FBXL7_DANRE
ID FBXL7_DANRE Reviewed; 489 AA.
AC A1A5X2;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=F-box/LRR-repeat protein 7;
DE AltName: Full=F-box and leucine-rich repeat protein 7;
GN Name=fbxl7; ORFNames=zgc:158346;
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000250|UniProtKB:Q9UJT9}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9UJT9}.
CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC complex SCF(FBXL7). {ECO:0000250|UniProtKB:Q5BJ29}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q5BJ29}. Note=Localizes to
CC the centrosome during spindle formation.
CC {ECO:0000250|UniProtKB:Q5BJ29}.
CC -!- SIMILARITY: Belongs to the FBXL7 family. {ECO:0000305}.
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DR EMBL; CR450710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC128845; AAI28846.1; -; mRNA.
DR EMBL; BC129207; AAI29208.1; -; mRNA.
DR RefSeq; NP_001073511.1; NM_001080042.1.
DR AlphaFoldDB; A1A5X2; -.
DR SMR; A1A5X2; -.
DR STRING; 7955.ENSDARP00000084255; -.
DR PaxDb; A1A5X2; -.
DR PeptideAtlas; A1A5X2; -.
DR Ensembl; ENSDART00000089822; ENSDARP00000084255; ENSDARG00000062251.
DR GeneID; 569430; -.
DR KEGG; dre:569430; -.
DR CTD; 23194; -.
DR ZFIN; ZDB-GENE-061215-122; fbxl7.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000158009; -.
DR HOGENOM; CLU_016072_5_0_1; -.
DR InParanoid; A1A5X2; -.
DR OMA; MIYCASI; -.
DR OrthoDB; 1027299at2759; -.
DR PhylomeDB; A1A5X2; -.
DR TreeFam; TF313434; -.
DR Reactome; R-DRE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-DRE-8951664; Neddylation.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:A1A5X2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000062251; Expressed in spleen and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
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; PF13516; LRR_6; 4.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 10.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Leucine-rich repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..489
FT /note="F-box/LRR-repeat protein 7"
FT /id="PRO_0000417991"
FT DOMAIN 109..155
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 168..193
FT /note="LRR 1"
FT REPEAT 194..219
FT /note="LRR 2"
FT REPEAT 220..245
FT /note="LRR 3"
FT REPEAT 251..279
FT /note="LRR 4"
FT REPEAT 280..305
FT /note="LRR 5"
FT REPEAT 306..331
FT /note="LRR 6"
FT REPEAT 332..357
FT /note="LRR 7"
FT REPEAT 358..383
FT /note="LRR 8"
FT REPEAT 384..409
FT /note="LRR 9"
FT REPEAT 410..435
FT /note="LRR 10"
FT REPEAT 436..461
FT /note="LRR 11"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 54220 MW; 4C611A29877AB9D5 CRC64;
MGANNGKQSG SEGKGSSSIS SDLSSSTDQT STKAPKNAAT SEDSDLSMRT VSTPSPALIL
PPRSSSAVLN GSSTSSSTFG TETIAMVHMP PTSLTHPQRC LRQPRDQQGA PVDILPDHAF
LQIFTHLPTN QLCRCARVCR RWYNLAWDPR LWRTIRLTGD VLHVDRALRV LTRRLCQDTP
NVCLTVETVM VSGCRRLTDR GLYTVAQSCP ELRRLEVAGC YNVSNEAVFE VVSRCPNLEH
LDVSGCSKVT CISLTRDVSV KLSPLHGQQI SIRFLDMTDC FALEDEGLHT IAAHCTQLTH
LYLRRCVRLT DEGLRFLVIY CPGVRELSVS DCRFISDFGL REIAKLEGRL RYLSIAHCSR
ITDVGVRYVA KYCSRLRYLN ARGCEGLTDH GIEHLAKSCL KLKSLDIGKC PLVSDAGLEQ
LALNSFNLKR LSLKSCESIT GRGLQVVAAN CFDLQLLNVQ DCDVSLEALR FVKRHCKRCI
IEHTNPAFF
