ID A0A671DIK6_RHIFE Unreviewed; 532 AA.
AC A0A671DIK6;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 23.
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:ENSRFEP00010000348.1};
OS Rhinolophus ferrumequinum (Greater horseshoe bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Rhinolophoidea;
OC Rhinolophidae; Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=59479 {ECO:0000313|Ensembl:ENSRFEP00010000348.1, ECO:0000313|Proteomes:UP000472240};
RN [1] {ECO:0000313|Ensembl:ENSRFEP00010000348.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25689317; DOI=10.1146/annurev-animal-090414-014900;
RA Koepfli K.P., Paten B., O'Brien S.J., Koepfli K.P., Paten B., Antunes A.,
RA Belov K., Bustamante C., Castoe T.A., Clawson H., Crawford A.J.,
RA Diekhans M., Distel D., Durbin R., Earl D., Fujita M.K., Gamble T.,
RA Georges A., Gemmell N., Gilbert M.T., Graves J.M., Green R.E., Hickey G.,
RA Jarvis E.D., Johnson W., Komissarov A., Korf I., Kuhn R., Larkin D.M.,
RA Lewin H., Lopez J.V., Ma J., Marques-Bonet T., Miller W., Murphy R.,
RA Pevzner P., Shapiro B., Steiner C., Tamazian G., Venkatesh B., Wang J.,
RA Wayne R., Wiley E., Yang H., Zhang G., Haussler D., Ryder O., O'Brien S.J.;
RT "The Genome 10K Project: a way forward.";
RL Annu Rev Anim Biosci 3:57-111(2015).
RN [2] {ECO:0000313|Ensembl:ENSRFEP00010000348.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=29166127; DOI=10.1146/annurev-animal-022516-022811;
RA Teeling E.C., Vernes S.C., Davalos L.M., Ray D.A., Gilbert M.T.P.,
RA Myers E.;
RT "Bat Biology, Genomes, and the Bat1K Project: To Generate Chromosome-Level
RT Genomes for All Living Bat Species.";
RL Annu Rev Anim Biosci 6:23-46(2018).
RN [3] {ECO:0000313|Ensembl:ENSRFEP00010000348.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Teeling E., Myers G., Vernes S., Pippel M., Winkler S., Fedrigo O.,
RA Rhie A., Koren S., Phillippy A., Lewin H., Damas J., Howe K.,
RA Mountcastle J., Jarvis E.D.;
RT "G10K-VGP greater horseshoe bat female genome, primary haplotype.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSRFEP00010000348.1}
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 AlphaFoldDB; A0A671DIK6; -.
DR FunCoup; A0A671DIK6; 84.
DR Ensembl; ENSRFET00010000390.1; ENSRFEP00010000348.1; ENSRFEG00010000292.1.
DR GeneTree; ENSGT00730000111285; -.
DR InParanoid; A0A671DIK6; -.
DR OMA; GHRENMS; -.
DR Proteomes; UP000472240; Chromosome 3.
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:UP000472240};
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 488..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 248..467
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..63
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..103
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 58364 MW; 1704A39BB92F75C9 CRC64;
MGEEQSTVSG GRPQEAGDPA GGATGHPEPP RPRGDSAGAP GPCAASAEPS ASGCGSDSCC
ADPSAREPTR SREAPCWTKS EAAGQPAGLA LTGPLNPQTL QQQLEEEEKA GDRNEGRGEQ
QEAPLGAEPE PRTRVGTRDG LVLDVLGQRR PPPAKRQVFC SVYCVENDLP LDSTAEHRSP
PASPPRAPPV TDPPSPRLPL PTDPLSPDGG SIELEFYLAP EPFSVPGLLG APPYSGLGGV
GDPYAPLMVL MCRVCLEDKP IKPLPCCKKA VCEECLKVYL SSQVQVGQVE IKCPITECFE
FLEEATVIYN LTHEDSIKYK YFLELGRIDS STKPCPQCKH FTTFKKKGHI PTPSRSESKY
KIQCPTCQFI WCFKCHSPWH EGVNCKEYKK GDKLLRHWAS EIEHGQRNAQ KCPKCKIHIQ
RTEGCDHMTC SQCNTNFCYR CGERYRQLRF FGDHTSNLSI FGCKYRYLPE RPHLRRLVRG
SVCAGKLFVA PLILVLGLAL GAIAVVIGLF VFPIYCLCKK QRKRSRTVSS RS
//
