ID   FBW1B_MOUSE             Reviewed;         542 AA.
AC   Q5SRY7; Q3TGM9; Q3TLZ8; Q8BY90; Q8K022; Q923H0;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=F-box/WD repeat-containing protein 11;
DE   AltName: Full=F-box and WD repeats protein beta-TrCP2;
DE   AltName: Full=F-box/WD repeat-containing protein 1B;
DE   AltName: Full=Homologous to Slimb protein {ECO:0000303|PubMed:11896578};
DE            Short=HOS {ECO:0000303|PubMed:11896578};
GN   Name=Fbxw11; Synonyms=Btrcp2, Fbw1b, Fbxw1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PATHWAY, AND INTERACTION
RP   WITH SKP1 AND NFKBIA.
RC   STRAIN=FVB/N;
RX   PubMed=11896578; DOI=10.1038/sj.onc.1205311;
RA   Bhatia N., Herter J.R., Slaga T.J., Fuchs S.Y., Spiegelman V.S.;
RT   "Mouse homologue of HOS (mHOS) is overexpressed in skin tumors and
RT   implicated in constitutive activation of NF-kappaB.";
RL   Oncogene 21:1501-1509(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Kidney, Mammary gland, Osteoclast, Sympathetic ganglion, and
RC   Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   [5]
RP   INDUCTION.
RX   PubMed=11850814; DOI=10.1038/sj.onc.1205132;
RA   Spiegelman V.S., Tang W., Katoh M., Slaga T.J., Fuchs S.Y.;
RT   "Inhibition of HOS expression and activities by Wnt pathway.";
RL   Oncogene 21:856-860(2002).
RN   [6]
RP   INTERACTION WITH PER3.
RX   PubMed=15917222; DOI=10.1074/jbc.m502862200;
RA   Shirogane T., Jin J., Ang X.L., Harper J.W.;
RT   "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-
RT   dependent degradation of the mammalian period-1 (Per1) protein.";
RL   J. Biol. Chem. 280:26863-26872(2005).
RN   [7]
RP   FUNCTION IN CIRCADIAN RHYTHMS, AND SUBCELLULAR LOCATION.
RX   PubMed=18782782; DOI=10.1093/jb/mvn112;
RA   Ohsaki K., Oishi K., Kozono Y., Nakayama K., Nakayama K.I., Ishida N.;
RT   "The role of {beta}-TrCP1 and {beta}-TrCP2 in circadian rhythm generation
RT   by mediating degradation of clock protein PER2.";
RL   J. Biochem. 144:609-618(2008).
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 (PubMed:11896578). Probably recognizes and binds to
CC       phosphorylated target proteins: the interaction with substrates
CC       requires the phosphorylation of the two serine residues in the
CC       substrates' destruction motif D-S-G-X(2,3,4)-S (By similarity).
CC       SCF(FBXW11) mediates the ubiquitination of phosphorylated CTNNB1 and
CC       participates in Wnt signaling regulation (By similarity). SCF(FBXW11)
CC       plays a key role in NF-kappa-B activation by mediating ubiquitination
CC       of phosphorylated NFKBIA, leading to its degradation by the proteasome,
CC       thereby allowing the associated NF-kappa-B complex to translocate into
CC       the nucleus and to activate transcription (PubMed:11896578). The
CC       SCF(FBXW11) complex also regulates NF-kappa-B by mediating
CC       ubiquitination of phosphorylated NFKB1: specifically ubiquitinates the
CC       p105 form of NFKB1, leading to its degradation (By similarity).
CC       SCF(FBXW11) mediates the ubiquitination of IFNAR1 (By similarity).
CC       SCF(FBXW11) mediates the ubiquitination of CEP68; this is required for
CC       centriole separation during mitosis (By similarity). Involved in the
CC       oxidative stress-induced a ubiquitin-mediated decrease in RCAN1 (By
CC       similarity). Mediates the degradation of CDC25A induced by ionizing
CC       radiation in cells progressing through S phase and thus may function in
CC       the intra-S-phase checkpoint (By similarity). Has an essential role in
CC       the control of the clock-dependent transcription via degradation of
CC       phosphorylated PER1 and phosphorylated PER2 (PubMed:18782782).
CC       SCF(FBXW11) mediates the ubiquitination of CYTH1, and probably CYTH2
CC       (By similarity). SCF(FBXW11) acts as a regulator of mTORC1 signaling
CC       pathway by catalyzing ubiquitination and subsequent proteasomal
CC       degradation of phosphorylated DEPTOR, TFE3 and MITF (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UKB1, ECO:0000269|PubMed:11896578,
CC       ECO:0000269|PubMed:18782782}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000269|PubMed:11896578}.
