FB11B_DANRE
ID FB11B_DANRE Reviewed; 534 AA.
AC A0A2R8RWN9; Q6PGW4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=F-box and WD repeat domain-containing 11-B {ECO:0000305};
GN Name=fbxw11b {ECO:0000312|ZFIN:ZDB-GENE-040426-2903};
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] (ISOFORM 2).
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=31402090; DOI=10.1016/j.ajhg.2019.07.005;
RA Holt R.J., Young R.M., Crespo B., Ceroni F., Curry C.J., Bellacchio E.,
RA Bax D.A., Ciolfi A., Simon M., Fagerberg C.R., van Binsbergen E.,
RA De Luca A., Memo L., Dobyns W.B., Mohammed A.A., Clokie S.J.H.,
RA Zazo Seco C., Jiang Y.H., Soerensen K.P., Andersen H., Sullivan J.,
RA Powis Z., Chassevent A., Smith-Hicks C., Petrovski S., Antoniadi T.,
RA Shashi V., Gelb B.D., Wilson S.W., Gerrelli D., Tartaglia M., Chassaing N.,
RA Calvas P., Ragge N.K.;
RT "De novo missense variants in FBXW11 cause diverse developmental phenotypes
RT including brain, eye, and digit anomalies.";
RL Am. J. Hum. Genet. 105:640-657(2019).
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 (By similarity). Participates in Wnt signaling regulation, and
CC plays a role in eye and jaw development (PubMed:31402090).
CC {ECO:0000250|UniProtKB:Q9UKB1, ECO:0000269|PubMed:31402090}.
CC -!- SUBUNIT: Self-associates. Component of the SCF(FBXW11) complex.
CC {ECO:0000250|UniProtKB:Q9UKB1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UKB1}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UKB1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A2R8RWN9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A2R8RWN9-2; Sequence=VSP_061016, VSP_061017;
CC -!- DEVELOPMENTAL STAGE: At 4 days post fertilization (dpf), it is widely
CC expressed in the brain and eyes. There are high levels of expression in
CC the retinal ganglion layer, the inner nuclear layer, the photoreceptor
CC layer, the ciliary marginal zone, jaw mesenchyme, oral epithelia, and
CC pectoral fins. {ECO:0000269|PubMed:31402090}.
CC -!- DOMAIN: The N-terminal D domain mediates homodimerization.
CC {ECO:0000250|UniProtKB:Q9Y297}.
CC -!- DISRUPTION PHENOTYPE: Knockdown of both fbxw11a and fbxw11b results in
CC abnormally developed pectoral fins and heart edema by day 3 post-
CC fertilization (3 dpf). At 5 dpf, knocked-down embryos show periocular
CC edema, small and misshapen eyes, and abnormal development of the jaw.
CC {ECO:0000269|PubMed:31402090}.
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DR EMBL; BX465186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056809; AAH56809.1; -; mRNA.
DR RefSeq; NP_998669.2; NM_213504.2.
DR AlphaFoldDB; A0A2R8RWN9; -.
DR SMR; A0A2R8RWN9; -.
DR Ensembl; ENSDART00000179825; ENSDARP00000154765; ENSDARG00000112841. [A0A2R8RWN9-1]
DR Ensembl; ENSDART00000184386; ENSDARP00000145308; ENSDARG00000017230. [A0A2R8RWN9-2]
DR Ensembl; ENSDART00000189591; ENSDARP00000145691; ENSDARG00000112841. [A0A2R8RWN9-2]
DR GeneID; 406825; -.
DR KEGG; dre:406825; -.
DR CTD; 406825; -.
DR ZFIN; ZDB-GENE-040426-2903; fbxw11b.
DR GeneTree; ENSGT00940000155898; -.
DR HOGENOM; CLU_000288_103_6_1; -.
DR OrthoDB; 666965at2759; -.
DR TreeFam; TF105679; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0002040; P:sprouting angiogenesis; IGI:ZFIN.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR021977; Beta-TrCP_D.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12125; Beta-TrCP_D; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM01028; Beta-TrCP_D; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat; Wnt signaling pathway.
FT CHAIN 1..534
FT /note="F-box and WD repeat domain-containing 11-B"
FT /id="PRO_0000452534"
FT DOMAIN 121..159
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 228..267
FT /note="WD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 268..307
FT /note="WD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 308..347
FT /note="WD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 351..390
FT /note="WD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 391..430
FT /note="WD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 431..463
FT /note="WD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 480..510
FT /note="WD 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 59..108
FT /note="Homodimerization domain D"
FT /evidence="ECO:0000250|UniProtKB:Q9Y297"
FT VAR_SEQ 2..23
FT /note="FDLKQTLLLISELMHLFLLRLQ -> EDKTLEQM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_061016"
FT VAR_SEQ 43
FT /note="K -> KSTFICPQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_061017"
SQ SEQUENCE 534 AA; 61462 MW; 456DB32A94ECC53C CRC64;
MFDLKQTLLL ISELMHLFLL RLQNTSVMDP QTADRSPKIT LIKVSNGPLT GSRKRPSEGN
YEKEKDVCIQ LFDQWSEADQ VEFVEHLISR MCHYQHGHIN SYLKPMLQRD FITALPAQGL
DHIAENILSF LDARSLCSAE LVCKEWQRVI SEGMLWKKLI ERMVRTDPLW KGLSERHQWE
KYLFKNRTTE VPPNSYYRSL YPKIIQDIET IEANWRCGRH NLQRIQCRSE NSKGVYCLQY
DDEKIISGLR DNSIKIWDKQ TLECLKILTG HTGSVLCLQY DERVIVTGSS DSTVRVWDVN
SGEVLNTLIH HNEAVLHLRF CNGLMVTCSK DRSIAVWDMA SPTDISLRRV LVGHRAAVNV
VDFDDKYIVS ASGDRTIKVW STSTCEFVRT LNGHKRGIAC LQYRDRLVVS GSSDNTIRLW
DIECGACLRV LEGHEELVRC IRFDNKRIVS GAYDGKIKVW DLQAALDPRA PASTLCLRTL
VEHSGRVFRL QFDEFQIISS SHDDTILIWD FLNVSTNGQT EGRSPSRTYT YISR
