FBX5_DANRE
ID FBX5_DANRE Reviewed; 384 AA.
AC Q0V967; A1L1Z7; Q1RM68; Q6DRG8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=F-box only protein 5 {ECO:0000305};
DE AltName: Full=Early mitotic inhibitor 1 {ECO:0000303|PubMed:19704007};
DE AltName: Full=Harpy protein {ECO:0000303|PubMed:20146251};
GN Name=fbxo5 {ECO:0000312|ZFIN:ZDB-GENE-030131-4027};
GN Synonyms=hrp {ECO:0000303|PubMed:20146251};
GN ORFNames=zgc:136397, zgc:158541;
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] {ECO:0000312|EMBL:AAT68109.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15256591; DOI=10.1073/pnas.0403929101;
RA Amsterdam A., Nissen R.M., Sun Z., Swindell E.C., Farrington S.,
RA Hopkins N.;
RT "Identification of 315 genes essential for early zebrafish development.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12792-12797(2004).
RN [2] {ECO:0000312|EMBL:AAI21729.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000312|EMBL:AAI21729.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=19704007; DOI=10.1128/mcb.00558-09;
RA Rhodes J., Amsterdam A., Sanda T., Moreau L.A., McKenna K., Heinrichs S.,
RA Ganem N.J., Ho K.W., Neuberg D.S., Johnston A., Ahn Y., Kutok J.L.,
RA Hromas R., Wray J., Lee C., Murphy C., Radtke I., Downing J.R.,
RA Fleming M.D., MacConaill L.E., Amatruda J.F., Gutierrez A., Galinsky I.,
RA Stone R.M., Ross E.A., Pellman D.S., Kanki J.P., Look A.T.;
RT "Emi1 maintains genomic integrity during zebrafish embryogenesis and
RT cooperates with p53 in tumor suppression.";
RL Mol. Cell. Biol. 29:5911-5922(2009).
RN [4]
RP MUTAGENESIS OF 155-SER--LEU-384; THR-159 AND ASP-162, AND FUNCTION.
RX PubMed=20146251; DOI=10.1002/dvdy.22227;
RA Riley B.B., Sweet E.M., Heck R., Evans A., McFarland K.N., Warga R.M.,
RA Kane D.A.;
RT "Characterization of harpy/Rca1/emi1 mutants: patterning in the absence of
RT cell division.";
RL Dev. Dyn. 239:828-843(2010).
RN [5]
RP FUNCTION.
RX PubMed=23082190; DOI=10.1371/journal.pone.0047658;
RA Robu M.E., Zhang Y., Rhodes J.;
RT "Rereplication in emi1-deficient zebrafish embryos occurs through a Cdh1-
RT mediated pathway.";
RL PLoS ONE 7:E47658-E47658(2012).
CC -!- FUNCTION: During embryonic development, regulates the integrity of the
CC genome and therefore the cell cycle progression by preventing
CC rereplication through an APC-Cdh1-dependent mechanism.
CC {ECO:0000269|PubMed:19704007, ECO:0000269|PubMed:20146251,
CC ECO:0000269|PubMed:23082190}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC {ECO:0000250|UniProtKB:Q9UKT4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UKT4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UKT4}.
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DR EMBL; AY648791; AAT68109.1; -; mRNA.
DR EMBL; BC115114; AAI15115.1; -; mRNA.
DR EMBL; BC121728; AAI21729.1; -; mRNA.
DR EMBL; BC129281; AAI29282.1; -; mRNA.
DR RefSeq; NP_001003869.1; NM_001003869.1.
DR AlphaFoldDB; Q0V967; -.
DR SMR; Q0V967; -.
DR STRING; 7955.ENSDARP00000056961; -.
DR PaxDb; Q0V967; -.
DR GeneID; 445392; -.
DR KEGG; dre:445392; -.
DR CTD; 26271; -.
DR ZFIN; ZDB-GENE-030131-4027; fbxo5.
DR eggNOG; ENOG502QPWN; Eukaryota.
DR InParanoid; Q0V967; -.
DR OrthoDB; 521317at2759; -.
DR PhylomeDB; Q0V967; -.
DR Reactome; R-DRE-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-DRE-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-DRE-176417; Phosphorylation of Emi1.
DR Reactome; R-DRE-68881; Mitotic Metaphase/Anaphase Transition.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q0V967; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:ZFIN.
DR GO; GO:0051276; P:chromosome organization; IMP:ZFIN.
DR GO; GO:0030097; P:hemopoiesis; IMP:ZFIN.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:ZFIN.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:ZFIN.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IBA:GO_Central.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; IMP:ZFIN.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ZFIN.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IBA:GO_Central.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044064; ZF_ZBR.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS51872; ZF_ZBR; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Metal-binding; Mitosis; Nucleus;
KW Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..384
FT /note="F-box only protein 5"
FT /id="PRO_0000258009"
FT DOMAIN 187..234
FT /note="F-box"
FT /evidence="ECO:0000255"
FT ZN_FING 311..359
FT /note="ZBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT REGION 25..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT MUTAGEN 155..384
FT /note="Missing: In hrpti245; abnormal bumpy head
FT accompanied by a shortened body axis of the embryo. During
FT embryonic development, mutants are slightly smaller and
FT show little or no growth thereafter. Induces rereplication
FT and mitosis cessation."
FT /evidence="ECO:0000269|PubMed:20146251"
FT MUTAGEN 159
FT /note="T->A: In hrpx1; recessive allele that is lethal and
FT induces a reduction of neurons number but with an increase
FT of size. Induces rereplication and mitosis cessation."
FT /evidence="ECO:0000269|PubMed:20146251"
FT MUTAGEN 162
FT /note="D->N: In hrpx1; recesive allele that is lethal and
FT induces a reduction of neurons number but with an increase
FT of size. Induces rereplication and mitosis cessation."
FT /evidence="ECO:0000269|PubMed:20146251"
FT CONFLICT 29
FT /note="H -> R (in Ref. 2; AAI21729)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="S -> P (in Ref. 1; AAT68109)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="G -> A (in Ref. 1; AAT68109)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="S -> P (in Ref. 2; AAI15115)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="T -> N (in Ref. 1; AAT68109)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="V -> I (in Ref. 1; AAT68109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 43044 MW; 8ACEA017ECFF0E40 CRC64;
MKCPNYTEDS TVLCHMEKTE TDLGEVKGHK VSPRKTGALS LRSPAATNVS TPLESRSKGP
HNKENYQNKR HSLDMASDDE VIFSGSGLTE DSGYLSLHNS QVDVDGLDSL ERSEENCVSS
QSLDVECHSG PCLPVLNFQE EACRELQRSY KKNRSYDWTV VDKVAENFGL HNVIGGKMGR
QFVDILCKLM RKDMRHILAR ILGLLGDCDL ISCTKVSRTW RKIICQDQLA LQRWKKAEKT
RRDSGRSMGS LSRDFTLDRV VFSCMQTVSS PPAHKAVKKP PCHMGGAQNA TKSSRFQQYV
EAAQSLKQHE SLRRCSRCSS PARFDAVMQR AVCTRISCAF EFCTLCQSAF HDSTPCRNTV
RSFSSTQKTL VAGSARSKRS IRRL