CC   -!- SUBUNIT: Self-associates (By similarity). Component of the SCF(FBXW11)
CC       complex formed of CUL1, SKP1, RBX1 and a FBXW11 dimer
CC       (PubMed:11896578). Interacts with BST2 and USP47 (By similarity).
CC       Interacts with TRIM21 (By similarity). Interacts with PER3
CC       (PubMed:15917222). Interacts with INAVA (By similarity). Interacts with
CC       REST (By similarity). {ECO:0000250|UniProtKB:Q9UKB1,
CC       ECO:0000269|PubMed:11896578, ECO:0000269|PubMed:15917222}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18782782}. Nucleus
CC       {ECO:0000269|PubMed:18782782}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q5SRY7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SRY7-2; Sequence=VSP_039581;
CC       Name=3;
CC         IsoId=Q5SRY7-3; Sequence=VSP_039580;
CC       Name=4;
CC         IsoId=Q5SRY7-4; Sequence=VSP_039579;
CC   -!- INDUCTION: Expression is negatively regulated by Wnt/beta-catenin
CC       pathway. {ECO:0000269|PubMed:11850814}.
CC   -!- DOMAIN: The N-terminal D domain mediates homodimerization.
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK72095.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY038079; AAK72095.1; ALT_FRAME; mRNA.
DR   EMBL; AK041532; BAC30975.1; -; mRNA.
DR   EMBL; AK149139; BAE28749.1; -; mRNA.
DR   EMBL; AK152181; BAE31012.1; -; mRNA.
DR   EMBL; AK160086; BAE35617.1; -; mRNA.
DR   EMBL; AK166226; BAE38644.1; -; mRNA.
DR   EMBL; AK168667; BAE40519.1; -; mRNA.
DR   EMBL; AL669844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL669951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC034261; AAH34261.1; -; mRNA.
DR   CCDS; CCDS36125.1; -. [Q5SRY7-2]
DR   CCDS; CCDS70157.1; -. [Q5SRY7-1]
DR   CCDS; CCDS70158.1; -. [Q5SRY7-3]
DR   RefSeq; NP_001258276.1; NM_001271347.1. [Q5SRY7-1]
DR   RefSeq; NP_001258277.1; NM_001271348.1. [Q5SRY7-3]
DR   RefSeq; NP_001258278.1; NM_001271349.1. [Q5SRY7-4]
DR   RefSeq; NP_598776.1; NM_134015.3. [Q5SRY7-2]
DR   AlphaFoldDB; Q5SRY7; -.
DR   SMR; Q5SRY7; -.
DR   BioGRID; 222123; 36.
DR   DIP; DIP-59921N; -.
DR   IntAct; Q5SRY7; 22.
DR   MINT; Q5SRY7; -.
DR   STRING; 10090.ENSMUSP00000075721; -.
DR   iPTMnet; Q5SRY7; -.
DR   PhosphoSitePlus; Q5SRY7; -.
DR   SwissPalm; Q5SRY7; -.
DR   EPD; Q5SRY7; -.
DR   MaxQB; Q5SRY7; -.
DR   PaxDb; 10090-ENSMUSP00000075721; -.
DR   PeptideAtlas; Q5SRY7; -.
DR   ProteomicsDB; 270960; -. [Q5SRY7-1]
DR   ProteomicsDB; 270961; -. [Q5SRY7-2]
DR   ProteomicsDB; 270962; -. [Q5SRY7-3]
DR   ProteomicsDB; 270963; -. [Q5SRY7-4]
DR   Pumba; Q5SRY7; -.
DR   Antibodypedia; 28871; 269 antibodies from 29 providers.
DR   DNASU; 103583; -.
DR   Ensembl; ENSMUST00000076383.8; ENSMUSP00000075721.8; ENSMUSG00000020271.18. [Q5SRY7-2]
DR   Ensembl; ENSMUST00000093205.13; ENSMUSP00000090893.7; ENSMUSG00000020271.18. [Q5SRY7-1]
DR   Ensembl; ENSMUST00000109366.8; ENSMUSP00000104991.2; ENSMUSG00000020271.18. [Q5SRY7-3]
DR   GeneID; 103583; -.
DR   KEGG; mmu:103583; -.
DR   UCSC; uc007ijx.2; mouse. [Q5SRY7-2]
DR   UCSC; uc007ijy.2; mouse. [Q5SRY7-3]
DR   UCSC; uc007ijz.2; mouse. [Q5SRY7-1]
DR   UCSC; uc007ika.2; mouse. [Q5SRY7-4]
DR   AGR; MGI:2144023; -.
DR   CTD; 23291; -.
DR   MGI; MGI:2144023; Fbxw11.
