ID U3IT99_ANAPP Unreviewed; 958 AA.
AC U3IT99;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=MIB2 {ECO:0000313|Ensembl:ENSAPLP00000010472.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000010472.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000010472.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000010472.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; U3IT99; -.
DR STRING; 8840.ENSAPLP00000010472; -.
DR Ensembl; ENSAPLT00000011186.2; ENSAPLP00000010472.2; ENSAPLG00000010686.2.
DR GeneTree; ENSGT00940000158097; -.
DR HOGENOM; CLU_007287_2_0_1; -.
DR OMA; HDAIGKD; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000016666; Chromosome 22.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16726; RING-HC_MIB2_rpt1; 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); 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; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR PANTHER; PTHR24202:SF4; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
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; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 1..80
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 86..138
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 149..227
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 464..496
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 497..529
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 530..562
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 631..655
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 665..697
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 958 AA; 106351 MW; 91B56C5AF01EEA3E CRC64;
MDSDPYASMQ VGMRVVRGVD WKWGSQDSGE GNVGTVVEIG RTGSPTTPDK TVVVQWDQGN
RTNYRTGFQG AYDLLLYDNA QIGVRHPNII CDCCKKHGIR GMRWKCKMCF DYDLCTQCYM
NNKHDLSHSF ERYETAHSQP VVVSPRQNLT RITLKGTFQG AKVVRGPDWE WGNQDGGEGK
TGRVVDIRGW DVETGRSVAS VTWADGTTNV YRVGHKGKVD LKCTVEASGG FYYKEHLPKL
GKPAELQRKE STDRHPFQHG DKVKCLLDID ILREMQEGHG GWNPKMAEFI GQTGTVHRIT
DRGDVRVQFN SETRWTFHPG ALTKLNTFWV GDVVRVIDDM ETVKRFQPGH GEWTDEMAPT
LGHIGKVIKV YGDGDLRVSV GEQSWTFNPA CLTAYQRDEE ANLMTTENAK ESKSTLITVL
EKLLSQKTES DHAGCLVIWA ALNNVVKVRE LLQKYPDKVD SKNQGRTALQ IASYQGYLDV
VKILLQAHAT VNLRDEEGDT ALHYAAFGNQ AEVARVLISK GANGDLLNNA KCTALYVAVS
QGFAEVVQAL CELNCDVNLP DSQGDTPLHY AITADYKVII EILTEVPNID FTVQNCQGFN
LLHYSALKGN KLAIKKILAR ARQLVDSKKE DGFTALHLAA LNNHKEVAEI LIKEGRCDVN
LKNNRNQTPL HLAVIQGHVG MVQLLVSEGS DVNAEDEDGD TAMHIALERQ QLMSVMMEKR
EGEMGLSLLS TLQASGFLGN VELNIGTAIA CYLAQEGADI NYANHRGKSP LDLVTDGRIV
QIIKDFSQKF REQQVSSDCS AVTCSLRRVH TTPNTMTNLS VSSVAVPTEC LVCSELALLI
HFFPCQHSIV CEECSRRMKK CIKCQVTITK KIKQGMCAVP TVQCYVLGRG LHSICLRNVH
KEESCVLGRE KRGVPIALIT FREVLSAGMG QNQAAETGHL RKLELCPAYS VQHRVLCS
//
