ZNRF3_XENLA
ID ZNRF3_XENLA Reviewed; 784 AA.
AC Q4KLR8;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=E3 ubiquitin-protein ligase ZNRF3;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase ZNRF3;
DE AltName: Full=Zinc/RING finger protein 3;
DE Flags: Precursor;
GN Name=znrf3;
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=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=22575959; DOI=10.1038/nature11019;
RA Hao H.X., Xie Y., Zhang Y., Charlat O., Oster E., Avello M., Lei H.,
RA Mickanin C., Liu D., Ruffner H., Mao X., Ma Q., Zamponi R., Bouwmeester T.,
RA Finan P.M., Kirschner M.W., Porter J.A., Serluca F.C., Cong F.;
RT "ZNRF3 promotes Wnt receptor turnover in an R-spondin-sensitive manner.";
RL Nature 485:195-200(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator
CC of the Wnt signaling pathway by mediating the ubiquitination and
CC subsequent degradation of Wnt receptor complex components
CC (PubMed:22575959). Along with RSPO2 and RNF43, constitutes a master
CC switch that governs limb specification (By similarity).
CC {ECO:0000250|UniProtKB:Q08D68, ECO:0000269|PubMed:22575959}.
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: Cell membrane {ECO:0000250|UniProtKB:Q9ULT6};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ZNRF3 family. {ECO:0000305}.
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DR EMBL; BC099029; AAH99029.1; -; mRNA.
DR RefSeq; NP_001090068.1; NM_001096599.1.
DR AlphaFoldDB; Q4KLR8; -.
DR SMR; Q4KLR8; -.
DR BioGRID; 592923; 2.
DR DNASU; 735142; -.
DR GeneID; 735142; -.
DR KEGG; xla:735142; -.
DR CTD; 735142; -.
DR Xenbase; XB-GENE-5937954; znrf3.S.
DR OrthoDB; 1487241at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 735142; Expressed in egg cell and 17 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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:0060173; P:limb development; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:2000051; P:negative regulation of non-canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0038018; P:Wnt receptor catabolic process; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd16799; RING-H2_ZNRF3; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR040700; ZNRF-3_ecto.
DR InterPro; IPR045903; ZNRF3_Znf_RING.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF18212; ZNRF_3_ecto; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Metal-binding; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..784
FT /note="E3 ubiquitin-protein ligase ZNRF3"
FT /id="PRO_0000418384"
FT TOPO_DOM ?..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 202..243
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 765..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 85475 MW; D2293B472713837B CRC64;
MVKDLLQNHM HPLGLCNNND EEDLYEYGWV GVVKLEQPEM DLKPCLTVLG KAKRAVQRGA
TAVIFDISDN PDAVEQLNQG LDDPLKRPVV YMKGMDAIKL MNIVNKQKGA RARIQHRPPR
QPTEYFDMGI FLAFFVVVSL VCLILLIKIK LKQRRSQNSM NRMAVQALEK METRKFKAKG
KVSREGSCGG LDTLSSSSIS DCAICLEKYI DGEELRVIPC THRFHKRCVD PWLLQNHTCP
HCRHNIIEQK KGGHGPGCVE NSLSHGRQQQ QQRVILPVHY PGRVQRTGPI AAYPTRTSMG
PHGNPITVLT VERPVEPDLY PARTPTFLAG YRPVSLDHAS SGHHCDLEHP PYPAPPAGHA
FRRAKYNGRG FNNGTCYSQY ETMYQHYYFQ GLSFPHQQEV GGSQASRVVE NGHNHSFHSG
NMLYQPAPTM MHMAPPSSVE SCYLHSQHQH RSVCSGYLAD VPCSDSSSSS SASSAQGHAS
SSDSMLDCTE ASNQGVYGSC STFRSSLSSD FDPYVYRSCS PAKTGGGDAP ASGGEGGTGR
GRVECRSHQT FPNSPSRDRL SSCSMEMNYS SNSSLERRGA VLSSGTVPDA SVSIAQSGGK
DRRGPEKGCA CCFQRQAGDP SSDCTTLYLG PEPHQTLGPS SSGGLYSVTS NILHRTDPGT
VLGHPSRSCC LYEENHGSCY NEDYAVSIQY ALAEAAAAAA AAAVAGCEAG QPIPIIPEDP
GYEGGLEYVG HVSWEMEGDE EEVLYCQEGP CCMLEEETRA LCRSTAKDRA GSTTGQDCHQ
TDTD
