SIAH1_CAEEL
ID SIAH1_CAEEL Reviewed; 419 AA.
AC Q965X6; O46223;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=E3 ubiquitin-protein ligase siah-1;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase SIAH1 {ECO:0000305};
DE AltName: Full=Seven in absentia homolog 1;
GN Name=siah-1; ORFNames=Y37E11AR.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Holloway A.J., Bowtell D.D.L.;
RT "Cloning and characterisation of the Caenorhabditis elegans homologue of
RT Drosophila seven-in-absentia.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH TIR-1.
RX PubMed=15048112; DOI=10.1038/ni1060;
RA Couillault C., Pujol N., Reboul J., Sabatier L., Guichou J.-F., Kohara Y.,
RA Ewbank J.J.;
RT "TLR-independent control of innate immunity in Caenorhabditis elegans by
RT the TIR domain adaptor protein TIR-1, an ortholog of human SARM.";
RL Nat. Immunol. 5:488-494(2004).
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. {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with tir-1. {ECO:0000269|PubMed:15048112}.
CC -!- INTERACTION:
CC Q965X6; Q95Y80: bet-1; NbExp=2; IntAct=EBI-311877, EBI-311872;
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. {ECO:0000250}.
CC -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
CC homodimerization and the interaction with substrate proteins. It is
CC related to the TRAF family. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB94380.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U89792; AAB94380.1; ALT_SEQ; Genomic_DNA.
DR EMBL; FO081773; CCD74038.1; -; Genomic_DNA.
DR PIR; T37470; T37470.
DR RefSeq; NP_500409.1; NM_068008.3.
DR AlphaFoldDB; Q965X6; -.
DR SMR; Q965X6; -.
DR BioGRID; 42277; 15.
DR DIP; DIP-27249N; -.
DR IntAct; Q965X6; 11.
DR STRING; 6239.Y37E11AR.2; -.
DR EPD; Q965X6; -.
DR PaxDb; Q965X6; -.
DR PeptideAtlas; Q965X6; -.
DR EnsemblMetazoa; Y37E11AR.2.1; Y37E11AR.2.1; WBGene00021369.
DR GeneID; 177138; -.
DR KEGG; cel:CELE_Y37E11AR.2; -.
DR CTD; 177138; -.
DR WormBase; Y37E11AR.2; CE21549; WBGene00021369; siah-1.
DR eggNOG; KOG3002; Eukaryota.
DR GeneTree; ENSGT00940000154837; -.
DR HOGENOM; CLU_028215_4_0_1; -.
DR InParanoid; Q965X6; -.
DR OMA; LNTIECA; -.
DR OrthoDB; 865584at2759; -.
DR PhylomeDB; Q965X6; -.
DR Reactome; R-CEL-373752; Netrin-1 signaling.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q965X6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q965X6; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00021369; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR004162; SINA-like_animal.
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; PTHR45877; 1.
DR Pfam; PF03145; Sina; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..419
FT /note="E3 ubiquitin-protein ligase siah-1"
FT /id="PRO_0000056173"
FT ZN_FING 156..191
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 208..268
FT /note="SIAH-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 205..400
FT /note="SBD"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 419 AA; 45804 MW; D055CA50EF402B02 CRC64;
MSNRNGGGGG GDYQDVIESL RRTQLIFEED DNNSSDSAPQ ANHLSRHQTS NSLVEDMVNH
SNGNPPPVPP GITQQQCQIG LTPRMSASPP SAVSTISGTA VLGKTMARVQ SNPPGSIPHN
TTTTAQGIQS VAPHIPIGGG GATDDSSAEI LSVFECPVCL EYMLPPYMQC SSGHLVCSNC
RPKLQCCPTC RGPTPSVRNL GLEKIANTVR FPCKFSTSGC PLNFHHADKT EHEELCEFRP
YCCPCPGASC KWQGGLSDVM EHLKKIHKSI TTLQGEDIVF LATDINLPGA VDWVMMQSCF
DYNFMLVLEK QEKYDPAQPT QMFYAVVQLI GSKKEADNFV YRLELSASRR RMSWEATPRS
IHEGVVVAIQ QSDCLAFDSN AAQLFAENGN LGINVTISRI DTPQRRHPNE LENSDLEYD
