ID SYVNB_XENLA Reviewed; 595 AA.
AC Q5XHH7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=E3 ubiquitin-protein ligase synoviolin B;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q86TM6};
DE AltName: Full=RING-type E3 ubiquitin transferase synoviolin B {ECO:0000305};
DE AltName: Full=Synovial apoptosis inhibitor 1-B;
GN Name=syvn1-b; Synonyms=hrd1-b;
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin
CC specifically from endoplasmic reticulum-associated UBC7 E2 ligase and
CC transfers it to substrates, promoting their degradation. Component of
CC the endoplasmic reticulum quality control (ERQC) system also called ER-
CC associated degradation (ERAD) involved in ubiquitin-dependent
CC degradation of misfolded endoplasmic reticulum proteins. Also promotes
CC the degradation of normal but naturally short-lived proteins. Protects
CC cells from ER stress-induced apoptosis. Sequesters p53 in the cytoplasm
CC and promotes its degradation, thereby negatively regulating its
CC biological function in transcription, cell cycle regulation and
CC apoptosis (By similarity). {ECO:0000250|UniProtKB:Q86TM6}.
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; Evidence={ECO:0000250|UniProtKB:Q86TM6};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q86TM6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86TM6}.
CC -!- DOMAIN: The RING-type zinc finger is required for E3 ligase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HRD1 family. {ECO:0000305}.
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DR EMBL; BC084080; AAH84080.1; -; mRNA.
DR RefSeq; NP_001088172.1; NM_001094703.1.
DR AlphaFoldDB; Q5XHH7; -.
DR SMR; Q5XHH7; -.
DR DNASU; 494996; -.
DR GeneID; 494996; -.
DR KEGG; xla:494996; -.
DR AGR; Xenbase:XB-GENE-6254740; -.
DR CTD; 494996; -.
DR Xenbase; XB-GENE-6254740; syvn1.S.
DR OrthoDB; 2912447at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 494996; Expressed in testis and 20 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd16479; RING-H2_synoviolin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22763:SF194; E3 UBIQUITIN-PROTEIN LIGASE SYNOVIOLIN; 1.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Endoplasmic reticulum; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..595
FT /note="E3 ubiquitin-protein ligase synoviolin B"
FT /id="PRO_0000280552"
FT TRANSMEM 1..19
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 20..35
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..129
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..218
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ZN_FING 285..324
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 230..264
FT /note="Interaction with p53/TP53"
FT /evidence="ECO:0000250"
FT REGION 335..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 463..494
FT /evidence="ECO:0000255"
FT COMPBIAS 335..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
SQ SEQUENCE 595 AA; 65919 MW; 5B8B3234C815E491 CRC64;
MTGASLALTA SVVAHAYYLK NQFYPTVVYL TKSSPSMAIL YIQAFVLVFL LGKFMGKVFF
GQLRAAEMEH LLERSWYAVT ETCLAFTVFR DDFSPRFVAL FTLLLFLKCF HWLAEDRVDF
MERSPNISWL FHFRILALML LLGVLDAFFV SHAYNSLVTR GASVQLVFGF EYAILMTMIL
AVFIKYILHS VDLQSENPWD NKAVYMLYTE LFTGFIKVLL YMAFMTIMVK VHTFPLFAIR
PMYLAMRQFK KAVTDAVMSR RAIRNMNTLY PDATAEELQA MDNVCIICRE EMVSGAKRLP
CNHIFHTSCL RSWFQRQQTC PTCRMDVLRA SLPTQPQTPA EQQNQHQAQQ QPTPVVPPQP
NFPPGMLPPF PPGMFPLWPP MGQFPPVPGA PVGNPPDEAN PGSSSGSSAR AGETSNVGSE
SHPGAALPGF PFPPPFLGMS ILPPFGLPPM PMPPAGFAGL TDEELRAMEG HERQNLEARL
QCLQNIHTLL DAAMLQINQY LTVLASIGPP QPPVSSSSSS SASASTEPTT SSVSEPVIDT
SSIVTTDSSQ QSASPVPVNV ETLGGAEGGE TPTEEPDNVE LRRRRLQKLE TTDSQ
//
