SYVN1_DANRE
ID SYVN1_DANRE Reviewed; 625 AA.
AC Q803I8; Q6NYA5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=E3 ubiquitin-protein ligase synoviolin;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q86TM6};
DE AltName: Full=RING-type E3 ubiquitin transferase synoviolin {ECO:0000305};
DE AltName: Full=Synovial apoptosis inhibitor 1;
GN Name=syvn1; Synonyms=hrd1; ORFNames=zgc:55735, zgc:77108;
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 [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) 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 -!- SEQUENCE CAUTION:
CC Sequence=AAH44465.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC044465; AAH44465.1; ALT_FRAME; mRNA.
DR EMBL; BC066677; AAH66677.1; -; mRNA.
DR AlphaFoldDB; Q803I8; -.
DR SMR; Q803I8; -.
DR STRING; 7955.ENSDARP00000100101; -.
DR PaxDb; Q803I8; -.
DR PRIDE; Q803I8; -.
DR ZFIN; ZDB-GENE-030131-7166; syvn1.
DR eggNOG; KOG0802; Eukaryota.
DR InParanoid; Q803I8; -.
DR PhylomeDB; Q803I8; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q803I8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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 Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..625
FT /note="E3 ubiquitin-protein ligase synoviolin"
FT /id="PRO_0000280550"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..40
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..135
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..212
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ZN_FING 291..330
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 236..270
FT /note="Interaction with p53/TP53"
FT /evidence="ECO:0000250"
FT REGION 337..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q86TM6"
FT CONFLICT 372
FT /note="I -> M (in Ref. 1; AAH66677)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="D -> E (in Ref. 1; AAH66677)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="E -> D (in Ref. 1; AAH66677)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="K -> R (in Ref. 1; AAH66677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 68757 MW; 73CCBBEC5A550566 CRC64;
MVRAALVTAT SLALTGAVVA HAYFLKHQFY PTVVYLTKSS PSMAVLYIQA FVLVFLLGKL
MRKVFFGQLR AAEMEHLIER SWYAVTETCL AFTVFRDDFS PRFVALFTLL LFLKCFHWLA
EDRVDFMERS PNISWVFHFR VLSLMVLLGV MDFLFVNHAC HSIITRGASV QLVFGFEYAI
LMTMVLTTFI KYTLHTIDLQ SENPWDNKAV YMLYTELFTG FIKVLLYMAF MTIMIKVHTF
PLFAIRPMYL AMRQFKKAVT DAIMSRRAIR NMNTLYPDAT PEDLQATDNV CIICREEMVT
GAKKLPCNHI FHSSCLRSWF QRQQTCPTCR MDVLRASQPN QTPAPPAAQA PAPPAPANAP
IPPPVNVAPG MIPQFPPGLF PFWGPFPGAP PPAVPGAPAA PTDTPQPSSD GAQGAESGAG
GLAQSTAEAA SAAPGAMPGF PFTMPPPFPS APWLPMPPPP PFMSSMPPPP SSLSSMSEAE
LRELEQEGRR GLEARLQCLH NIHTLLDAAM LNIHHYLSTV ATLSPPRSET NTGETSESAN
VESSPSTANT ETAGQEIQSQ SGESINGAAG FSQPDSTTEG EKDVKEEDED DGEPSAAELR
RRRLRKLETT NTPDHGNLLK LASVN
