ID A0A8M3B3U1_DANRE Unreviewed; 1028 AA.
AC A0A8M3B3U1;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 18-JUN-2025, entry version 17.
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_009292721.1,
GN ECO:0000313|ZFIN:ZDB-GENE-060503-156};
GN Synonyms=ankib1 {ECO:0000313|RefSeq:XP_009292721.1}, si:dkey-231l1.6
GN {ECO:0000313|RefSeq:XP_009292721.1};
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 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_009292721.1};
RN [1] {ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000313|RefSeq:XP_009292721.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_009292721.1};
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_009292721.1; XM_009294446.4.
DR GeneID; 566524; -.
DR AGR; ZFIN:ZDB-GENE-060503-156; -.
DR CTD; 566524; -.
DR ZFIN; ZDB-GENE-060503-156; ankib1a.
DR OrthoDB; 69641at2759; -.
DR Proteomes; UP000000437; 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; IPR027370; Znf-RING_euk.
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; PF12796; Ank_2; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF13445; zf-RING_UBOX; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
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 284..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 604..631
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 304..319
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..859
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1028 AA; 115583 MW; 5DA3D0A3BF6F52E8 CRC64;
MGNTATKFRK ALINGDEGLA CQLYESNPQF KEALEPNASY GEPYQHNTPL HYASRHAMTR
LIRSFLFCKD GNPNKCNVHN ETALHLLCMG PQILLGEGAL QPRFSRPQED QQKRAECLQM
ILQWTGAKLD QGEYERANVN ATDNKKSTCL HYAAAAGMKN CVELLVKNAA DLFVENEDRE
TPCDCAEKQH HKDLALSLES QMVFSQVPGA QEIEAEYAAL DRREPYEGLK LQDLRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEDWMSNAEE CCQRSGVQMP TPPPSGYNAW
DTLPSPRTPR TTRSSVTSPD EISLLSPTDG LALCGICMSS ISVFEDPVDM SCGHEFCRAC
WEGFLNLKIQ EGEAHNIFCP AYDCFQLVPV EVIESVVSRE MDKRYLQFDI KAFVDNNPAI
HWCPVARCER AVRLTRPGPG ASDPLSFPLL KAPAVDCGKG HLFCWECLGD AHEPCDCETW
KMWLQKVSEM KPEELAGVSE AYEDAANCLW LLSNSKPCAN CKSPIQKNEG CNHMQCAKCK
YDFCWICLEE WKKHSSSTGG YYRCTRYEVI QQVEEQSKEM TVEAEKKHKS FQELDRFMHY
YTRYKNHEHS YQLEERLLKT AKEKMEQLSK AFIGRDGAPP DTTFIEDGVH ELLKTRRILK
CSYPYSFFLE PKSTKKEIFE LMQTDLEMVT EDLAQKVNRP YLRTPRHKII SATYLVQQKR
REFLASVARG VAPNDSPEAP RRSFAGGTWD WEYLGFASPE EYSEFQYRRR HRQRRRGDLL
RLHSLRSNTP EPHDSSDATA ETHEGGTSQR HGISTALGSL DEDDPNILLA IQLSLQESGL
ALDPEPQDSD ASVGASGSSL PSRLDSVPQT SDPPRASMSS SELLELGDSL MRLGDISSRY
TPFNINSYPD ALGTAFSPSD PDCLDPSTNA NLLGNIMAWF HDMNPQSIAL IPSSASDAGN
ETHALGEPAK AEQTEAESAE MESKEGEVSE CVEDAKTEAS DLTVCPESSA DPQVNSLSLE
WEEEVHLV
//
