SIAH1_CAEBR
ID SIAH1_CAEBR Reviewed; 434 AA.
AC A8X679;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=E3 ubiquitin-protein ligase siah-1 {ECO:0000250|UniProtKB:Q965X6};
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 {ECO:0000250|UniProtKB:Q965X6};
GN Name=siah-1 {ECO:0000312|EMBL:CAP28140.2}; ORFNames=CBG08288;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP28140.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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|UniProtKB:P61092}.
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 {ECO:0000250|UniProtKB:P61092}.
CC -!- SUBUNIT: Interacts with tir-1. {ECO:0000250|UniProtKB:P61092}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. {ECO:0000250|UniProtKB:Q8IUQ4}.
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|UniProtKB:Q8IUQ4}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000255}.
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DR EMBL; HE601100; CAP28140.2; -; Genomic_DNA.
DR AlphaFoldDB; A8X679; -.
DR SMR; A8X679; -.
DR STRING; 6238.CBG08288; -.
DR WormBase; CBG08288a; CBP42226; WBGene00030107; Cbr-siah-1.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_028215_4_0_1; -.
DR InParanoid; A8X679; -.
DR OMA; LNTIECA; -.
DR OrthoDB; 865584at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008549; Chromosome IV.
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: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 3: Inferred from homology;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..434
FT /note="E3 ubiquitin-protein ligase siah-1"
FT /id="PRO_0000394290"
FT ZN_FING 171..206
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 223..283
FT /note="SIAH-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 27..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..415
FT /note="SBD"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT COMPBIAS 37..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
SQ SEQUENCE 434 AA; 47370 MW; E44F567FBB4D4AE4 CRC64;
MSNRKGGGGA GDYQEVIESL RRSQLIFEED ENAGPEIPTV VTSSSSASSQ RSSASQHHRL
NNMVVGGGGR DNEMSNNQNG NTPSVTIPSQ CQVMTPRISS PSSVMAPSVT VTSGTVQQGK
TFARIQGSSP SNTTHSTPTV AQAMQSVAPH IPIVGAGADD SSAEILSVFE CPVCLEYMLP
PYMQCPSGHL VCSNCRPKLQ CCPTCRGPTP SVRNLGLEKI ANTVRFPCKF SNSGCPLNFH
HIDKMDHEEL CEYRPYSCPC PGASCKWQGA LADVMDHLKK VHKSITTLQG EDIVFLATDI
NLPGAVDWVM MQSCFDYNFM LVLEKQEKYD PAQSTQMFYA VVQLIGSKKE ADNFVYRLEL
SANRRRMSWE ATPRSIHEGV AFAIQQSDCL AFDTSAAQLF AENGNLGINV TISRIDGQQR
RHPNESDAVD VEYD
