ID A0A9N9SR48_DIABA Unreviewed; 291 AA.
AC A0A9N9SR48;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
GN ORFNames=DIABBA_LOCUS2670 {ECO:0000313|EMBL:CAG9828771.1};
OS Diabrotica balteata (Banded cucumber beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Galerucinae; Diabroticina; Diabroticites;
OC Diabrotica.
OX NCBI_TaxID=107213 {ECO:0000313|EMBL:CAG9828771.1, ECO:0000313|Proteomes:UP001153709};
RN [1] {ECO:0000313|EMBL:CAG9828771.1}
RP NUCLEOTIDE SEQUENCE.
RA King R.;
RL Submitted (JAN-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that is required for
CC specification of R7 photoreceptor cell fate in the eye by mediating the
CC ubiquitination and subsequent proteasomal degradation of Tramtrack
CC (ttk). E3 Ubiquitin ligases accept ubiquitin from an E2 ubiquitin-
CC conjugating enzyme in the form of a thioester and then directly
CC transfers the ubiquitin to targeted substrates. Acts via the formation
CC of a complex with ebi and phyl that ubiquitinates the transcription
CC repressor ttk, a general inhibitor of photoreceptor differentiation, in
CC a subset of photoreceptor cells in the eye, leading to the
CC differentiation of cells into neurons. Also involved in external
CC sensory organ development. {ECO:0000256|ARBA:ARBA00060311}.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates. {ECO:0000256|RuleBase:RU201113}.
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 ECO:0000256|RuleBase:RU201113};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU201113}.
CC -!- SUBUNIT: Component of some E3 complex at least composed of sina, ebi
CC and phyl. Interacts with eff. {ECO:0000256|ARBA:ARBA00062579}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. {ECO:0000256|RuleBase:RU201113}.
CC -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
CC interaction with substrate proteins. It is related to the TRAF family.
CC {ECO:0000256|RuleBase:RU201113}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000256|ARBA:ARBA00009119, ECO:0000256|RuleBase:RU201113}.
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DR EMBL; OU898285; CAG9828771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9N9SR48; -.
DR OrthoDB; 941555at2759; -.
DR Proteomes; UP001153709; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-ARBA.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd03829; Sina; 1.
DR FunFam; 2.60.210.10:FF:000002; E3 ubiquitin-protein ligase; 1.
DR FunFam; 3.30.40.10:FF:000041; E3 ubiquitin-protein ligase SINAT3; 1.
DR Gene3D; 2.60.210.10; Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2, Chain A; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR004162; SINA-like_animal.
DR InterPro; IPR049548; Sina-like_RING.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR45877; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR PANTHER; PTHR45877:SF2; E3 UBIQUITIN-PROTEIN LIGASE SINA-RELATED; 1.
DR Pfam; PF21362; Sina_RING; 1.
DR Pfam; PF03145; Sina_TRAF; 1.
DR Pfam; PF21361; Sina_ZnF; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU201113};
KW Reference proteome {ECO:0000313|Proteomes:UP001153709};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU201113}; Vision {ECO:0000256|ARBA:ARBA00023305};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU201113};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00455}.
FT DOMAIN 49..84
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 101..161
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 291 AA; 31817 MW; C8A953457353F85A CRC64;
MAQVVSQKRG RGLGTGETSS ASSSSTNQLS ALSTAPGTLT DELAALFECP VCFEVVLPPI
MQCQVGHLVC ASCRPKLSCC PTCRGTLGNI RNLAMEKVAN NLMFPCKHKS TGCRMTLGLN
EKAEHEEICE FRPYSCPCPG ASCSWQGQLD KVMVHLQHAH KNITTLNGED IVFLATEINL
AGAVDWVMMQ SCFGHHFMLV LEKQEKNDGH TQFFAIVQLI GSRKQAEHFA YRLELNGNRR
RLIWEAMPRS SHEGVASAIM GSDCLVFDNS IAQHFADNGN LGINVTISLV C
//
