FBXL5_DANRE
ID FBXL5_DANRE Reviewed; 679 AA.
AC Q2YDQ5;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=F-box/LRR-repeat protein 5;
DE AltName: Full=F-box and leucine-rich repeat protein 5;
GN Name=fbxl5;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI10115.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC110114; AAI10115.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q2YDQ5; -.
DR SMR; Q2YDQ5; -.
DR STRING; 7955.ENSDARP00000106526; -.
DR PaxDb; Q2YDQ5; -.
DR ZFIN; ZDB-GENE-030131-900; fbxl5.
DR eggNOG; ENOG502QS5I; Eukaryota.
DR InParanoid; Q2YDQ5; -.
DR PhylomeDB; Q2YDQ5; -.
DR Reactome; R-DRE-8951664; Neddylation.
DR Reactome; R-DRE-917937; Iron uptake and transport.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q2YDQ5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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; 3.
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..679
FT /note="F-box/LRR-repeat protein 5"
FT /id="PRO_0000390466"
FT DOMAIN 205..251
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 316..342
FT /note="LRR 1"
FT REPEAT 343..367
FT /note="LRR 2"
FT REPEAT 368..395
FT /note="LRR 3"
FT REPEAT 396..426
FT /note="LRR 4"
FT REPEAT 565..595
FT /note="LRR 5"
FT REPEAT 596..623
FT /note="LRR 6"
FT REPEAT 624..649
FT /note="LRR 7"
FT REGION 1..159
FT /note="Hemerythrin-like"
FT /evidence="ECO:0000250"
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 679 AA; 75732 MW; 4C64AF1AD595FF24 CRC64;
MAPFPDEVDV FTGPHWRMKQ LVGLYSEKLS NTNFSNNRDF RSFLQSLLDT FTEFKKHEQI
ENECIMELLQ ERSHTVYHVH ADNKLSDMLT LFQKGLRSVT SEFEQLNYAQ QLKERLEAFT
QDFIPHMKEE EEVYQPMLME YFSYEELKAI KQQVMLQHCS SQCQSSCSDT HTLLKGLSLW
SHAELQKAFK YSDHEKTGDE RVLERVSVSS LPQELLLRIF RFLGPQDLCR CAQVCSVWTQ
VTRTGSLWRH LYPVRWARGE YYSGPPGDLD LEPDDDWIKS LQDDGRAYQE WDEDADVDES
EEASAERSSI SALQREKLLL NGIIQKLLPA VGSSVRSLSL AYSSTLSSKM VRQMLSLCPN
LTHLDLTQTD VSDSAFDSWC ALGACGTLQH LDLSGCDKIT DRTLKILSVG LGDSSTPSPA
HKLLQAPPSP IRIEEPRLQP MGRSCQDLIF KRRPGGRGSG CGPTHIWVLD PVKLADIEDA
ADWSRRGGVA SQEIGCGGIS EALSASCCCR RSQRRGFRTG LSSSPWQYGD ALCGHSSCCS
SDAAAIRTQS DLQATGGSAE LRTKCWFEGQ SCAEHHNRTD QSGAQRALRF LSLSGCHQIT
DLGLRCVCLR GGLPLLEHLN LSGCPLITGA GLQEVVSASP ALNIEHFYYC DNINGPHADT
ASGCQNLQCG FRVCCRSGE
