ID A0A9W7ITT9_HIBTR Unreviewed; 307 AA.
AC A0A9W7ITT9;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=HRI_003897800 {ECO:0000313|EMBL:GMJ02286.1};
OS Hibiscus trionum (Flower of an hour).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus.
OX NCBI_TaxID=183268 {ECO:0000313|EMBL:GMJ02286.1, ECO:0000313|Proteomes:UP001165190};
RN [1] {ECO:0000313|EMBL:GMJ02286.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hamamatsu line {ECO:0000313|EMBL:GMJ02286.1};
RA Koshimizu S., Masuda S., Ishii T., Shirasu K., Hoshino A., Arita M.;
RT "Genome and transcriptome analyses reveal genes involved in the formation
RT of fine ridges on petal epidermal cells in Hibiscus trionum.";
RL Submitted (MAY-2023) to the EMBL/GenBank/DDBJ databases.
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. It probably triggers the ubiquitin-mediated
CC degradation of different substrates. Mediates the proteasomal-dependent
CC degradation of ATG6, a component of the autophagosome complex. Requires
CC TRAF1A/MUSE14 and TRAF1B/MUSE13 to target ATG6 for ubiquitination and
CC subsequent regulation of autophagosome assembly. Modulates directly the
CC ubiquitination and proteasomal-dependent degradation of FREE1, a
CC component of the ESCRT-I complex. Modulates directly the ubiquitination
CC and proteasomal-dependent degradation of ELC/VPS23A, a component of the
CC ESCRT-I complex. {ECO:0000256|ARBA:ARBA00054480}.
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 -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000256|ARBA:ARBA00004419}. Endosome, multivesicular body
CC {ECO:0000256|ARBA:ARBA00004559}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000256|ARBA:ARBA00009119}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GMJ02286.1}.
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DR EMBL; BSYR01000036; GMJ02286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9W7ITT9; -.
DR OrthoDB; 941555at2759; -.
DR Proteomes; UP001165190; Unassembled WGS sequence.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-ARBA.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IEA:UniProtKB-ARBA.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd16571; RING-HC_SIAHs; 1.
DR CDD; cd03829; Sina; 1.
DR FunFam; 3.30.40.10:FF:000041; E3 ubiquitin-protein ligase SINAT3; 1.
DR FunFam; 2.60.210.10:FF:000004; E3 ubiquitin-protein ligase SINAT5-like; 1.
DR FunFam; 3.30.40.10:FF:000311; E3 ubiquitin-protein ligase SINAT5-like; 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; IPR052088; E3_ubiquitin-ligase_SINA.
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; PTHR10315; E3 UBIQUITIN PROTEIN LIGASE SIAH; 1.
DR PANTHER; PTHR10315:SF117; RING-TYPE E3 UBIQUITIN TRANSFERASE; 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 Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP001165190};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00455}.
FT DOMAIN 59..95
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 112..172
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
SQ SEQUENCE 307 AA; 34860 MW; CAF70FDE3ABC8986 CRC64;
MAPGGSACKE VVESHSPVAD YDIPSTKTES NTTTMKNAVS FVGKHGIHSN NGVYELLECP
VCTNLMYPPI HQCPNGHTLC SNCKIRVHNC CPTCRYDLGN IRCLALEKVA ESLELPCKFQ
NLGCHDIFPY YSKLKHEQHC RFRPYNCPYA GSECSVTGDI PTLVAHLKDD HKVDMHDGCT
FNHRYVKSNP HEVENATWML TVFNCFGRQF CLHFEAFQLG MAPVYMAFLR FMGDDNEAKK
FSYSLEVGAN GRKLIWQGIP RSIRDSHRKV RDSQDGLVIQ RNLALYFSGG DRQELKLRVT
GRIWKEE
//
