FBXL5_HUMAN
ID FBXL5_HUMAN Reviewed; 691 AA.
AC Q9UKA1; A8MSK4; B4DIB5; Q4W5A8; Q8NHP3; Q9NXN2; Q9P0I0; Q9P0X5; Q9UJT7;
AC Q9UKC8;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=F-box/LRR-repeat protein 5;
DE AltName: Full=F-box and leucine-rich repeat protein 5;
DE AltName: Full=F-box protein FBL4/FBL5;
DE AltName: Full=p45SKP2-like protein;
GN Name=FBXL5; Synonyms=FBL4, FBL5, FLR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10531037; DOI=10.1016/s0960-9822(00)80021-4;
RA Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.;
RT "A family of mammalian F-box proteins.";
RL Curr. Biol. 9:1180-1182(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10945468; DOI=10.1006/geno.2000.6211;
RA Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.;
RT "cDNA cloning and expression analysis of new members of the mammalian F-box
RT protein family.";
RL Genomics 67:40-47(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Shimbara N.;
RT "cDNA cloning of a new human protein, FLR1, containing both motifs of F-box
RT and leucine-rich repeat.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 56-691 (ISOFORMS 1/2).
RC TISSUE=Colon, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-691 (ISOFORM 1).
RC TISSUE=Adrenal gland;
RA Huang C., Zhang C., Wu T., Peng Y., Gu Y., Jin Y., Jiang C., Li Y., Han Z.,
RA Wang Y., Chen Z., Fu G.;
RT "A novel gene expressed in the human adrenal gland.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 157-691 (ISOFORMS 1/2).
RX PubMed=10531035; DOI=10.1016/s0960-9822(00)80020-2;
RA Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M.,
RA Pagano M.;
RT "Identification of a family of human F-box proteins.";
RL Curr. Biol. 9:1177-1179(1999).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DCTN1.
RX PubMed=17532294; DOI=10.1016/j.bbrc.2007.05.068;
RA Zhang N., Liu J., Ding X., Aikhionbare F., Jin C., Yao X.;
RT "FBXL5 interacts with p150Glued and regulates its ubiquitination.";
RL Biochem. Biophys. Res. Commun. 359:34-39(2007).
RN [12]
RP FUNCTION, INTERACTION WITH ACO1 AND IREB2, IDENTIFICATION IN A SCF PROTEIN
RP LIGASE COMPLEX, IRON-BINDING, DOMAIN HEMERYTHRIN-LIKE, UBIQUITINATION, AND
RP MUTAGENESIS OF HIS-15 AND HIS-57.
RX PubMed=19762596; DOI=10.1126/science.1176333;
RA Vashisht A.A., Zumbrennen K.B., Huang X., Powers D.N., Durazo A., Sun D.,
RA Bhaskaran N., Persson A., Uhlen M., Sangfelt O., Spruck C., Leibold E.A.,
RA Wohlschlegel J.A.;
RT "Control of iron homeostasis by an iron-regulated ubiquitin ligase.";
RL Science 326:718-721(2009).
RN [13]
RP FUNCTION, INTERACTION WITH ACO1 AND IREB2, IDENTIFICATION IN A SCF PROTEIN
RP LIGASE COMPLEX, IRON-BINDING, DOMAIN HEMERYTHRIN-LIKE, UBIQUITINATION, AND
RP MUTAGENESIS OF HIS-57 AND GLU-61.
RX PubMed=19762597; DOI=10.1126/science.1176326;
RA Salahudeen A.A., Thompson J.W., Ruiz J.C., Ma H.-W., Kinch L.N., Li Q.,
RA Grishin N.V., Bruick R.K.;
RT "An E3 ligase possessing an iron responsive hemerythrin domain is a
RT regulator of iron homeostasis.";
RL Science 326:722-726(2009).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-160, AND IRON-BINDING SITES.
RX PubMed=22492618; DOI=10.1002/cbic.201200043;
RA Shu C., Sung M.W., Stewart M.D., Igumenova T.I., Tan X., Li P.;
RT "The structural basis of iron sensing by the human F-box protein FBXL5.";
RL ChemBioChem 13:788-791(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-161, AND IRON-BINDING SITES.
RX PubMed=22253436; DOI=10.1074/jbc.m111.308684;
RA Thompson J.W., Salahudeen A.A., Chollangi S., Ruiz J.C., Brautigam C.A.,
RA Makris T.M., Lipscomb J.D., Tomchick D.R., Bruick R.K.;
RT "Structural and molecular characterization of iron-sensing hemerythrin-like
RT domain within F-box and leucine-rich repeat protein 5 (FBXL5).";
RL J. Biol. Chem. 287:7357-7365(2012).
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 {ECO:0000269|PubMed:17532294, ECO:0000269|PubMed:19762596,
CC ECO:0000269|PubMed:19762597}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC Interacts with ACO1/IRP1, IREB2/IRP2; the interaction depends on the
CC 4Fe-4S cluster. Interacts with DCTN1/p150-glued.
