FBXL5_XENLA
ID FBXL5_XENLA Reviewed; 678 AA.
AC Q6INS1;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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; BC072202; AAH72202.1; -; mRNA.
DR RefSeq; NP_001085061.1; NM_001091592.1.
DR AlphaFoldDB; Q6INS1; -.
DR SMR; Q6INS1; -.
DR DNASU; 432131; -.
DR GeneID; 432131; -.
DR KEGG; xla:432131; -.
DR CTD; 432131; -.
DR Xenbase; XB-GENE-968570; fbxl5.L.
DR OMA; XDWYSGP; -.
DR OrthoDB; 1282076at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 432131; Expressed in testis and 19 other tissues.
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; 3.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 5.
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..678
FT /note="F-box/LRR-repeat protein 5"
FT /id="PRO_0000390468"
FT DOMAIN 202..248
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 314..340
FT /note="LRR 1"
FT REPEAT 341..366
FT /note="LRR 2"
FT REPEAT 367..392
FT /note="LRR 3"
FT REPEAT 393..420
FT /note="LRR 4"
FT REPEAT 566..594
FT /note="LRR 5"
FT REPEAT 595..622
FT /note="LRR 6"
FT REPEAT 623..648
FT /note="LRR 7"
FT REPEAT 655..678
FT /note="LRR 8"
FT REGION 1..159
FT /note="Hemerythrin-like"
FT /evidence="ECO:0000250"
FT REGION 285..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..305
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:0000250"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 678 AA; 76873 MW; 2013E77811AA8E10 CRC64;
MAPFPDEVDL FTGPHWRMKQ LVGRYCEKLS NTNFSNNNDL LALLQSLYET FKEFKMHEQI
ENEYIIGLLQ QRSHTVYNVH SDNKLSEMLV LFEKGMKNVK NEYKQLNYVQ QLKERLEAFT
SDFLPHMKEE EEVFQPMLME YFTYDEMKDI KKKVIAQHCS QKDTTELLRG LSLWNKAEEL
QKVLKYSVDE KAERNSKTQK SSSSISSLPP EVMLNIFTYL NPQDLCRCSQ VNTEWAQLAK
TGSLWRHLYP VLWARGDWYS GSHAYLDNEP DEDWISRRKD ESRAYQEWDE DADIDESEET
GEEEDSSISM AQREKELLNS LVHYILPYVG HSVKTLVLAY SSATSSKVIR QMLEYCPNLE
HLDLTQTDIS DSAFNGWHFG ACQTLHHIDL SGCDKITDLT LEKLSVALGI PSAHKKRLLK
CYRNNRTLKD IRNQMRCSSL AQITGESTIY SDAFWANSDR SQDYTSPPIW ILDSGNPGDI
EDAADWKFRT TDGLCVLEMA PSVTCFSNGC CSRARPGRWT NVGWQEHCKA ATVSYCGHTL
CGNTLRTIHT LPEASALCNI GTRTLHSDIT DCFPGSAKSD QQAARALQFL SLSGCHQITD
HGLRALTIGG GLPKLEHLNL SGCLNVTGSG LQDLVATCPS LNDEHFYYCD NISGPHGATA
SGCQNLQCGF RMCCRSGE
