ID W5U9X3_ICTPU Unreviewed; 1030 AA.
AC W5U9X3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=mib1 {ECO:0000313|EMBL:AHH38733.1,
GN ECO:0000313|RefSeq:XP_017351008.2};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH38733.1};
RN [1] {ECO:0000313|EMBL:AHH38733.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed {ECO:0000313|EMBL:AHH38733.1};
RX PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA Peatman E., Liu Z.;
RT "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT Seq analysis of a doubled haploid homozygote.";
RL BMC Genomics 13:595-595(2012).
RN [2] {ECO:0000313|RefSeq:XP_017351008.2}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017351008.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; JT409568; AHH38733.1; -; mRNA.
DR RefSeq; XP_017351008.1; XM_017495519.1.
DR RefSeq; XP_017351008.2; XM_017495519.3.
DR GeneID; 108280494; -.
DR KEGG; ipu:108280494; -.
DR CTD; 57534; -.
DR OrthoDB; 45541at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000221080; Chromosome 20.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16724; RING-HC_MIB1_rpt1; 1.
DR CDD; cd16725; RING-HC_MIB1_rpt2; 1.
DR CDD; cd16727; RING-HC_MIB1_rpt3; 1.
DR CDD; cd02339; ZZ_Mind_bomb; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR042056; MIB1/2_ZZ.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR040847; SH3_15.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR24202:SF53; E3 UBIQUITIN-PROTEIN LIGASE MIB1-RELATED; 1.
DR PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 3.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00184; RING; 3.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 6.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 3.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 2: Evidence at transcript level;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
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:PRU00228}.
FT DOMAIN 6..74
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 80..132
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 143..221
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 463..495
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 496..528
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 529..561
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 562..594
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 631..656
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 665..697
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 817..852
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 864..899
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 987..1020
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1030 AA; 112645 MW; 9D372F69A99DF2FE CRC64;
MSSGRNNRVM MEGVGARVIR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV VWDNGTAANY
RCSGAYDVRI LDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC AECTNYDLCT TCYHGDKHHL
RHRFYRITTP GSERVLLESR RKSKKITARG IFTGGRVVRG VDWQWEDQDG GNGRRGKVTE
IQDWSAASPH SAAYVLWDNG AKNLYRVGFE GMSDLKCVQD AKGGTFYRDH CPVLGEQNGN
RNPGGLQIGD LVNIDLDLEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS
GNRWTFNPAV LTKANVARSG EVPAGAEGGS SQFMVGDLVQ ICYDIDRIKL LQRGHGEWAE
AMLPTLGKMG RVQQIYSDSD LKVEVCGTSW TYNPAAVTKV APAGSAITNA SGERLSQLLK
KLFETQESGD INEELVKAAA NGDLAKVEDI LKRPDVDVNG QCAGHTAMQA ASQNGHVDVL
KLLLKHNVDL EAEDKDGDRA VHHAAFGDEG SVIEVLHRGG ADLNARNKRR QTPLHIAVNK
GHLQVVKTLL DFGCHPSLQD SEGDTPLHDA ISKKRDDMLS VLLEAGADVT ITNNNGFNAL
HHAALRGNPS AMRVLLSKLP RPWIVDEKKD DGYTALHLAA LNNHVEVAEL LVHQGSASLD
VQNVNQQTAL HLAVERQHTQ IVRLLVRAEA KLDVQDKDGD TPLHEALRHH TLSQLRQLQD
MQDVSKVEPW EPSKNTLIMG LGTQGAEKKS AASIACFLAA NGADLTIRNK KGQSPLDLCP
DPSLCKALAK CHKEKTSGQV GSRSPSLNSN NETLEECMVC SDMKRDTLFG PCGHIATCSL
CSPRVKKCLI CKDQVQSRTK IEECVVCSDK KAAVLFQPCG HMCACENCAS LMKKCVQCRA
VVERRTPFVL CCGGKGMEDA TDDEDLTGGS NSVAGGSQDL LQPNNLALSW SSGNIPALQR
DKDNTNVNAD VQKLQQQLQD IKEQTMCPVC LDRLKNMIFM CGHGTCQLCG DRMSECPICR
KAIERRILLY
//
