ID A0A2K6GM79_PROCO Unreviewed; 542 AA.
AC A0A2K6GM79;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 18-JUN-2025, entry version 34.
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:ENSPCOP00000027350.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000027350.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000027350.1}
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 RefSeq; XP_012516318.1; XM_012660864.1.
DR AlphaFoldDB; A0A2K6GM79; -.
DR STRING; 379532.ENSPCOP00000027350; -.
DR Ensembl; ENSPCOT00000038163.1; ENSPCOP00000027350.1; ENSPCOG00000026159.1.
DR GeneID; 105823610; -.
DR KEGG; pcoq:105823610; -.
DR CTD; 154214; -.
DR GeneTree; ENSGT00730000111285; -.
DR OMA; GHRENMS; -.
DR OrthoDB; 74050at9443; -.
DR Proteomes; UP000233160; Unassembled WGS sequence.
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:UP000233160};
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 499..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..478
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..216
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 59396 MW; F4F1F79806D98269 CRC64;
MGEEQSTVSG GDRPQESRAL AGGTAGHPEP ARPRGDSAGA PGPHAASAES SGGGCGSNSG
CADTSTPEPA RSWGTPAWRR SQAPGLSAGL ALNGPLNPQT LQLQLEQEEE EEEAGDRKEG
GDEQQEAPPG EELEPRTRDG APNGLVLDVL GQQRPLPAKR QVFCSVYCVE SDLPKAPAGE
QRSPPASPGR APPVPNPPST PSSFPSPRLS LPSDPLSPDG GSIELEFYLA PEPFSMPSLL
GAPPYSGLGG VGDPYAPLMV LMCRVCLEDK PIKPLPCCKK AVCDECLKVY LSSQVQLGQV
EIKCPITECF EFLEETTVVY NLTHEDSIKY KYFLELGRID SSTKPCPQCK HFTTFKKKGH
IPTPSRSESK YKIQCPTCQF VWCFKCHSPW HEGVNCKEYK KGDKLLRHWA SEIEHGQRNA
QKCPKCKIHI QRTEGCDHMT CSQCNTNFCY RCGERYRQLR FFGDHTSNLS IFGCKYRYLP
ERPHLRRLVR GSVCAGKLFI APLILVLGLA LGAIAVVIGL FVFPIYCLCK KQRKRSRTGM
HW
//
