FBX43_XENLA
ID FBX43_XENLA Reviewed; 651 AA.
AC Q8AXF4; Q9PTL8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=F-box only protein 43;
DE AltName: Full=Early mitotic inhibitor 2;
DE AltName: Full=Emi1-related protein 1;
DE AltName: Full=F-box protein 26;
DE AltName: Full=Xerp1;
GN Name=fbxo43; Synonyms=emi2, erp1, fbx26;
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=10531041; DOI=10.1016/s0960-9822(00)80006-8;
RA Regan-Reimann J.D., Duong Q.V., Jackson P.K.;
RT "Identification of novel F-box proteins in Xenopus laevis.";
RL Curr. Biol. 9:R762-R763(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP PHOSPHORYLATION, UBIQUITINATION, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=15713843; DOI=10.1101/gad.320705;
RA Schmidt A., Duncan P.I., Rauh N.R., Sauer G., Fry A.M., Nigg E.A.,
RA Mayer T.U.;
RT "Xenopus polo-like kinase Plx1 regulates XErp1, a novel inhibitor of APC/C
RT activity.";
RL Genes Dev. 19:502-513(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION AT SER-33,
RP UBIQUITINATION, AND MUTAGENESIS OF 32-ASP-SER-33 AND 283-ASP-SER-284.
RX PubMed=15753281; DOI=10.1073/pnas.0501108102;
RA Tung J.J., Hansen D.V., Ban K.H., Loktev A.V., Summers M.K.,
RA Adler J.R. III, Jackson P.K.;
RT "A role for the anaphase-promoting complex inhibitor Emi2/XErp1, a homolog
RT of early mitotic inhibitor 1, in cytostatic factor arrest of Xenopus
RT eggs.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4318-4323(2005).
RN [4]
RP PHOSPHORYLATION.
RX PubMed=16040245; DOI=10.1016/j.cub.2005.07.030;
RA Liu J., Maller J.L.;
RT "Calcium elevation at fertilization coordinates phosphorylation of
RT XErp1/Emi2 by Plx1 and CaMK II to release metaphase arrest by cytostatic
RT factor.";
RL Curr. Biol. 15:1458-1468(2005).
RN [5]
RP PHOSPHORYLATION AT THR-195, AND MUTAGENESIS OF SER-194; THR-195 AND
RP THR-336.
RX PubMed=16127448; DOI=10.1038/nature04093;
RA Rauh N.R., Schmidt A., Bormann J., Nigg E.A., Mayer T.U.;
RT "Calcium triggers exit from meiosis II by targeting the APC/C inhibitor
RT XErp1 for degradation.";
RL Nature 437:1048-1052(2005).
RN [6]
RP PHOSPHORYLATION AT THR-195, AND MUTAGENESIS OF 32-ASP-SER-33.
RX PubMed=16407128; DOI=10.1073/pnas.0509549102;
RA Hansen D.V., Tung J.J., Jackson P.K.;
RT "CaMKII and polo-like kinase 1 sequentially phosphorylate the cytostatic
RT factor Emi2/XErp1 to trigger its destruction and meiotic exit.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:608-613(2006).
CC -!- FUNCTION: Required to prevent anaphase onset in cytostatic factor-
CC arrested oocytes. Inhibits the anaphase-promoting complex/cyclosome
CC (APC/C) ubiquitin ligase and prevents cyclin degradation. Probably
CC recognizes and binds to some phosphorylated proteins and promotes their
CC ubiquitination and degradation. {ECO:0000269|PubMed:15713843,
CC ECO:0000269|PubMed:15753281}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q8AXF4; Q6GQ04: cdc27.S; NbExp=3; IntAct=EBI-8609042, EBI-995003;
CC Q8AXF4; Q6IRD3: ppp2r2a.S; NbExp=2; IntAct=EBI-8609042, EBI-15659454;
CC Q8AXF4; Q5XH34: ppp2r5e.S; NbExp=2; IntAct=EBI-8609042, EBI-16014794;
CC Q8AXF4; Q9PTN1: rps6ka3.L; NbExp=3; IntAct=EBI-8609042, EBI-15630603;
CC -!- DEVELOPMENTAL STAGE: Accumulates during oocyte maturation.
CC {ECO:0000269|PubMed:15713843}.
CC -!- PTM: Phosphorylated on Thr-195 by CaMK2 in response to calcium during
CC egg activation, which promotes subsequent phosphorylation by PLK1,
CC ubiquitination and protesomal degradation.
CC {ECO:0000269|PubMed:15713843, ECO:0000269|PubMed:15753281,
CC ECO:0000269|PubMed:16040245, ECO:0000269|PubMed:16127448,
CC ECO:0000269|PubMed:16407128}.
