ZNRF2_DANRE
ID ZNRF2_DANRE Reviewed; 217 AA.
AC Q08CN9;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=E3 ubiquitin-protein ligase znrf2;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase znrf2;
DE AltName: Full=Zinc/RING finger protein 2;
GN Name=znrf2; ORFNames=zgc:152865;
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;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in the establishment and maintenance of
CC neuronal transmission and plasticity via its ubiquitin ligase activity.
CC E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating
CC enzyme in the form of a thioester and then directly transfer the
CC ubiquitin to targeted substrates. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q8NHG8};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NHG8}. Lysosome
CC membrane {ECO:0000250|UniProtKB:Q8NHG8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8NHG8}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q8NHG8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8NHG8}.
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DR EMBL; BC124159; AAI24160.1; -; mRNA.
DR RefSeq; NP_001070196.1; NM_001076728.1.
DR AlphaFoldDB; Q08CN9; -.
DR SMR; Q08CN9; -.
DR STRING; 7955.ENSDARP00000099393; -.
DR PaxDb; Q08CN9; -.
DR Ensembl; ENSDART00000158047; ENSDARP00000134291; ENSDARG00000098792.
DR GeneID; 767761; -.
DR KEGG; dre:767761; -.
DR CTD; 767761; -.
DR ZFIN; ZDB-GENE-060929-24; znrf2b.
DR eggNOG; KOG0801; Eukaryota.
DR GeneTree; ENSGT00940000159017; -.
DR InParanoid; Q08CN9; -.
DR OrthoDB; 1256682at2759; -.
DR PhylomeDB; Q08CN9; -.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q08CN9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000098792; Expressed in retina and 21 other tissues.
DR ExpressionAtlas; Q08CN9; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 Cell membrane; Cell projection; Endosome; Lipoprotein; Lysosome; Membrane;
KW Metal-binding; Myristate; Reference proteome; Synapse; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..217
FT /note="E3 ubiquitin-protein ligase znrf2"
FT /id="PRO_0000277805"
FT ZN_FING 174..215
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 217 AA; 22638 MW; B16652F2FCEAE0E0 CRC64;
MGAKQSSPAA NGRTRAYSGS DLPSATASVN GRTAAVLRYN NSQGASGATS AASASSSAAV
ASQFISSRTR SVGPSARPQS GINIPNSGAY SSADSGNSTP EEPGGERERS TGAPRLVIGS
LPAHLSPHLF GGFKCPVCSK FISSDEMDLH LVMCLTKPRV TYNEDVLSKD AGECAICLEE
LLQGDTIARL PCLCIYHKGC IDEWFEVNRS CPEHPAD
