TRCB_XENLA
ID TRCB_XENLA Reviewed; 518 AA.
AC Q91854; P70037; P70038; Q6AX69;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Beta-TrCP;
DE AltName: Full=Beta-transducin repeat-containing protein;
GN Name=fbxw1; Synonyms=btrcp;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8393141; DOI=10.1128/mcb.13.8.4953-4966.1993;
RA Spevak W., Keiper B.D., Stratowa C., Castanon M.J.;
RT "Saccharomyces cerevisiae cdc15 mutants arrested at a late stage in
RT anaphase are rescued by Xenopus cDNAs encoding N-ras or a protein with
RT beta-transducin repeats.";
RL Mol. Cell. Biol. 13:4953-4966(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 302-518.
RX PubMed=8952061;
RX DOI=10.1002/(sici)1520-6408(1996)19:3<190::aid-dvg2>3.0.co;2-4;
RA Hudson J.W., Alarcon V.B., Elinson R.P.;
RT "Identification of new localized RNAs in the Xenopus oocyte by differential
RT display PCR.";
RL Dev. Genet. 19:190-198(1996).
RN [4]
RP INTERACTION WITH FBXO5.
RX PubMed=17159919; DOI=10.1038/sj.embor.7400853;
RA Bernis C., Vigneron S., Burgess A., Labbe J.C., Fesquet D., Castro A.,
RA Lorca T.;
RT "Pin1 stabilizes Emi1 during G2 phase by preventing its association with
RT SCF(betatrcp).";
RL EMBO Rep. 8:91-98(2007).
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. Probably recognizes and binds to phosphorylated target
CC proteins. May participate in Wnt signaling.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) ubiquitin-protein ligase
CC complex. Interacts with fbxo5 (PubMed:17159919). {ECO:0000250,
CC ECO:0000269|PubMed:17159919}.
CC -!- INTERACTION:
CC Q91854; Q91572: cpeb1-a; NbExp=2; IntAct=EBI-7161238, EBI-65730;
CC -!- DEVELOPMENTAL STAGE: Present in fully grown and progesterone-matured
CC oocytes. The level change very little even after zygotic gene
CC transcription begins following the midblastula transition. Do not
CC increase in abundance in the gastrula, neurula, tailbud, or tadpole
CC embryo.
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DR EMBL; M98268; AAA02810.1; -; mRNA.
DR EMBL; BC079732; AAH79732.1; -; mRNA.
DR EMBL; U63921; AAB49671.1; -; mRNA.
DR EMBL; U63922; AAB49672.1; -; mRNA.
DR PIR; B48088; B48088.
DR RefSeq; NP_001081064.1; NM_001087595.1.
DR AlphaFoldDB; Q91854; -.
DR SMR; Q91854; -.
DR BioGRID; 98964; 3.
DR DIP; DIP-44075N; -.
DR IntAct; Q91854; 2.
DR MINT; Q91854; -.
DR DNASU; 394362; -.
DR GeneID; 394362; -.
DR KEGG; xla:394362; -.
DR CTD; 394362; -.
DR Xenbase; XB-GENE-865578; btrc.S.
DR OrthoDB; 666965at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 394362; Expressed in egg cell and 19 other tissues.
DR GO; GO:0008013; F:beta-catenin binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0051219; F:phosphoprotein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
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; 6.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat;
KW Wnt signaling pathway.
FT CHAIN 1..518
FT /note="Beta-TrCP"
FT /id="PRO_0000050987"
FT DOMAIN 119..157
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 230..258
FT /note="WD 1"
FT REPEAT 270..298
FT /note="WD 2"
FT REPEAT 310..338
FT /note="WD 3"
FT REPEAT 353..381
FT /note="WD 4"
FT REPEAT 393..421
FT /note="WD 5"
FT REPEAT 433..461
FT /note="WD 6"
FT REPEAT 482..510
FT /note="WD 7"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 302..304
FT /note="GEM -> EFR (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 516..518
FT /note="GLA -> AAH (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 59507 MW; 2A52EC19028127F3 CRC64;
MEGFSCSLQP PTASEREDCN RDEPPRKIIT EKNTLRQTKL ANGTSSMIVP KQRKLSANYE
KEKELCVKYF EQWSECDQVE FVEHLISRMC HYQHGHINTY LKPMLQRDFI TALPARGLDH
IAENILSYLD AKSLCSAELV CKEWYRVTSD GMLWKKLIER MVRTDSLWRG LAERRGWGQY
LFKNKPPDGK TPPNSFYRAL YPKIIQDIET IESNWRCGRH SLQRIHCRSE TSKGVYCLQY
DDQKIVSGLR DNTIKIWDKN TLECKRVLMG HTGSVLCLQY DERVIITGSS DSTVRVWDVN
TGEMLNTLIH HCEAVLHLRF NNGMMVTCSK DRSIAVWDMA SATDITLRRV LVGHRAAVNV
VDFDDKYIVS ASGDRTIKVW NTSTCEFVRT LNGHKRGIAC LQYRDRLVVS GSSDNTIRLW
DIECGACLRV LEGHEELVRC IRFDNKRIVS GAYDGKIKVW DLVAALDPRA PAGTLCLRTL
VEHSGRVFRL QFDEFQIVSS SHDDTILIWD FLNDPGLA
