FB11A_DANRE
ID FB11A_DANRE Reviewed; 562 AA.
AC A0A2R8QFQ6; Q7ZVZ1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=F-box and WD repeat domain-containing 11-A {ECO:0000305};
GN Name=fbxw11a {ECO:0000312|ZFIN:ZDB-GENE-030131-6305};
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 (JAN-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=A0A2R8QFQ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A2R8QFQ6-2; Sequence=VSP_061015;
CC -!- DEVELOPMENTAL STAGE: At 4 days post fertilization (dpf), it is
CC expressed at low levels in the retina and brain, and at higher levels
CC in the jaw mesenchyme. {ECO:0000269|PubMed:31402090}.
CC -!- DOMAIN: The N-terminal D domain mediates homodimerization.
CC {ECO:0000250|UniProtKB:Q9UKB1}.
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; CABZ01001946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; LO018288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC045356; AAH45356.1; -; mRNA.
DR RefSeq; NP_958467.1; NM_201310.1. [A0A2R8QFQ6-2]
DR RefSeq; XP_005173126.1; XM_005173069.3. [A0A2R8QFQ6-1]
DR AlphaFoldDB; A0A2R8QFQ6; -.
DR SMR; A0A2R8QFQ6; -.
DR STRING; 7955.ENSDARP00000037531; -.
DR Ensembl; ENSDART00000167293; ENSDARP00000139358; ENSDARG00000104806. [A0A2R8QFQ6-2]
DR Ensembl; ENSDART00000188082; ENSDARP00000151798; ENSDARG00000104806. [A0A2R8QFQ6-1]
DR GeneID; 334373; -.
DR KEGG; dre:334373; -.
DR CTD; 334373; -.
DR ZFIN; ZDB-GENE-030131-6305; fbxw11a.
DR eggNOG; KOG0281; Eukaryota.
DR GeneTree; ENSGT00940000155898; -.
DR HOGENOM; CLU_000288_103_6_1; -.
DR OMA; RCATDYE; -.
DR OrthoDB; 666965at2759; -.
DR TreeFam; TF105679; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR ExpressionAtlas; A0A2R8QFQ6; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0030515; F:snoRNA binding; 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..562
FT /note="F-box and WD repeat domain-containing 11-A"
FT /id="PRO_0000452533"
FT DOMAIN 149..187
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 256..295
FT /note="WD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 296..335
FT /note="WD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 336..375
FT /note="WD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 379..418
FT /note="WD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 419..458
FT /note="WD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 459..491
FT /note="WD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 508..538
FT /note="WD 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 87..136
FT /note="Homodimerization domain D"
FT /evidence="ECO:0000250|UniProtKB:Q9UKB1"
FT VAR_SEQ 14..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_061015"
SQ SEQUENCE 562 AA; 64108 MW; A258CF8B008A5197 CRC64;
MDPDKEDKTL ELMCSLPRSV WLGCSSVAES LCALRCLQSL PSSRAHNQNM TGMESQINTD
EVSPKKTTVF KLGNGSLAGS RKRPSQGSFD KEKDLCIQLF DQWSESDQVE FVEHLIARMC
HYQHGHINSY LKPMLQRDFI TALPARGLDH IAENILSFLD ARSLCSAELV CREWQRVISD
GMLWKKLIER MVRTDPLWKG LSERHQWEKY LFKNRTNEVP PNSYYHSLYP KIIQDIETIE
ANWRCGRHNL QRIQCRSENS KGVYCLQYDD DKIISGLRDN SIKIWDKQSL ECLKVLTGHT
GSVLCLQYDE RVIVTGSSDS TVRVWDVSSG EVLNTLIHHN EAVLHLRFCN GLMVTCSKDR
SIAVWDMASA TDISLRRVLV GHRAAVNVVD FDDKYIVSAS GDRTIKVWST STCEFVRTLN
GHKRGIACLQ YRDRLVVSGS SDNTIRLWDI ECGACLRVLE GHEELVRCIR FDNKRIVSGA
YDGKIKVWDL QAALDPRAPA STLCLRTLVE HSGRVFRLQF DEFQIISSSH DDTILIWDFL
NVSSNGQSDG RSPSRTYTYV SR
