ID   ZNRF1_XENLA             Reviewed;         195 AA.
AC   Q66KG7; Q801R3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
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;
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=Embryo, and Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) 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; BC047964; AAH47964.1; -; mRNA.
DR   EMBL; BC080402; AAH80402.1; -; mRNA.
DR   RefSeq; NP_001080802.1; NM_001087333.1.
DR   AlphaFoldDB; Q66KG7; -.
DR   SMR; Q66KG7; -.
DR   DNASU; 380496; -.
DR   GeneID; 380496; -.
DR   KEGG; xla:380496; -.
DR   CTD; 380496; -.
DR   Xenbase; XB-GENE-998330; znrf1.S.
DR   OMA; YNVRTQR; -.
DR   OrthoDB; 1256682at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 380496; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   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..195
FT                   /note="E3 ubiquitin-protein ligase ZNRF1"
FT                   /id="PRO_0000277802"
FT   ZN_FING         152..193
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        26
FT                   /note="P -> T (in Ref. 1; AAH47964)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   195 AA;  20732 MW;  D55CFA7DC9B6DA1F CRC64;
     MGGKQSSASR SRAPFPGVSS DDSAVPPSSN FGHFRGGGAM GLRSRSVSSV SGLDPPAAAL
     PFGLYRAGPD TERGGGSGSE DSRGGLYLGS RASLADTLHI TPRWIGAHSG FRCPICSKSV
     ASDEMEMHFI MCLSKPRLSY NDDVLTRDAG ECVICLEELS QGDTIARLPC LCIYHKSCID
     SWFEVNRCCP EHPSD