CC -!- PTM: Ubiquitinated by FBXW1 during egg activation, which promotes
CC proteasomal degradation.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14554.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF14554.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AF176353; AAF14554.1; ALT_SEQ; mRNA.
DR EMBL; AF450296; AAN76807.1; -; mRNA.
DR EMBL; AY928267; AAX18427.1; -; mRNA.
DR RefSeq; NP_001093338.1; NM_001099868.1.
DR RefSeq; XP_018121628.1; XM_018266139.1.
DR AlphaFoldDB; Q8AXF4; -.
DR BioGRID; 674682; 7.
DR DIP; DIP-46217N; -.
DR IntAct; Q8AXF4; 10.
DR MINT; Q8AXF4; -.
DR iPTMnet; Q8AXF4; -.
DR PRIDE; Q8AXF4; -.
DR GeneID; 100101275; -.
DR KEGG; xla:100101275; -.
DR CTD; 100101275; -.
DR Xenbase; XB-GENE-951950; fbxo43.L.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 100101275; Expressed in egg cell and 7 other tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0010948; P:negative regulation of cell cycle process; IEA:UniProt.
DR GO; GO:0051784; P:negative regulation of nuclear division; IEA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044064; ZF_ZBR.
DR Pfam; PF00646; F-box; 1.
DR SMART; SM00647; IBR; 1.
DR PROSITE; PS51872; ZF_ZBR; 1.
PE 1: Evidence at protein level;
KW Meiosis; Metal-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..651
FT /note="F-box only protein 43"
FT /id="PRO_0000247236"
FT DOMAIN 424..499
FT /note="F-box"
FT ZN_FING 579..627
FT /note="ZBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT REGION 14..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 583
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 586
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 601
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 606
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 611
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 614
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 619
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT MOD_RES 33
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000305|PubMed:15753281"
FT MOD_RES 195
FT /note="Phosphothreonine; by CaMK2"
FT /evidence="ECO:0000269|PubMed:16127448,
FT ECO:0000269|PubMed:16407128"
FT MUTAGEN 32..33
FT /note="DS->AA: Prevents ubiquitination and degradation in
FT response to calcium."
FT /evidence="ECO:0000269|PubMed:15753281,
FT ECO:0000269|PubMed:16407128"
FT MUTAGEN 194
FT /note="S->A: Prevents ubiquitination and degradation in
FT response to calcium."
FT /evidence="ECO:0000269|PubMed:16127448"
FT MUTAGEN 195
FT /note="T->A: Prevents ubiquitination and degradation in
FT response to calcium."
FT /evidence="ECO:0000269|PubMed:16127448"
FT MUTAGEN 283..284
FT /note="DS->AA: No effect on ubiquitination and degradation
FT in response to calcium."
FT /evidence="ECO:0000269|PubMed:15753281"
FT MUTAGEN 336
FT /note="T->A: No effect on ubiquitination and degradation in
FT response to calcium."
FT /evidence="ECO:0000269|PubMed:16127448"
SQ SEQUENCE 651 AA; 72303 MW; 48C53C789FE6491D CRC64;
MANLLENFAA HHSMTAGAKK KADHQDTSVS QDSGYSDSLK GFSPDSHKSG NFLETVTEGY
ENSENIDPTL ILSPIKYELS WGADTRESKQ LAPLYETPRV GKKEFSLRRR LLISKATSGG
NLDFDVSVCS AESCGREKSL RRIPSHEGSL SNSFADSPRD GSYEPIATST LKTESESGTS
CKKWRLSFAQ QRSSTLDDSK SDSIPLPEVE NISPVQHSLA SSTDDSILYE ETIFGAPTTP
TCNFIVKEEF QTPISNLAAN FRFNLCTPDV GHVSDFDISV TEDSAFHSLS LDKSQDSITD
HEGSFQELIQ KPRETSKAVN NKSRLRKLDR CRRLSTLRER GSQSEVEEEG NEVPVLSSAY
KLKVARASVD EENEFSSDES RVHSLLSSDD LTGKPALRVL HEMLLRSTRK RPQQATVQDL
LGSSGCFELP EDSLSRLIGR KMGLETFDIL AELKNRNLKH ILASILDLVN AASICSMCRV
SRDWRDVVLQ DKSAHQRRKA YIKKLKTEAE QGRQLSFEDS ATRLNILSRS ALRSVQIQAR
SAFRTPTSSL TPGDNKSIHS ASKHQEYLKV AKTLFTDEAL KPCPRCQYPA KYQALKKRGT
CSRKDCGFDF CSLCLCTFHG SKECGTGSAK RIPKKEALPG SAQSKRNLKR L
