FBXL5_SALSA
ID FBXL5_SALSA Reviewed; 696 AA.
AC C0HAC0;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=F-box/LRR-repeat protein 5;
DE AltName: Full=F-box and leucine-rich repeat protein 5;
GN Name=fbxl5;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
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; BT059276; ACN10989.1; -; mRNA.
DR RefSeq; XP_013978382.1; XM_014122907.1.
DR AlphaFoldDB; C0HAC0; -.
DR SMR; C0HAC0; -.
DR STRING; 8030.ENSSSAP00000082709; -.
DR GeneID; 106560246; -.
DR KEGG; sasa:106560246; -.
DR OrthoDB; 1282076at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000087266; Chromosome ssa10.
DR Bgee; ENSSSAG00000067925; Expressed in ovary and 16 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; 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..696
FT /note="F-box/LRR-repeat protein 5"
FT /id="PRO_0000390467"
FT DOMAIN 205..251
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 343..367
FT /note="LRR 1"
FT REPEAT 368..395
FT /note="LRR 2"
FT REPEAT 396..421
FT /note="LRR 3"
FT REPEAT 582..612
FT /note="LRR 4"
FT REPEAT 613..640
FT /note="LRR 5"
FT REPEAT 641..666
FT /note="LRR 6"
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 696 AA; 78309 MW; 4E5C4E0890331365 CRC64;
MAPFPDEVDV FTGPHWRMKQ LVGLYCEKLS QTNFSNNNDF RSFLQSLCAT FKEFKMHEQI
ENEYIIGLLQ QRSCNVYNVH SDNKLSEMLS LFEKGLRSVK SENEQLNYAQ QLKERLEAFT
QDFLPHMKEE EEVFQPMLMQ YFTYEELKDI KKQVIAQHSS QQRWDCAAEV LKGLSLWSQA
EELHKAFKYA DHEKTDDELE KELCSTHISQ LPTEILLCLF RYLGPEDLCH CGQVCSAWSD
LAKTGSLWRH LYPVRWARGD YYRGPPDDVN QEPDEEWVKS LQDEGKAYQE WDEDADVDES
DASCEDSLAI SAAQREKKLL NGMIQNLLPA VGSSVRSIVL AYSSTVSSKM VRQILSLCPN
LTHLDLTQTD VTDSAFDSWS SLWACLSLEH LDLSGCEKLT DRTLKKLSLG LGDLASPTCS
EKRSDRRAKL LKSPPSPISL LDKRSLRPTG HSRQVLIFKQ WPGKLGSAPC SPTRVWVLDA
SELADIEDAA EWNRRRGVST PEVRGFVETQ PGGLSCCCRR RRGGFRTGFS TSYWQQQYGL
GEAGCGHSTC CTGETALRTL GGLQYESYTT RGSAGAEFRT KCSSGGQLCL ECDNRTDPSD
GRRSLRFLSL SGCYQVTDLG LRALSQRGGL PLLEHLNLSG CLLITEVGLQ ELVSACPALN
DEHFYYCDNI NGPHADTASG CQNLQCGFRV CCRSGE