DR   VEuPathDB; HostDB:ENSMUSG00000020271; -.
DR   eggNOG; KOG0281; Eukaryota.
DR   GeneTree; ENSGT00940000155898; -.
DR   HOGENOM; CLU_000288_103_6_1; -.
DR   InParanoid; Q5SRY7; -.
DR   OMA; PTHTACY; -.
DR   OrthoDB; 337075at2759; -.
DR   TreeFam; TF105679; -.
DR   Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-MMU-202424; Downstream TCR signaling.
DR   Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-MMU-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 103583; 27 hits in 81 CRISPR screens.
DR   ChiTaRS; Fbxw11; mouse.
DR   PRO; PR:Q5SRY7; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5SRY7; Protein.
DR   Bgee; ENSMUSG00000020271; Expressed in endocardial cushion and 255 other cell types or tissues.
DR   ExpressionAtlas; Q5SRY7; baseline and differential.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR   GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR   GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0048854; P:brain morphogenesis; IBA:GO_Central.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR   GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR   GO; GO:0031023; P:microtubule organizing center organization; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; IMP:UniProtKB.
DR   GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:MGI.
DR   GO; GO:0042753; P:positive regulation of circadian rhythm; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB.
DR   GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR   GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0008090; P:retrograde axonal transport; IBA:GO_Central.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd22183; F-box_FBXW1B; 1.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   Gene3D; 6.10.250.1840; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR14604:SF6; F-BOX AND WD REPEAT DOMAIN-CONTAINING 11-B; 1.
DR   PANTHER; PTHR14604; WD40 REPEAT PF20; 1.
DR   Pfam; PF12125; Beta-TrCP_D; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF00400; WD40; 7.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM01028; Beta-TrCP_D; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 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.
DR   Genevisible; Q5SRY7; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Biological rhythms; Cell cycle; Cytoplasm; Nucleus;
KW   Reference proteome; Repeat; Ubl conjugation pathway; WD repeat;
KW   Wnt signaling pathway.
FT   CHAIN           1..542
FT                   /note="F-box/WD repeat-containing protein 11"
FT                   /id="PRO_0000396126"
FT   DOMAIN          121..167
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REPEAT          238..275
FT                   /note="WD 1"
FT   REPEAT          278..315
FT                   /note="WD 2"
FT   REPEAT          318..355
FT                   /note="WD 3"
FT   REPEAT          361..398
FT                   /note="WD 4"
FT   REPEAT          401..440
FT                   /note="WD 5"
FT   REPEAT          442..478
FT                   /note="WD 6"
FT   REPEAT          490..527
FT                   /note="WD 7"
FT   REGION          67..116
FT                   /note="Homodimerization domain D"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         16..49
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_039579"
FT   VAR_SEQ         16..48
FT                   /note="CSVPRSLWLGCANLVESMCALSCLQSMPSVRCL -> NTSVMEDQNEDESPK
FT                   KSALW (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_039580"
FT   VAR_SEQ         49
FT                   /note="Q -> QNTSVMEDQNEDESPKKSALWQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11896578,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_039581"
FT   CONFLICT        219
FT                   /note="I -> V (in Ref. 2; BAE38644)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        534
FT                   /note="S -> F (in Ref. 1; AAK72095)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   542 AA;  62063 MW;  D95A78A6977B828A CRC64;
     MEPDSVIEDK TIELMCSVPR SLWLGCANLV ESMCALSCLQ SMPSVRCLQI SNGTSSVIVS
     RKRPSEGNYQ KEKDLCIKYF DQWSESDQVE FVEHLISRMC HYQHGHINSY LKPMLQRDFI
     TALPEQGLDH IAENILSYLD ARSLCAAELV CKEWQRVISE GMLWKKLIER MVRTDPLWKG
     LSERRGWDQY LFKNRPTDGP PNSFYRSLYP KIIQDIETIE SNWRCGRHNL QRIQCRSENS
     KGVYCLQYDD DKIISGLRDN SIKIWDKSSL ECLKVLTGHT GSVLCLQYDE RVIVTGSSDS
     TVRVWDVNTG EVLNTLIHHN EAVLHLRFSN GLMVTCSKDR SIAVWDMASA TDITLRRVLV
     GHRAAVNVVD FDDKYIVSAS GDRTIKVWST STCEFVRTLN GHKRGIACLQ YRDRLVVSGS
     SDNTIRLWDI ECGACLRVLE GHEELVRCIR FDNKRIVSGA YDGKIKVWDL QAALDPRAPA
     STLCLRTLVE HSGRVFRLQF DEFQIISSSH DDTILIWDFL NVPPSAQNET RSPSRTYTYI
     SR
//