ID   ZNRF1_XENTR             Reviewed;         195 AA.
AC   F7EP40;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 57.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
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; AAMC01003501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01003502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01003503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001016977.1; NM_001016977.2.
DR   AlphaFoldDB; F7EP40; -.
DR   SMR; F7EP40; -.
DR   STRING; 8364.ENSXETP00000027937; -.
DR   PaxDb; F7EP40; -.
DR   GeneID; 549731; -.
DR   KEGG; xtr:549731; -.
DR   CTD; 84937; -.
DR   Xenbase; XB-GENE-998325; znrf1.
DR   eggNOG; KOG0801; Eukaryota.
DR   HOGENOM; CLU_062700_0_1_1; -.
DR   InParanoid; F7EP40; -.
DR   OMA; HSPTVPF; -.
DR   OrthoDB; 1256682at2759; -.
DR   PhylomeDB; F7EP40; -.
DR   TreeFam; TF317681; -.
DR   Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000007681; Expressed in skeletal muscle tissue and 18 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   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
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_0000415579"
FT   ZN_FING         152..193
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..84
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"
SQ   SEQUENCE   195 AA;  20817 MW;  948ADC8F69193B42 CRC64;
     MGGKQSSASR SRAPFPGVSS DDSAVPPSSN FGHFRAGGAM GLRSRSVSSV SGLDPPAPGL
     PFGLYRAGPD TERGGSSGSE DSRGDLYLGS RASLADTLQI APRWIGAHSG FRCPICSKSV
     APDEMEMHFI MCLSKPRLSY NDDVLTRDAG ECVICLEELS QGDTIARLPC LCIYHKSCID
     SWFEVNRCCP EHPSD