CC {ECO:0000269|PubMed:17532294, ECO:0000269|PubMed:19762596,
CC ECO:0000269|PubMed:19762597}.
CC -!- INTERACTION:
CC Q9UKA1; P63208: SKP1; NbExp=12; IntAct=EBI-2692340, EBI-307486;
CC Q9UKA1; Q13148: TARDBP; NbExp=3; IntAct=EBI-2692340, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:17532294}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UKA1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKA1-2; Sequence=VSP_008417;
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.
CC {ECO:0000269|PubMed:19762596, ECO:0000269|PubMed:19762597}.
CC -!- PTM: Polybiquitinated 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.
CC {ECO:0000269|PubMed:19762596, ECO:0000269|PubMed:19762597}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF66616.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAF67489.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH30656.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAW92737.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF176700; AAF03700.1; -; mRNA.
DR EMBL; AF199420; AAF09249.1; -; mRNA.
DR EMBL; AF142481; AAF66616.1; ALT_INIT; mRNA.
DR EMBL; AK000153; BAA90978.1; -; mRNA.
DR EMBL; AK295510; BAG58427.1; -; mRNA.
DR EMBL; BX537957; CAD97924.1; -; mRNA.
DR EMBL; AC114744; AAY40929.1; -; Genomic_DNA.
DR EMBL; AC116651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471069; EAW92737.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471069; EAW92739.1; -; Genomic_DNA.
DR EMBL; BC030656; AAH30656.1; ALT_INIT; mRNA.
DR EMBL; AF157323; AAF67489.1; ALT_INIT; mRNA.
DR EMBL; AF174591; AAF04512.1; -; mRNA.
DR CCDS; CCDS3415.1; -. [Q9UKA1-1]
DR CCDS; CCDS54745.1; -. [Q9UKA1-2]
DR RefSeq; NP_001180463.1; NM_001193534.1.
DR RefSeq; NP_001180464.1; NM_001193535.1. [Q9UKA1-2]
DR RefSeq; NP_036293.1; NM_012161.3. [Q9UKA1-1]
DR PDB; 3U9J; X-ray; 1.60 A; A/B=1-160.
DR PDB; 3U9M; X-ray; 1.95 A; A/C/E/G=1-160.
DR PDB; 3V5X; X-ray; 1.85 A; A/B=1-161.
DR PDB; 3V5Y; X-ray; 2.10 A; A/B/C/D=1-161.
DR PDB; 3V5Z; X-ray; 2.18 A; A/B=1-161.
DR PDB; 6VCD; EM; 3.00 A; B=200-691.
DR PDBsum; 3U9J; -.
DR PDBsum; 3U9M; -.
DR PDBsum; 3V5X; -.
DR PDBsum; 3V5Y; -.
DR PDBsum; 3V5Z; -.
DR PDBsum; 6VCD; -.
DR AlphaFoldDB; Q9UKA1; -.
DR SMR; Q9UKA1; -.
DR BioGRID; 117625; 44.
DR IntAct; Q9UKA1; 30.
DR MINT; Q9UKA1; -.
DR STRING; 9606.ENSP00000344866; -.
DR iPTMnet; Q9UKA1; -.
DR PhosphoSitePlus; Q9UKA1; -.
DR BioMuta; FBXL5; -.
DR DMDM; 37537864; -.
DR MassIVE; Q9UKA1; -.
DR PaxDb; Q9UKA1; -.
DR PeptideAtlas; Q9UKA1; -.
DR PRIDE; Q9UKA1; -.
DR ProteomicsDB; 84748; -. [Q9UKA1-1]
DR ProteomicsDB; 84749; -. [Q9UKA1-2]
DR Antibodypedia; 9778; 205 antibodies from 28 providers.
DR DNASU; 26234; -.
DR Ensembl; ENST00000341285.8; ENSP00000344866.3; ENSG00000118564.15. [Q9UKA1-1]
DR Ensembl; ENST00000412094.6; ENSP00000408679.2; ENSG00000118564.15. [Q9UKA1-2]
DR GeneID; 26234; -.
DR KEGG; hsa:26234; -.
DR MANE-Select; ENST00000341285.8; ENSP00000344866.3; NM_012161.4; NP_036293.1.
DR UCSC; uc003goc.3; human. [Q9UKA1-1]
DR CTD; 26234; -.
DR DisGeNET; 26234; -.
DR GeneCards; FBXL5; -.
DR HGNC; HGNC:13602; FBXL5.
DR HPA; ENSG00000118564; Low tissue specificity.
DR MIM; 605655; gene.
DR neXtProt; NX_Q9UKA1; -.
DR OpenTargets; ENSG00000118564; -.
DR PharmGKB; PA28025; -.
DR VEuPathDB; HostDB:ENSG00000118564; -.
DR eggNOG; ENOG502QS5I; Eukaryota.
