SINA_SCHMA
ID SINA_SCHMA Reviewed; 371 AA.
AC Q86MW9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=E3 ubiquitin-protein ligase sina;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase sina {ECO:0000305};
DE AltName: Full=Seven in absentia homolog;
DE AltName: Full=SmSINA;
GN Name=SINA;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN DEGRADATION OF SMRXR1 AND SMRXR2,
RP AND TISSUE SPECIFICITY.
RX PubMed=12967711; DOI=10.1016/s0166-6851(03)00188-9;
RA Fantappie M.R., Osman A., Ericsson C., Niles E.G., LoVerde P.T.;
RT "Cloning of Schistosoma mansoni Seven in absentia (SmSINA)(+) homologue
RT cDNA, a gene involved in ubiquitination of SmRXR1 and SmRXR2.";
RL Mol. Biochem. Parasitol. 131:45-54(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. Mediates the ubiquitin-mediated degradation of
CC nuclear receptors for retinoids SmRXR1 and SmRXR2.
CC {ECO:0000269|PubMed:12967711}.
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}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Colocalizes with SmRXR1 and
CC SmRXR2 in vitelline cells. {ECO:0000269|PubMed:12967711}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY227022; AAO67521.1; -; mRNA.
DR RefSeq; XP_018646300.1; XM_018790387.1.
DR AlphaFoldDB; Q86MW9; -.
DR SMR; Q86MW9; -.
DR STRING; 6183.Smp_000650.1; -.
DR GeneID; 8343550; -.
DR KEGG; smm:Smp_000650; -.
DR CTD; 8343550; -.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_028215_0_0_1; -.
DR OMA; TSIAQFC; -.
DR OrthoDB; 780610at2759; -.
DR PhylomeDB; Q86MW9; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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..371
FT /note="E3 ubiquitin-protein ligase sina"
FT /id="PRO_0000056179"
FT ZN_FING 126..161
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 178..238
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 175..366
FT /note="SBD"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 371 AA; 40584 MW; 890D25874A6527F6 CRC64;
MNNSITEVNM SVPSRATNSN NTILSEERTC HRSQMASSDA VGRTMALLPI NHNHALHHGI
KLMPHINMPH REVGATTPLV TNSGTASTCS MSLPGSMSSA SDTVCNILPH NTSDSSSIDL
ASLFECPVCM DYALPPIMQC QSGHIVCASC RSKLSSCPTC RGNLDNIRNL AMEKLASSVL
FPCKYSTSGC PETFHYTSKS EHEAACEYRP YDCPCPGASC KWLGELEQVM PHLVHHHKSI
TTLQGEDIVF LATDISLPGA VDWVMMQSCF GHSFMLVLEK QERVPDQIFF ALVQLIGTRK
QADQFVYRLE LNGHRRRLTW EACPRSIHDG VQSAIAVSDC LVFDSNTAHS FAENGNLGIN
VTISQVSPSI S
