ID A0A0S3S8T7_PHAAN Unreviewed; 304 AA.
AC A0A0S3S8T7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 10-JUN-2026, entry version 51.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=Vigan.06G017400 {ECO:0000313|EMBL:BAT89260.1};
GN ORFNames=VIGAN_06017400 {ECO:0000313|EMBL:BAT89260.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT89260.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT89260.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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}.
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DR EMBL; AP015039; BAT89260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3S8T7; -.
DR OrthoDB; 100at72025; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000291084; Chromosome 6.
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-UniPathway.
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:SF111; E3 UBIQUITIN-PROTEIN LIGASE DIS1; 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:UP000291084};
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 56..92
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 109..169
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 13..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 304 AA; 34457 MW; 9CB49042F6E04CAF CRC64;
MASSNLFFDD IRSKVDVDPP QNEESTDVGE LVNDPGQTTL KPNGTVSSSV RELLECPVCL
NAMYPPIHQC SNGHTICSGC KPRVHNRCPT CRHELGNIRC LALEKVAASL ELPCKYQGFG
CIGIYPYYSK LKHESQCAYR PYNCPYAGSE CSIMGDIPYL VAHLKDDHKV DMHNGSTFNH
RYVKSNPHEV ENATWMLTVF SCFGQYFCLH FEAFQLGMAP VYIAFLRFMG DDNEAKNYSY
SLEVGGNGRK MIWQGVPRSI RDSHRKVRDS FDGLIIQRNM ALFFSGGDRK ELKLRVTGRI
WKEQ
//