DR GeneTree; ENSGT00390000006172; -.
DR HOGENOM; CLU_017503_0_0_1; -.
DR InParanoid; Q9UKA1; -.
DR OMA; GEMFCGH; -.
DR OrthoDB; 1282076at2759; -.
DR PhylomeDB; Q9UKA1; -.
DR TreeFam; TF331105; -.
DR PathwayCommons; Q9UKA1; -.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9UKA1; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 26234; 30 hits in 1121 CRISPR screens.
DR ChiTaRS; FBXL5; human.
DR GeneWiki; FBXL5; -.
DR GenomeRNAi; 26234; -.
DR Pharos; Q9UKA1; Tbio.
DR PRO; PR:Q9UKA1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UKA1; protein.
DR Bgee; ENSG00000118564; Expressed in monocyte and 213 other tissues.
DR ExpressionAtlas; Q9UKA1; baseline and differential.
DR Genevisible; Q9UKA1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; NAS:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA: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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Iron; Leucine-rich repeat;
KW Metal-binding; Reference proteome; Repeat; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..691
FT /note="F-box/LRR-repeat protein 5"
FT /id="PRO_0000119845"
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 BINDING 15
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 80
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT VAR_SEQ 29..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_008417"
FT MUTAGEN 15
FT /note="H->A: Abolishes iron-binding and promotes its
FT degradation."
FT /evidence="ECO:0000269|PubMed:19762596"
FT MUTAGEN 57
FT /note="H->A: Abolishes iron-binding and promotes its
FT degradation."
FT /evidence="ECO:0000269|PubMed:19762596,
FT ECO:0000269|PubMed:19762597"
FT MUTAGEN 61
FT /note="E->A: Abolishes iron-binding and promotes its
FT degradation."
FT /evidence="ECO:0000269|PubMed:19762597"
FT CONFLICT 52
FT /note="K -> T (in Ref. 8; AAH30656)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="Missing (in Ref. 2; AAF09249)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="G -> R (in Ref. 8; AAH30656)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="V -> I (in Ref. 4; BAA90978)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:3U9J"
FT HELIX 12..31
FT /evidence="ECO:0007829|PDB:3U9J"
FT HELIX 37..64
FT /evidence="ECO:0007829|PDB:3U9J"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:3U9J"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:3U9J"
FT HELIX 102..132
FT /evidence="ECO:0007829|PDB:3U9J"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:3U9J"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:3U9J"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:6VCD"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:6VCD"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6VCD"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:6VCD"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6VCD"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:6VCD"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:6VCD"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:6VCD"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6VCD"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:6VCD"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:6VCD"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:6VCD"
FT TURN 350..354
FT /evidence="ECO:0007829|PDB:6VCD"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:6VCD"
FT TURN 370..375
FT /evidence="ECO:0007829|PDB:6VCD"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:6VCD"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:6VCD"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:6VCD"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:6VCD"
FT HELIX 613..617
FT /evidence="ECO:0007829|PDB:6VCD"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:6VCD"
FT HELIX 641..648
FT /evidence="ECO:0007829|PDB:6VCD"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:6VCD"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:6VCD"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:6VCD"
SQ SEQUENCE 691 AA; 78555 MW; 923A1B31590E5145 CRC64;
MAPFPEEVDV FTAPHWRMKQ LVGLYCDKLS KTNFSNNNDF RALLQSLYAT FKEFKMHEQI
ENEYIIGLLQ QRSQTIYNVH SDNKLSEMLS LFEKGLKNVK NEYEQLNYAK QLKERLEAFT
RDFLPHMKEE EEVFQPMLME YFTYEELKDI KKKVIAQHCS QKDTAELLRG LSLWNHAEER
QKFFKYSVDE KSDKEAEVSE HSTGITHLPP EVMLSIFSYL NPQELCRCSQ VSMKWSQLTK
TGSLWKHLYP VHWARGDWYS GPATELDTEP DDEWVKNRKD ESRAFHEWDE DADIDESEES
AEESIAISIA QMEKRLLHGL IHNVLPYVGT SVKTLVLAYS SAVSSKMVRQ ILELCPNLEH
LDLTQTDISD SAFDSWSWLG CCQSLRHLDL SGCEKITDVA LEKISRALGI LTSHQSGFLK
TSTSKITSTA WKNKDITMQS TKQYACLHDL TNKGIGEEID NEHPWTKPVS SENFTSPYVW
MLDAEDLADI EDTVEWRHRN VESLCVMETA SNFSCSTSGC FSKDIVGLRT SVCWQQHCAS
PAFAYCGHSF CCTGTALRTM SSLPESSAMC RKAARTRLPR GKDLIYFGSE KSDQETGRVL
LFLSLSGCYQ ITDHGLRVLT LGGGLPYLEH LNLSGCLTIT GAGLQDLVSA CPSLNDEYFY
YCDNINGPHA DTASGCQNLQ CGFRACCRSG E
