SYVNA_XENLA
ID SYVNA_XENLA Reviewed; 605 AA.
AC Q6NRL6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=E3 ubiquitin-protein ligase synoviolin A;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q86TM6};
DE AltName: Full=RING-type E3 ubiquitin transferase synoviolin A {ECO:0000305};
DE AltName: Full=Synovial apoptosis inhibitor-1-A;
GN Name=syvn1-a; Synonyms=hrd1-a;
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=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-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}.
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; BC070731; AAH70731.1; -; mRNA.
DR RefSeq; NP_001084825.1; NM_001091356.1.
DR AlphaFoldDB; Q6NRL6; -.
DR SMR; Q6NRL6; -.
DR DNASU; 431869; -.
DR GeneID; 431869; -.
DR KEGG; xla:431869; -.
DR CTD; 431869; -.
DR Xenbase; XB-GENE-1005365; syvn1.L.
DR OrthoDB; 897451at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 431869; Expressed in liver and 19 other tissues.
DR GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032832; E3_lig_synoviolin/Hrd1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22763:SF169; PTHR22763:SF169; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 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..605
FT /note="E3 ubiquitin-protein ligase synoviolin A"
FT /id="PRO_0000280551"
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..605
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 334..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 465..496
FT /evidence="ECO:0000255"
FT COMPBIAS 334..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..397
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
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 605 AA; 66954 MW; F998B91A8E6D8EFC CRC64;
MTGASLALTA AVVAHAYYLK NQFYPTVVYL TKSSPSMAVL YIQAFVLVFL LGKFMGKVFF
GQLRAAEMEH LLERSWYAVT ETCLAFTVFR DDFSPRFVAL FTLLLFLKCF HWLAEDRVDF
MERSPNISWL FHFRILALML LLGVLDAFFV SHAYHSLVIR GASVQLVFGF EYAILMTVIL
TVFIKYILHS VDLQSENPWD NKAVYMLYTE LFTGFIKVLL YVAFMTIMVK VHTFPLFAIR
PMYLAMRQFK KAVTDAIMSR RAIRNMNTLY PDATAEELQA MDNVCIICRE EMVTGAKRLP
CNHIFHTSCL RSWFQRQQTC PTCRMDVLRA SLPTQPQTPT EQQNQHQNQA QQQPTPVIPP
QPNFPPGILP PFPPGMFPLW PPMGPFPPVP GAPGGNPPDE ANPGSSSGSS PRPGETSNVG
SESQPGAALP GFPFPPPFLG MPILPPFGLP PMPMPPAGFT GLTDEELRAM EGHERQNLEA
RLQCLQNIHT LLDAAMLQIN QYLTVLASIG PPQPPISSTS TSTSSAASAS TAPTTSNISE
PVIPVDTTST VTNTESSQQS APPAPVSVET LSGAEGGETT TEEPDNVELR RRRLQKLETG
TTDSQ
