ID   A0A3Q7UIN5_VULVU        Unreviewed;       267 AA.
AC   A0A3Q7UIN5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
GN   Name=SIAH3 {ECO:0000313|RefSeq:XP_025873037.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025873037.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025873037.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025873037.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025873037.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU201113};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|RuleBase:RU201113}.
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   RefSeq; XP_025873037.1; XM_026017252.1.
DR   AlphaFoldDB; A0A3Q7UIN5; -.
DR   STRING; 9627.ENSVVUP00000039879; -.
DR   Ensembl; ENSVVUT00000052171; ENSVVUP00000039879; ENSVVUG00000028402.
DR   KEGG; vvp:112933928; -.
DR   OMA; AQVTPCM; -.
DR   OrthoDB; 222086at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03829; Sina; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR   InterPro; IPR004162; SINA-like_animal.
DR   InterPro; IPR008974; TRAF-like.
DR   PANTHER; PTHR45877; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR   PANTHER; PTHR45877:SF5; SEVEN IN ABSENTIA HOMOLOG 3; 1.
DR   Pfam; PF03145; Sina_TRAF; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU201113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU201113};
KW   Zinc {ECO:0000256|RuleBase:RU201113};
KW   Zinc-finger {ECO:0000256|RuleBase:RU201113}.
FT   DOMAIN          159..253
FT                   /note="Seven-in-absentia protein TRAF-like"
FT                   /evidence="ECO:0000259|Pfam:PF03145"
SQ   SEQUENCE   267 AA;  30502 MW;  2C184247B8B78349 CRC64;
     MLFFTQCFGA VLDLIHLRFQ HYKARRVFSA AGQLVCVVNP THNLKYVSSR RTVTQSAPEQ
     GNFPPHHLTH HHRHHRPHHH LRHHARPHHL HHQEAGLHAA QVTPCMCPLF SCQWEGHLEV
     VVPHLRQMHR VDILQGAEIV FLATDMHLPA PADWIIMHSC LGHHFLLVLR KQERHEGHPQ
     FFATMMLIGT PTQADCFTYR LELNRNHRRL KWEATPRSVL ECVDSVITDG DCLVLNTSLA
     QLFSDNGSLA IGIAITATEV CSSEAEM
//