SIAH2_DANRE
ID SIAH2_DANRE Reviewed; 331 AA.
AC Q7SYL3; Q8JHZ9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 126.
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-like;
DE Short=Siah-2;
GN Name=siah2l; Synonyms=siah2, siaz; ORFNames=zgc:66284;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=12915316; DOI=10.1016/s1567-133x(03)00061-9;
RA Ro H., Kim K.E., Huh T.L., Lee S.-K., Rhee M.;
RT "Expression pattern of Siaz gene during the zebrafish embryonic
RT development.";
RL Gene Expr. Patterns 3:483-488(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DOMAIN.
RX PubMed=15055544;
RA Ro H., Jang Y., Rhee M.;
RT "The RING domain of Siaz, the zebrafish homologue of Drosophila seven in
RT absentia, is essential for cellular growth arrest.";
RL Mol. Cells 17:160-165(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. Induces cellular growth arrest by
CC inhibiting the G2/M transition (PubMed:15055544). May play a role in
CC the regulation of the cellular clock function (By similarity).
CC {ECO:0000250|UniProtKB:O43255, ECO:0000269|PubMed:15055544}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7SYL3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7SYL3-2; Sequence=VSP_010167, VSP_010168;
CC -!- TISSUE SPECIFICITY: In embryos it is expressed in all blastomeres
CC starting at the mid-blastulla. After 20 somite stage, it is expressed
CC mainly in the posterior part. Expressed in brain, including the eye,
CC the cranial cavity, otic vesicle, optic chiasm and in the gut.
CC {ECO:0000269|PubMed:12915316}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:12915316}.
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:0000269|PubMed:15055544}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000305}.
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DR EMBL; AF411696; AAN03677.1; -; mRNA.
DR EMBL; BC054674; AAH54674.1; -; mRNA.
DR AlphaFoldDB; Q7SYL3; -.
DR SMR; Q7SYL3; -.
DR STRING; 7955.ENSDARP00000065168; -.
DR PaxDb; Q7SYL3; -.
DR ZFIN; ZDB-GENE-030922-1; siah2l.
DR eggNOG; KOG3002; Eukaryota.
DR InParanoid; Q7SYL3; -.
DR PhylomeDB; Q7SYL3; -.
DR Reactome; R-DRE-373752; Netrin-1 signaling.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q7SYL3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; -; 1.
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 Alternative splicing; Biological rhythms; Cell cycle; Metal-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..331
FT /note="E3 ubiquitin-protein ligase Siah2"
FT /id="PRO_0000056171"
FT ZN_FING 89..124
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 142..202
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..331
FT /note="SBD"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 197..208
FT /note="LMHAHKSITTLQ -> HVQSMTVLQRPS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010167"
FT VAR_SEQ 209..331
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010168"
FT CONFLICT 34
FT /note="Missing (in Ref. 2; AAH54674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 34494 MW; 10594890BF60F4B2 CRC64;
MSRPSSAGGA AGGLGAGKAG GSKHGGSGGT TASAAAAAAA AAAAAAAAAA AAGVSGSVAG
SGTVPAAAVA LPVAALPGQS PELTALFECP VCFDYVLPPI LQCQAGHLVC NQCRQKLSCC
PTCRGPLTPS IRNLAMEKVA STLPFPCKYS SAGCLLSLHH SEKPEHEEVC EFRPYTCPCP
GASCKWQGSL EEVMPHLMHA HKSITTLQGE DIVFLATDIN LPGAVDWVMM QSCFGHHFML
VLEKQEKYEG HQQFFAIVLL IGTRKQAENF AYRLELNGNR RRLTWEATPR SIHDGVAAAI
MNSDCLVFDT SIAHLFADNG NLGINVTISM C
