ID   FBXL5_PONAB             Reviewed;         691 AA.
AC   Q5R6E1;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   The German cDNA consortium;
RL   Submitted (NOV-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.
CC       Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued
CC       (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       Interacts with ACO1, IREB2/IRP2; the interaction depends on the 4Fe-4S
CC       cluster. Interacts with DCTN1/p150-glued (By similarity).
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; CR860550; CAH92675.1; -; mRNA.
DR   RefSeq; NP_001126565.1; NM_001133093.1.
DR   AlphaFoldDB; Q5R6E1; -.
DR   SMR; Q5R6E1; -.
DR   STRING; 9601.ENSPPYP00000016331; -.
DR   GeneID; 100173556; -.
DR   KEGG; pon:100173556; -.
DR   CTD; 26234; -.
DR   eggNOG; ENOG502QS5I; Eukaryota.
DR   InParanoid; Q5R6E1; -.
DR   OrthoDB; 1282076at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; 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..691
FT                   /note="F-box/LRR-repeat protein 5"
FT                   /id="PRO_0000390465"
FT   DOMAIN          202..248
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REPEAT          340..364
FT                   /note="LRR 1"
FT   REPEAT          365..392
FT                   /note="LRR 2"
FT   REPEAT          393..418
FT                   /note="LRR 3"
FT   REPEAT          479..508
FT                   /note="LRR 4"
FT   REPEAT          576..607
FT                   /note="LRR 5"
FT   REPEAT          608..635
FT                   /note="LRR 6"
FT   REPEAT          636..661
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   691 AA;  78553 MW;  3F225397BAB6A674 CRC64;
     MAPFPEEVDV FTAPHWRTKQ LVGLYCDKLS KTNFSNNNDF RALLQSLYAT FKEFKMHEQI
     ENEYIIGLLQ QRSQTIYNVH SDNKLSEMLS LFEKGLKNVK NEYEQLNYAK QLKERLEAFT
     RDFLPHMKEE EEVFQPMLME YFTYEELKDI KKKVIAQHCS QKDTAELLRG LSLWNHAEER
     QKFFKYSVDE KSDKEAEVSE HSTGITHLPP EVMLSIFSYL NPQELCRCSQ VSMKWSQLTK
     TGSLWKHLYP VHWARGDWYS GPATGLDTEP DEEWVKNRKD ESRAFHEWDE DADIDESEES
     VEESIAISIA QMEKRLLHGL IHNVLPYVGT SVKTLVLAYS SAVSSKMVRQ ILELCPNLEH
     LDLTQTDISD SAFDSWSWLG CCQSLRHLDL SGCEKITDVA LEKISRALGI LTSHQSGFLK
     TSTSKITSTT WKNKDVTMQS TKQYAYLHDL TNKGIGEEID NEHPWTKPVS SENFTSPYLW
     MLDAEDLADI EDTVEWRHRN VESLCVVETA SNFSCSTSGC FSKDIVGLRT SVCWQQHCAS
     PAFAYCGHSF CCTGTALRTM SALPESSAMC RKASRTRLPR GKDLIYFGSE KSDQETGRVL
     LFLSLSGCYQ ITDHGLRVLT LGGGLPYLEH LNLSGCLTIT GAGLQDLVSA CPSLNDEYFY
     YCDNINGPHA DTASGCQNLQ CGFRACCRSG E