FBXL5_XENTR
ID FBXL5_XENTR Reviewed; 660 AA.
AC Q5XGI3;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=F-box/LRR-repeat protein 5;
DE AltName: Full=F-box and leucine-rich repeat protein 5;
GN Name=fbxl5;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase
CC complex that plays a central role in iron homeostasis by promoting the
CC ubiquitination and subsequent degradation of ireb2/irp2. Upon high iron
CC and oxygen level, it specifically recognizes and binds ireb2/irp2,
CC promoting its ubiquitination and degradation by the proteasome (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC -!- DOMAIN: The hemerythrin-like region acts as an oxygen and iron sensor
CC by binding oxygen through a diiron metal-center. In absence of oxygen
CC and iron, the protein is ubiquitinated and degraded (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated upon iron and oxygen depletion, leading to its
CC degradation by the proteasome. Ubiquitination is regulated by the
CC hemerythrin-like region that acts as an oxygen and iron sensor (By
CC similarity). {ECO:0000250}.
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DR EMBL; BC084456; AAH84456.1; -; mRNA.
DR RefSeq; NP_001011072.1; NM_001011072.1.
DR AlphaFoldDB; Q5XGI3; -.
DR PaxDb; Q5XGI3; -.
DR GeneID; 496483; -.
DR KEGG; xtr:496483; -.
DR CTD; 26234; -.
DR Xenbase; XB-GENE-968565; fbxl5.
DR eggNOG; ENOG502QS5I; Eukaryota.
DR InParanoid; Q5XGI3; -.
DR OrthoDB; 1282076at2759; -.
DR Reactome; R-XTR-8951664; Neddylation.
DR Reactome; R-XTR-917937; Iron uptake and transport.
DR Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd12109; Hr_FBXL5; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR012312; Hemerythrin-like.
DR InterPro; IPR045808; Hr_FBXL5.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF01814; Hemerythrin; 1.
DR Pfam; PF13516; LRR_6; 2.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 4.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Iron; Leucine-rich repeat; Metal-binding; Reference proteome;
KW Repeat; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..660
FT /note="F-box/LRR-repeat protein 5"
FT /id="PRO_0000390469"
FT DOMAIN 200..246
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 311..337
FT /note="LRR 1"
FT REPEAT 338..362
FT /note="LRR 2"
FT REPEAT 363..389
FT /note="LRR 3"
FT REPEAT 390..417
FT /note="LRR 4"
FT REPEAT 551..576
FT /note="LRR 5"
FT REPEAT 577..604
FT /note="LRR 6"
FT REPEAT 605..630
FT /note="LRR 7"
FT REPEAT 631..649
FT /note="LRR 8"
FT REGION 1..157
FT /note="Hemerythrin-like"
FT /evidence="ECO:0000250"
FT REGION 283..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..301
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 15
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 80
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 660 AA; 74820 MW; AEF9A60E6BD6CF95 CRC64;
MAPFPDEVDL FTGPHWRMKQ LVGRYCEKLS NTNFSSNTDF LALLQSLYET FKEFKMHEQI
ENEYIIGLLQ QRSQTVFNVH SDNKLSEMLV LFEKGMKNNE YEQLNYAQQL KERLEAFTSD
FLPHMKEEEE VFQPMLMEYF TYDELKDIKK KVIAQHCSQK DTAELLRGFS LWNKAEELQK
VFKYSVDEKI ERDSKNRKSS ASICNLPPEV MLNIFSYLNP QDLCRCSQVN TKWAQLARTG
SLWRHLYPVL WARGDWYSGP PTHLDNEPDE DWISRRKDES RAYQEWDEDA DIDESEETGE
DDPSISVAQR EKELLNSLVH YILPYIGHSV KTLVLAYSSA TSNKVIRQIL EYCPNMEHLD
LTQTDISDSA FNGWCFGACQ TLRHIDLSGC EKITDSALEK LSVALGMPLA HKKRLLKCYR
NNRTVKDIRN QMRCGSLAQI TGESGIYSDY SSSQIWILNS GNLGDIEDAA DWKFRTTDGL
GVLEMTPNLT CFSNGCCSRA VPGRWTNVIR QEHCKAAPLN YCGHTLCGNT LRTIQALPGS
NIGTKTLQSE IRDICPGSAK LDQQVARVLQ FLSLSGCHQI TDHGLRVLTI GGGLPNLEHL
NLSGCLNVTG SGLQDLVSAC PSLNDEHFYY CDNISGPHAA TASGCQNLQC GFRACCRSGE
