ID A0A0D9RUT0_CHLSB Unreviewed; 307 AA.
AC A0A0D9RUT0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 18-JUN-2025, entry version 46.
DE RecName: Full=E3 ubiquitin-protein ligase RNF217 {ECO:0000256|ARBA:ARBA00067769};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE AltName: Full=IBR domain-containing protein 1 {ECO:0000256|ARBA:ARBA00081613};
DE AltName: Full=RING finger protein 217 {ECO:0000256|ARBA:ARBA00080640};
GN Name=RNF217 {ECO:0000313|Ensembl:ENSCSAP00000012369.1};
OS Chlorocebus sabaeus (Green monkey) (Simia sabaea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000012369.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000012369.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000012369.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2
CC ubiquitin-conjugating enzymes in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. Mediates the
CC degradation of the iron exporter ferroportin/SLC40A1 and thus regulates
CC iron homeostasis. {ECO:0000256|ARBA:ARBA00054457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Interacts with HAX1. {ECO:0000256|ARBA:ARBA00065998}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF217 subfamily.
CC {ECO:0000256|ARBA:ARBA00061413}.
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DR EMBL; AQIB01065511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01065512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01065513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01065514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01065515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01065516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01065517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01065518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01065519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01065520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0D9RUT0; -.
DR STRING; 60711.ENSCSAP00000012369; -.
DR Ensembl; ENSCSAT00000014395.1; ENSCSAP00000012369.1; ENSCSAG00000016302.1.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00730000111285; -.
DR OMA; PQTEMPW; -.
DR Proteomes; UP000029965; Chromosome 13.
DR Bgee; ENSCSAG00000016302; Expressed in fibroblast and 7 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20342; BRcat_RBR_RNF217; 1.
DR CDD; cd20350; Rcat_RBR_RNF217; 1.
DR CDD; cd16622; vRING-HC-C4C4_RBR_RNF217; 1.
DR FunFam; 1.20.120.1750:FF:000008; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000264; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047551; BRcat_RBR_RNF217.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047552; Rcat_RBR_RNF217.
DR InterPro; IPR047550; RNF217_RBR_vRING-HC.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 264..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..243
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
SQ SEQUENCE 307 AA; 35207 MW; 74B5B9BA6DBFDF54 CRC64;
MPSLLGAPPY SGLGGVGDPY APLMVLMCRV CLEDKPIKPL PCCKKAVCEE CLKVYLSAQV
QLGQVEIKCP ITECFEFLEE TTVVYNLTHE DSIKYKYFLE LGRIDSSTKP CPQCKHFTTF
KKKGHIPTPS RSESKYKIQC PTCQFVWCFK CHSPWHEGVN CKEYKKGDKL LRHWASEIEH
GQRNAQKCPK CKIHIQRTEG CDHMTCSQCN TNFCYRCGER YRQLRFFGDH TSNLSIFGCK
YRYLPERPHL RRLVRGSVCA GKLFIAPLIM VLGLALGAIA VVIGLFVFPI YCLCKKQRKR
SRTGMHW
//
