ID A0A8C1HQF9_CYPCA Unreviewed; 538 AA.
AC A0A8C1HQF9;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 2.
DT 18-JUN-2025, entry version 18.
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};
OS Cyprinus carpio carpio.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000067572.2, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000067572.2}
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 Ensembl; ENSCCRT00000073233.2; ENSCCRP00000067572.2; ENSCCRG00000036431.2.
DR GeneTree; ENSGT00730000111285; -.
DR OMA; QCSSCQF; -.
DR Proteomes; UP001108240; Unplaced.
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:UP001108240};
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 493..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 254..472
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 60856 MW; B6B0D080F0C1B4B4 CRC64;
MEDESSVCVN VTAQNMPGCT GRDGESVHVS SGTRSTDFGR DARRSDAKVP SSLSLSSKDV
LEFHKHKHEP GGNNKENNER ETIRAVDILR RNFGSTIRDP EDPKDLEKVG FDITLNDLGH
ENDDERMQCS TKSLQQNMES NSGLGDPDGN HHIDYNIDLK SGEDPSLSKE HVYCTVYCIA
NDNYRIPVEK RTSDHQATSL SPSSSSSSDV LVLPPIDLPN SELNHDHYPE PYTVSDLMLS
GLNSSYNTDS SLSVVLTCRI CLDDKQTVPL HCCKNAVCEE CLKRYIISQV HVGRAHLVCP
ITECSGFLEE SLVISHLSSE ELAKYKYLLE LSRLDFSTKP CPHCSLFTSL KSHSQQMSTK
SEHKYKIQCT KCQFVWCFKC HAPWHEGLKC RDYRKGDKLL RHWASVIEHG QRNAQKCPRC
KIHIQRTEGC DHMTCTQCNT NFCYRCGEKY RHLRFFGDHT SNLSVFGCKY RYLPEKPHLR
RLVRGSVCMS KVLVAPVVIV LVVVVGALAL VIGLFALPIY YTCKRRRKRS QGSGRWLC
//
