MIB2_CHICK
ID MIB2_CHICK Reviewed; 954 AA.
AC Q5ZIJ9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=E3 ubiquitin-protein ligase MIB2;
DE EC=2.3.2.27;
DE AltName: Full=Mind bomb homolog 2;
DE AltName: Full=RING-type E3 ubiquitin transferase MIB2 {ECO:0000305};
GN Name=MIB2; ORFNames=RCJMB04_25j24;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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. {ECO:0000250|UniProtKB:Q8R516}.
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 {ECO:0000250}.
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DR EMBL; AJ720785; CAG32444.1; -; mRNA.
DR RefSeq; NP_001006301.1; NM_001006301.1.
DR AlphaFoldDB; Q5ZIJ9; -.
DR SMR; Q5ZIJ9; -.
DR STRING; 9031.ENSGALP00000002233; -.
DR PaxDb; Q5ZIJ9; -.
DR PRIDE; Q5ZIJ9; -.
DR GeneID; 419408; -.
DR KEGG; gga:419408; -.
DR CTD; 142678; -.
DR VEuPathDB; HostDB:geneid_419408; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR InParanoid; Q5ZIJ9; -.
DR OrthoDB; 220300at2759; -.
DR PhylomeDB; Q5ZIJ9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5ZIJ9; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd02339; ZZ_Mind_bomb; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 3.30.40.10; -; 2.
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; 1.
DR Pfam; PF13857; Ank_5; 2.
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; 8.
DR SMART; SM00184; RING; 2.
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; 5.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Cytoplasm; Metal-binding; Notch signaling pathway;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..954
FT /note="E3 ubiquitin-protein ligase MIB2"
FT /id="PRO_0000055950"
FT DOMAIN 1..80
FT /note="MIB/HERC2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT DOMAIN 149..227
FT /note="MIB/HERC2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT REPEAT 464..493
FT /note="ANK 1"
FT REPEAT 497..526
FT /note="ANK 2"
FT REPEAT 530..559
FT /note="ANK 3"
FT REPEAT 563..591
FT /note="ANK 4"
FT REPEAT 597..626
FT /note="ANK 5"
FT REPEAT 631..661
FT /note="ANK 6"
FT REPEAT 665..694
FT /note="ANK 7"
FT REPEAT 698..726
FT /note="ANK 8"
FT REPEAT 766..795
FT /note="ANK 9"
FT ZN_FING 86..138
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 830..865
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 910..943
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 106
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 115
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="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ SEQUENCE 954 AA; 106340 MW; E30E00D125A34F87 CRC64;
MDLDPYASMQ VGMRVVRGVD WKWGSQDSGE GNVGTVVEIG RTGSPTTPDK TVVVQWDQGN
RTNYRTGFQG AYDLLLYDNA QIGVRHPNII CDCCKKHGIR GMRWKCKMCF DYDLCTQCYM
NNKHDLSHAF ERYETAHSQP VLVSPRQNLT RITLKGTFQG AKVVRGPDWE WGNQDGGEGK
TGRVVDIRGW DVETGRSVAS VTWSDGTTNV YRVGHKGKVD LKCTVEASGG FYYKEHLPKL
GKPAELQRKE STDRHPFQHG DKVKCLLDID ILREMQEGHG GWNPKMAEFI GQTGTVHRIT
DRGDVRVQFN SETRWTFHPG ALTKLNTFWV GDVVRVIDDM ETVKRFQPGH GEWTDEMAPT
LGHIGKVIKV YGDGDLRVSV GDQSWTFNPA CLTAYQRDEE ANLMTTENAK ESKSTLITVL
EKLLSQKTES DHAGCLVIWA ALNNAAKVRE LLQKYPDKVD NKNQGRTALQ IASYQGHLDV
VKILLQAHAT VNLRDEEGDT ALHYAAFGNQ ADVARVLMAK GAGADLLNNA KCTALYVAVS
QGFTEVVQAL CELNCDVNLP DSHGDTPLHY AITADYKVII EILTEVPNID FTVQNCQGFN
LLHYSALKGN KLAIKKILAR ARQLVDSKKE DGFTALHLAA LNNHKEVAEI LIKEGRCDVN
VKNNRNQTPL HLAIIQGHVG LVQLLVSEGS DVNAEDEDGD TAMHIALERQ QLMSVLMEKR
EGEMGSSLFS KLQASGFLGN VELNVGTAIA CYLAQEGADI NYANHRGKSP LDLITDGRIV
QIIKDFSQKF REQQVSSDCS AITCSLRRVH TTPNTMTNLS VSSVAVPTEC LVCSELALLI
HFFPCQHSIV CEECSRRMKK CIKCQVTITK KLKRDSTEVE CSPSSESTDQ RKLMEELQNR
YRQMEERITC PICIDDQIKL VFQCGHGSCP DCSTALTVCP ICRQAIRERI QIFV
