ID A0A6P3W3D6_CLUHA Unreviewed; 1105 AA.
AC A0A6P3W3D6;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=Ankyrin repeat and IBR domain-containing protein 1 {ECO:0000256|ARBA:ARBA00069741};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=ankib1a {ECO:0000313|RefSeq:XP_012688382.2};
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_012688382.2};
RN [1] {ECO:0000313|RefSeq:XP_012688382.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC enzymes and then transfers it to substrates.
CC {ECO:0000256|ARBA:ARBA00003976}.
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 -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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DR RefSeq; XP_012688382.2; XM_012832928.3.
DR AlphaFoldDB; A0A6P3W3D6; -.
DR Ensembl; ENSCHAT00020005272; ENSCHAP00020004860; ENSCHAG00020002389.
DR GeneID; 105904963; -.
DR KEGG; char:105904963; -.
DR Proteomes; UP000515152; Chromosome 19.
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; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd20361; Rcat_RBR_ANKIB1; 1.
DR CDD; cd16774; RING-HC_RBR_ANKIB1; 1.
DR FunFam; 1.20.120.1750:FF:000003; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 1.25.40.20:FF:000040; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000129; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047564; Rcat_RBR_ANKIB1.
DR InterPro; IPR047563; RING-HC_RBR_ANKIB1.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR003903; UIM_dom.
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; PF00023; Ank; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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 REPEAT 145..177
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 330..568
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 334..380
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 293..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..984
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1081
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1105 AA; 124566 MW; E5CBA920A817FAE2 CRC64;
MGNTATKFRK ALMSGDESLA WQLYESNPQF KESLDPNASY GEPYQHNTPL HYASRHAMTR
LIRSFLFCKD GNPNKRNVHN ETSLHLLCMG PQILLAEGAL QPRLLRPLQD EQRRAECLQM
ALKWTGAKLD AGEYERADVN TADNRKSTCL HYSAAGGMKI CVELLVKSGA DLFAENEERE
TPCDCAERQQ HKELAHSLES QMVFSQDPGA QDIEAEYAAL DRREPYEGLK LQDLRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMSNAED CCQRSGVQMP TPPPSGYNAW
DTLPSPRTPR TTRSSVTSPD EISLSPAEDG LALCGICMCS ISVFEDPVDM SCGHEFCRAC
WEGFLNLKIQ EGEAHNIFCP AYDCFQLVPV EVIESVVSRE MDKRYLQFDI KAFVDNNPAI
RWCPVARCER AVRLTRPSPA SSDPLSFPLL RAPAVDCGKG HLFCWECLGD AHEPCDCETW
KLWLQKVAEM KPEELAGVNE AYEDAANCLW LLTNSKPCAN CKSPIQKNEG CNHMQCAKCK
YDFCWICLEE WKKHSSSTGG YYRCTRYEVI QQVEEQSKEM TVEAEKKHKS YQELDRFMHY
YSRYKNHEHS YQLEQRLLKT AKEKMEQLSR VFMGREGSPP DTTFIEDGVQ ELLKTRRILK
CSYPYGFFLE PKSTKKEIFE LMQTDLEMVT EDLAQKVNRP YLRTPRHKII SAACLVQQKR
REFLASVARG VAPNDSPEAP RRSFAGGTWD WEYLGFASPE EYSEFQYRRR HRQRRRGDML
SLHSLRSNTP DPNDPSDSTL DGPDGGGSRR RLNISTALGS LDEDDPNILL AIQLSLQESG
LSGDTDTQDG LSSDASLGAI GSSLPSRLDA APHALELPRA SLSSSQLLEI GDSLMRLGNI
TSQYMPPDSL RPYGDPSSAS SSIAATTVSI TDPFSPGDPD CSDPSENANL LGNIMAWFHD
MNPQKIALMS DDTDDTLPLD EAEPQWEAPE VPTTQPQDKE TEVGKDEEEL WPPCPVLEET
EGLVLERPDL LELGCMEEEC LQSPTKLSME VAATLTPPDT EGSAPPPQEE EEEEEEEEEE
KDGCHHDNTQ PTDLPSEWEE QVHLV
//
