ID A0A665V9V7_ECHNA Unreviewed; 550 AA.
AC A0A665V9V7;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
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=RING finger protein 217 {ECO:0000256|ARBA:ARBA00080640};
GN Name=rnf217 {ECO:0000313|Ensembl:ENSENLP00000028097.1};
OS Echeneis naucrates (Live sharksucker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Echeneidae; Echeneis.
OX NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000028097.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000028097.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSENLP00000028097.1}
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 -!- 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 RefSeq; XP_029352858.1; XM_029496998.1.
DR AlphaFoldDB; A0A665V9V7; -.
DR FunCoup; A0A665V9V7; 200.
DR Ensembl; ENSENLT00000028940.1; ENSENLP00000028097.1; ENSENLG00000012556.1.
DR GeneID; 115038145; -.
DR InParanoid; A0A665V9V7; -.
DR OMA; QCSSCQF; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000472264; Chromosome 24.
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 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; 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:UP000472264};
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 505..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 269..484
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 61716 MW; 35B8B3837BFE1293 CRC64;
MGRDKPGMED DGPVTDACEM PGFISSFEEG KAKLSRNLST ETSFVDAKVE RPVRDLNRRV
TGSDSAAGGE GEPGEPGQRD AEGNNNNNCN GGGERRRRAS AVEILRRNLA VTKSPSLCLN
TDSRMQRQAE RDTRRNSDVT HRHGREWGRE TDEAAAQNEP TLHGVTSPDA PVAQCHRVCD
SDSNESSGVK EHVYCTVYCI AGDSRPKDGQ TTHRHDEAVP SDAPELDPET EREAGSSPEP
ALYTVDDLVD PFGDIYHQLY RDQHGAESVI HSCRVCLEDK TIAPLPCCRK AVCDECLKFY
VSSQVRVGKP YISCPIPECS GSLDDGMVIS HLANEDLAKY RYFLELNQLD SSTKPCPQCS
HFTSLKKHNP NHSEHKYKIQ CSNCQFVWCF KCHAPWHNGL KCRDYRKGDK LLRTWASVIE
HGQRNAQKCP QCKIHIQRTE GCDHMTCAQC NTNFCYRCGE RYRHLRFFGD HTSNLSVFGC
KYRYLPDKPH LRRLIRGSVC ATKVLIAPVV ILLVVVLGAL ALVIGLVVFP VYYVCKRRKK
QRTQGSGRWI
//
