ID Q29D96_DROPS Unreviewed; 1208 AA.
AC Q29D96; A0A6I8UBW6;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC4812194 {ECO:0000313|RefSeq:XP_001353017.1};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_001353017.1};
RN [1] {ECO:0000313|RefSeq:XP_001353017.1}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_001353017.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_001353017.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_001353017.1; XM_001352981.3.
DR AlphaFoldDB; Q29D96; -.
DR SMR; Q29D96; -.
DR STRING; 46245.Q29D96; -.
DR EnsemblMetazoa; FBtr0288671; FBpp0287109; FBgn0079168.
DR GeneID; 4812194; -.
DR KEGG; dpo:4812194; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR HOGENOM; CLU_007287_1_0_1; -.
DR InParanoid; Q29D96; -.
DR OMA; CCGGIGR; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0079168; Expressed in female reproductive system and 2 other cell types or tissues.
DR ExpressionAtlas; Q29D96; baseline.
DR GO; GO:0045179; C:apical cortex; IEA:EnsemblMetazoa.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblMetazoa.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:EnsemblMetazoa.
DR GO; GO:0046331; P:lateral inhibition; IEA:EnsemblMetazoa.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0045807; P:positive regulation of endocytosis; IEA:EnsemblMetazoa.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0008104; P:protein localization; IEA:EnsemblMetazoa.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:EnsemblMetazoa.
DR GO; GO:0007423; P:sensory organ development; IEA:EnsemblMetazoa.
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; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13606; Ank_3; 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 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000001819};
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}.
FT DOMAIN 74..142
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 148..200
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 211..289
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 955..990
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1002..1037
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1165..1198
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1208 AA; 128371 MW; 2BE2F105720FC47D CRC64;
MSCAATLSAA KDTTNAANAS GAPTSGTSST AAVGVVVSSG GAGNVAAVAG GTTASTAAAG
GGASAGASSA AAVARRFSME GVGARVIRGP DWKWNKQDGG EGHVGTVRNF ESAEEVVVVW
DNGTAANYRC AGAYDLRILD SAPTGVKHEG TMCDTCRQQP IFGIRWKCAE CINYDLCSIC
YHGDKHHLRH RFYRITTPGG ERTMLEPRRK SKKVLARGIF PGARVVRGVD WQWEDQDGGV
GRRGKVNEIQ DWSSASPRSA AYVIWDNGSK NLYRVGFEGM ADLKVVNDAK GSNVYRDHLP
LLGENGPGKG PHGFQIGDKV TVDLDLEIVQ SLQHGHGGWT DGMFECLSNA GMVVGIDEDH
DIVVAYNSGN RWTFNPAVLT KVSSPTTAPP EFQVGDIVKI CSDVESIKIL QRGHGEWADA
MQLTLGKIGR VQQVYHDNDL KVEVGNTSWT YNPLAVCKVA SSTADGNCAP VIPSGERLSA
ILKKLFEPNI SGDATEEFVK AAANGFAARC EEYLAGAAAG QQPSTSSASP SAAGPDVNVN
GVFAGHTALQ AASQNGHTEV IQVLLRHAVD VEIEDKDGDR AVHHAAFGDE AAVIEILAKA
GADLNARNKR RQTSLHIAVN KGHLNVVKTL LTLGCHPSLQ DSEGDTPLHD AISKEHDEML
SLLLDFGADI TLNNNNGFNA LHHAALKGNP SAMKILLTKT NRPWIVEEKK DDGYTALHLA
ALNNHVEIAE LLVHMGKANM DRQNVNLQTA LHLAVERQHV QIVKLLVQDG ADLNIPDKDG
DTPLHEALRH HTLSQLKQLQ DVEGFGKLLM GLRNANNKKA SASIACFLAA NGADLTLKNR
KQQTPLDLCP DPNLCKTLVK CYNERKTDDS ELPGNVAGTS LNARARAAAG GGASGGGGGP
AAIMHQSSSA SLPPAPAASA SASSSSFGLN GLNSDMSQSL HVEPLKTGGT SLEECMVCSD
AKRDTVFKPC GHVSCCDTCA PRVKKCLICR ETVSSREKID ECMVCSDRRA AVFFRPCGHM
VACEHCSVLM KKCVLCRTQV DEMLSFSLCC GGIGRPEKVT SNAAVSQLIC QLPEVGEKFM
EASAIPCVNT SGHSVAMNNT VVTPVAGSSN QLNSQNNLLV AAAAASSNLA ASSGMVAPSN
VNNFQMDDVQ KLKQQLQDIK EQTMCPVCFD RIKNMVFLCG HGTCQMCGDQ IEGCPICRKT
VEKRILLF
//
