SIAH2_XENLA
ID SIAH2_XENLA Reviewed; 313 AA.
AC Q9I8X5;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=E3 ubiquitin-protein ligase siah2;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase SIAH2 {ECO:0000305};
DE AltName: Full=Seven in absentia homolog 2;
DE AltName: Full=Xsiah-2;
GN Name=siah2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11335112; DOI=10.1016/s0925-4773(01)00332-x;
RA Bogdan S., Senkel S., Esser F., Ryffel G.U., Pogge von Strandmann E.;
RT "Misexpression of Xsiah-2 induces a small eye phenotype in Xenopus.";
RL Mech. Dev. 103:61-69(2001).
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. Involved in eye morphogenesis, probably triggers
CC the ubiquitin-mediated degradation of different substrates
CC (PubMed:11335112). May play a role in the regulation of the cellular
CC clock function (By similarity). {ECO:0000250|UniProtKB:O43255,
CC ECO:0000269|PubMed:11335112}.
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: Homodimer. {ECO:0000250|UniProtKB:O43255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11335112}.
CC -!- TISSUE SPECIFICITY: Widely expressed in early embryos until stage 40.
CC It is then expressed in brain, spinal cord and in the developing and
CC mature eye. {ECO:0000269|PubMed:11335112}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:11335112}.
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}.
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DR EMBL; AF155509; AAF80255.1; -; mRNA.
DR RefSeq; NP_001079089.1; NM_001085620.1.
DR AlphaFoldDB; Q9I8X5; -.
DR SMR; Q9I8X5; -.
DR GeneID; 373622; -.
DR KEGG; xla:373622; -.
DR CTD; 373622; -.
DR Xenbase; XB-GENE-1004954; siah2.L.
DR OMA; NKPCGKQ; -.
DR OrthoDB; 780610at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 373622; Expressed in zone of skin and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Biological rhythms; Cytoplasm; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..313
FT /note="E3 ubiquitin-protein ligase siah2"
FT /id="PRO_0000056172"
FT ZN_FING 69..104
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 122..182
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..311
FT /note="SBD"
FT COMPBIAS 16..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 313 AA; 34099 MW; 9CF9C291C49B19EB CRC64;
MSRPSSAGPC ASKPCGKQKQ PPPPPPHAPS LPATISGGPG ASAPPAPTAA AITGPLSQQH
QELTSLFECP VCFDYVLPPI LQCQAGHLVC NQCRQKLSCC PTCRASLTPS IRNLAMEKVA
SAVLFPCKYA STGCSLSLHH TEKPEHEDIC EYRPYSCPCP GASCKWQGSL ENVMQHLTHS
HKSITTLQGE DIVFLATDIN LPGAVDWVMM QYCFNHHFML VLEKQEKYEG HQQFFAIVLL
IGTRKQAENY AYRLELNGNR RRLTWEATPR SIHDGVAAAI MNSDCLVFDT AIAHLFADNG
NLGINVTIST CCP
