RNF43_XENTR
ID RNF43_XENTR Reviewed; 689 AA.
AC P0DPR2;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=E3 ubiquitin-protein ligase RNF43;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 43;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF43;
DE Flags: Precursor;
GN Name=rnf43;
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).
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=29769720; DOI=10.1038/s41586-018-0118-y;
RA Szenker-Ravi E., Altunoglu U., Leushacke M., Bosso-Lefevre C., Khatoo M.,
RA Thi Tran H., Naert T., Noelanders R., Hajamohideen A., Beneteau C.,
RA de Sousa S.B., Karaman B., Latypova X., Basaran S., Yuecel E.B., Tan T.T.,
RA Vlaminck L., Nayak S.S., Shukla A., Girisha K.M., Le Caignec C.,
RA Soshnikova N., Uyguner Z.O., Vleminckx K., Barker N., Kayserili H.,
RA Reversade B.;
RT "RSPO2 inhibition of RNF43 and ZNRF3 governs limb development independently
RT of LGR4/5/6.";
RL Nature 557:564-569(2018).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator
CC of the Wnt signaling pathway by mediating the ubiquitination,
CC endocytosis and subsequent degradation of Wnt receptor complex
CC components Frizzled. Acts on both canonical and non-canonical Wnt
CC signaling pathway (By similarity). Along with RSPO2 and ZNRF3,
CC constitutes a master switch that governs limb specification
CC (PubMed:29769720). {ECO:0000250|UniProtKB:Q68DV7,
CC ECO:0000269|PubMed:29769720}.
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; Evidence={ECO:0000250|UniProtKB:Q68DV7};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q68DV7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q68DV7};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q68DV7}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q68DV7}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:Q68DV7}. Nucleus
CC envelope {ECO:0000250|UniProtKB:Q68DV7}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous knockdown of RNF43 and ZNRF3 results
CC in ectopic limb development. {ECO:0000269|PubMed:29769720}.
CC -!- SIMILARITY: Belongs to the ZNRF3 family. {ECO:0000305}.
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DR EMBL; CM004444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002935238.2; XM_002935192.4.
DR AlphaFoldDB; P0DPR2; -.
DR SMR; P0DPR2; -.
DR STRING; 8364.ENSXETP00000026492; -.
DR GeneID; 100491274; -.
DR KEGG; xtr:100491274; -.
DR CTD; 54894; -.
DR Xenbase; XB-GENE-952685; rnf43.
DR Reactome; R-XTR-4641263; Regulation of FZD by ubiquitination.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000037241; Expressed in neurula embryo and 12 other tissues.
DR ExpressionAtlas; P0DPR2; baseline.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005109; F:frizzled binding; 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:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0038018; P:Wnt receptor catabolic process; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 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; Developmental protein; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Wnt signaling pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..689
FT /note="E3 ubiquitin-protein ligase RNF43"
FT /id="PRO_0000445702"
FT TOPO_DOM 28..191
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..689
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ZN_FING 268..308
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 386..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..522
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 85..113
FT /evidence="ECO:0000250|UniProtKB:Q68DV7"
SQ SEQUENCE 689 AA; 76971 MW; 09E6E792268E4A04 CRC64;
MNRARLQLAS LWLLLTVTLQ AVASAMGTTE REMDVKALIR VTPLQAEESG GVGQGNLTLE
GLFARVAEIS PAEGRLLQFH PLSLCNTSED DQTKPGFISI VKLETPDRDT QPCLSLANKA
RLAGERGAHA VLFDITNDRG ALQQLQQPAG INQPVVLIWG PDAEKLMDVV NKNKEALVKI
EVQEQPKWLH HDIWILLTVA GTVMFFVLYA VARLLCRQPP PQDSIQQQTL LAISRLGTRR
YQQRMLKDQR ASGGWVETAS TSSSVPVCAI CLEEFTDGQE LRILPCCHEY HLGCVDPWLR
QNHTCPLCMY DILDSGTPPR PLAHRAPSQT QLWGRYPGSA RLMSHLPPHG TPMVFPTPNN
SLFLPRAPYY LDHTHHWQMP EQMAMQMRTH RRGAEGTREL GISPGCQDSS GYLPDDPGSD
SSSGPCHGSS SENCTDISLH CLHGTSSSSV HSSQSNQEDS SPPALASYLL PQGELPALNP
LLSTQASYAS HVHFHQHRHH HYRRNQPSMS HSHPHRSKRR TKVSRADPSY YREHRHTTGA
NGELRSLMVR REPRPSCSRT CFDPRTNREH PRHQQSMPQA ASVVQGSSEP DVATSLRGSR
TDPPSRTYRK KKSSAPSHLP LLYSPRHCHP ANSVQMSESS HPRWAEEVRL LHSRVNSHRE
NTAMMHLYHP PHHNQGATEE IEAVCEHAV
