MIB1_XENLA
ID MIB1_XENLA Reviewed; 1011 AA.
AC Q6GNY1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=E3 ubiquitin-protein ligase mib1;
DE EC=2.3.2.27;
DE AltName: Full=Mind bomb homolog 1;
DE AltName: Full=RING-type E3 ubiquitin transferase mib1 {ECO:0000305};
GN Name=mib1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC Delta receptors, which act as ligands of Notch proteins. Positively
CC regulates the Delta-mediated Notch signaling by ubiquitinating the
CC intracellular domain of Delta, leading to endocytosis of Delta
CC receptors (By similarity). {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriolar satellite {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
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DR EMBL; BC073370; AAH73370.1; -; mRNA.
DR RefSeq; NP_001085805.1; NM_001092336.1.
DR AlphaFoldDB; Q6GNY1; -.
DR SMR; Q6GNY1; -.
DR BioGRID; 102395; 1.
DR DNASU; 444232; -.
DR GeneID; 444232; -.
DR KEGG; xla:444232; -.
DR CTD; 444232; -.
DR Xenbase; XB-GENE-1001398; mib1.L.
DR OMA; CCGGIGR; -.
DR OrthoDB; 220300at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 444232; Expressed in internal ear and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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 CDD; cd02339; ZZ_Mind_bomb; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR Gene3D; 3.30.40.10; -; 3.
DR Gene3D; 3.30.60.90; -; 1.
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 Pfam; PF12796; Ank_2; 3.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00184; RING; 3.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF159034; SSF159034; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
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; Coiled coil; Cytoplasm; Cytoskeleton; Metal-binding;
KW Notch signaling pathway; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1011
FT /note="E3 ubiquitin-protein ligase mib1"
FT /id="PRO_0000055946"
FT DOMAIN 6..74
FT /note="MIB/HERC2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT DOMAIN 143..221
FT /note="MIB/HERC2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT REPEAT 430..460
FT /note="ANK 1"
FT REPEAT 463..492
FT /note="ANK 2"
FT REPEAT 496..525
FT /note="ANK 3"
FT REPEAT 529..558
FT /note="ANK 4"
FT REPEAT 562..591
FT /note="ANK 5"
FT REPEAT 595..627
FT /note="ANK 6"
FT REPEAT 631..661
FT /note="ANK 7"
FT REPEAT 665..694
FT /note="ANK 8"
FT REPEAT 698..729
FT /note="ANK 9"
FT ZN_FING 80..132
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 820..855
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 867..902
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 964..997
FT /note="RING-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 936..963
FT /evidence="ECO:0000255"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ SEQUENCE 1011 AA; 110689 MW; AEF6140D211DD3A4 CRC64;
MSGSRNNRVM VEGVGARVAR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV VWDNGTAANY
RCSGAYDLRI MDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC AECTNYDLCT VCYHGDKHHL
RHRFYRITTP GSERVLLESR RKSKKITARG IFAGARVVRG VDWQWEDQDG GNGRRGKVTE
IQDWSASSPH SAAYVLWDNG AKNLYRVGFE GMSDLKCVQD AKGGSFYRDH CPVLGEQNGN
RNPGGLLIGD LVNIDLELEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS
GNRWTFNPAV LTKANVVRSG DAAQGAEGGT SPFQVGDLVQ ICYDIERIKL LQRGHGEWAE
AMLPTLGKVG RVQQIYSDND LKVEVCGTSW TYNPAAVSRV ASVGSAISNA TGERLSQLLK
KLFETQESGD LNEELVKAAA NGDVAKVDDL LKRQDVDVNG QCAGHTAMQA ASQNGHVDIL
KLLLKHSVDV EAEDKDGDRA VHHAAFGDEG TVIEVLQRGG ADLNARNKRR QTPLHIAVNK
GHLQVVKKLL DFSCHPSLQD SEGDTPLHDA ISKKRDDILA VLLEAGADVT ITNNNGFNAL
HHAALRGNPS AMRVLLSKLP RPWIVDEKKD DGYTALHLAA LNNHVEVAEL LVHQGSANLD
IQNVNQQTAL HLAVERQHTQ IVRLLVRAEA KLDIQDKDGD TPLHEALRHH TLSQLRQLQD
MQDVGKVDTT TWEPSKNTLI MGLGTQGAEK KSAASIACFL AANGADLAVR NKKGQSPLDL
CPDPNLCKTL AKCHKEKSSG QVGSHSPSMI NNDSETLEEC MVCSDLKRDT LFGPCGHIAT
CSLCSPRVKK CLLCKEQVQS RTKIEECVVC SDKKAAVLFQ PCGHMCACEN CASLMKKCVQ
CRAVVERRVP FVMCCSGKGT EDVADDIAGG NIPALQKDKD NTNVNADVQK LQQQLQDIKE
QTMCPVCLDR LKNMIFMCGH GTCQLCGDRM SECPICRKAI ERRILLYSMS C
