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SYVNB_XENLA
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   03-AUG-2022, entry version 102.
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   CTD; 494996; -.
DR   Xenbase; XB-GENE-6254740; syvn1.S.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 494996; Expressed in testis and 20 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..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
 
 
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