PPGGWAQPRQ MDEKTKKAEE MALSLTRAVA
GGDEQVAMKC AIWLAEQRVP LSVQLKPEAS PTQDIRLWVS VEDAQLHAVT IWLTVRPDMT
VASLKDMVFL DYGFPPVLQQ WVIGQRLARD QETLHSHGVR QNGDSAYLYL LSARNTSLNP
QELQRERQLR MLEDLGFKDL TLQPRGPLEP VTPKPGVPQE LGRGQPDAVP EPPPVGWQCP
GCTFINKPTR PGCEMCCRAR PEAYQVPASY QPDEEERARL AGEEESLRQY QQRKQKQQEG
NYLQHVQLDQ RSLVLNTEPA ECPVCYSVLA PGEAVVLREC LHTFCRECLQ GTIRNSQEAE
VSCPFIDNTY SCSGKLLERE IKALLTAEDY QRFLDLGISI AENRSAFSYH CKTPDCKGWC
FFEDDVNEFT CPVCFHVNCL LCKAIHEQMN CKEYQEDLAL RAQNDVAARQ TTEMLKVMLQ
QGEAMRCPQC QIVVQKKDGC DWIRCTVCHT EICWVTKGPR WGPGGPGDTS GGCRCRVNGI
PCHPSCQNCH
//
