ID   ZNRF1_DANRE             Reviewed;         215 AA.
AC   Q6P4U6;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=E3 ubiquitin-protein ligase znrf1;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase znrf1;
DE   AltName: Full=Zinc/RING finger protein 1;
GN   Name=znrf1; ORFNames=zgc:77896;
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].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that plays a role in neuron cells
CC       differentiation. Plays a role in the establishment and maintenance of
CC       neuronal transmission and plasticity. {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 {ECO:0000250}. Lysosome {ECO:0000250}.
CC       Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC       activity. {ECO:0000250}.
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DR   EMBL; BC063239; AAH63239.1; -; mRNA.
DR   RefSeq; NP_957164.1; NM_200870.1.
DR   AlphaFoldDB; Q6P4U6; -.
DR   SMR; Q6P4U6; -.
DR   STRING; 7955.ENSDARP00000026082; -.
DR   PaxDb; Q6P4U6; -.
DR   Ensembl; ENSDART00000010495; ENSDARP00000026082; ENSDARG00000020475.
DR   GeneID; 393844; -.
DR   KEGG; dre:393844; -.
DR   CTD; 84937; -.
DR   ZFIN; ZDB-GENE-040426-1905; znrf1.
DR   eggNOG; KOG0801; Eukaryota.
DR   GeneTree; ENSGT00940000159278; -.
DR   HOGENOM; CLU_062700_0_1_1; -.
DR   InParanoid; Q6P4U6; -.
DR   OMA; YNVRTQR; -.
DR   OrthoDB; 1256682at2759; -.
DR   PhylomeDB; Q6P4U6; -.
DR   TreeFam; TF317681; -.
DR   Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q6P4U6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 25.
DR   Bgee; ENSDARG00000020475; Expressed in muscle tissue and 30 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
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   Endosome; Lipoprotein; Lysosome; Membrane; Metal-binding; Myristate;
KW   Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..215
FT                   /note="E3 ubiquitin-protein ligase znrf1"
FT                   /id="PRO_0000277801"
FT   ZN_FING         172..213
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   215 AA;  22875 MW;  30A1C627806608A9 CRC64;
     MGGKQSTAGR PRGAFPGVST DDSAVPPSAH FGHYRPGGTM GLRSRSVSSV AGMGIDHSAT
     VPFGFYTPRG TDSDRAGGGS GSDPAHNGNG YQETGGGHHT DGMLYLGSRA SLADTLPLHI
     APRWFSAHSG FKCPVCSKSV ASNEMEVHFI MCLSKPRLSY NDDVLSRDAG ECVICLEELQ
     QGDTIARLPC LCIYHKSCID SWFEINRSCP EHPSD