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 27-MAR-2024, entry version 64.
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; 8364-ENSXETP00000016718; -.
DR Ensembl; ENSXETT00000016718; ENSXETP00000016718; ENSXETG00000007681.
DR GeneID; 549731; -.
DR KEGG; xtr:549731; -.
DR AGR; Xenbase:XB-GENE-998325; -.
DR Xenbase; XB-GENE-998325; znrf1.
DR eggNOG; KOG0801; Eukaryota.
DR HOGENOM; CLU_062700_0_1_1; -.
DR InParanoid; F7EP40; -.
DR OMA; MGIDHNA; -.
DR OrthoDB; 5474929at2759; -.
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 Bgee; ENSXETG00000007681; Expressed in skeletal muscle tissue and 18 other cell types or 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 CDD; cd16695; mRING-CH-C4HC2H_ZNRF2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46661:SF2; E3 UBIQUITIN-PROTEIN LIGASE ZNRF1; 1.
DR PANTHER; PTHR46661; E3 UBIQUITIN-PROTEIN LIGASE ZNRF1-LIKE PROTEIN; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SUPFAM; SSF57850; RING/U-box; 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
//
