FBX5_XENTR
ID FBX5_XENTR Reviewed; 391 AA.
AC Q28GK6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=F-box only protein 5 {ECO:0000305};
GN Name=fbxo5 {ECO:0000312|EMBL:CAJ81361.1}; ORFNames=TEgg046m03.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:CAJ81361.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates progression through early mitosis by inhibiting the
CC anaphase promoting complex/cyclosome (APC). Binds to the APC activators
CC cdc20 to prevent APC activation. Can also bind directly to the APC to
CC inhibit substrate-binding. Required to arrest unfertilized eggs at
CC metaphase of meiosis II, by preventing their release from metaphase of
CC meiosis II, through inhibition of APC-dependent cyclin B destruction
CC leading to stabilization of cyclin B-cdk1 complex activity.
CC {ECO:0000250|UniProtKB:Q90Z80}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By
CC similarity). Interacts with btrc. Interacts with skp1. Interacts with
CC cdc20. Interacts with pin1; stabilizes fbxo5 by preventing its
CC association with btrc in an isomerization-dependent pathway; this
CC interaction is present during G2 phase and prevents fbxo5 degradation.
CC Interacts with plk1 (By similarity). {ECO:0000250|UniProtKB:Q90Z80,
CC ECO:0000250|UniProtKB:Q9UKT4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q90Z80}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q90Z80}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q90Z80}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q90Z80}. Note=In
CC interphase, localizes in a punctate manner in the nucleus and cytoplasm
CC with some perinuclear concentration. In mitotic cells, localizes
CC throughout the cell, particularly at the spindle. At metaphase,
CC localized at mitotic centrosomes. Decreases centrosome localization as
CC cells progressed through telophase. {ECO:0000250|UniProtKB:Q90Z80}.
CC -!- DOMAIN: The C-terminal region is required for APC inhibition.
CC {ECO:0000250|UniProtKB:Q90Z80}.
CC -!- PTM: Proteolysed; proteolysis is induced by both cyclin B-cdk1 and
CC cyclin A-cdk1/2 complex through probable phosphorylation. Proteolysis
CC is inhibited by pin1 during G2. {ECO:0000250|UniProtKB:Q90Z80}.
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DR EMBL; CR761353; CAJ81361.1; -; mRNA.
DR RefSeq; NP_001037934.1; NM_001044469.1.
DR AlphaFoldDB; Q28GK6; -.
DR SMR; Q28GK6; -.
DR PaxDb; Q28GK6; -.
DR GeneID; 733555; -.
DR KEGG; xtr:733555; -.
DR CTD; 26271; -.
DR Xenbase; XB-GENE-953946; fbxo5.
DR eggNOG; ENOG502QPWN; Eukaryota.
DR InParanoid; Q28GK6; -.
DR OrthoDB; 521317at2759; -.
DR Reactome; R-XTR-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-XTR-176417; Phosphorylation of Emi1.
DR Reactome; R-XTR-68881; Mitotic Metaphase/Anaphase Transition.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0106061; P:negative regulation of exit from meiosis; ISS:UniProtKB.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IBA:GO_Central.
DR GO; GO:0045841; P:negative regulation of mitotic metaphase/anaphase transition; ISS:UniProtKB.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; 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; IPR044064; ZF_ZBR.
DR Pfam; PF00646; F-box; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS51872; ZF_ZBR; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Metal-binding; Mitosis;
KW Nucleus; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..391
FT /note="F-box only protein 5"
FT /id="PRO_0000258012"
FT DOMAIN 198..245
FT /note="F-box"
FT /evidence="ECO:0000255"
FT ZN_FING 318..366
FT /note="ZBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT REGION 365..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
SQ SEQUENCE 391 AA; 44000 MW; 187D02D2B330A437 CRC64;
MMCGFTSNQS PKKLSSKKLS ATNVHLEISP VKCDSPCKGY ENVQASYLDT ANCTTVTRGA
DIKDDLPLHN KENLLHRFGD LETHSDEEYS GLQDSGYSSI LQNDSPCQDE TDNNVSDIQL
RETPKNFVQF QKPLHTLSTK NLPALRFEEA MCSTLKKMRK TSKKIDWNAV DDVVCGGNYG
LENLIGKNMG LERFDILAEL FHRDFKHLLT KILRHLSAMD LINVISVSTT WRKILQKDNS
AYNSYKLGCK ELCEKKAKVS AHTATRDESL CRVPLASVQK VAASSLCTSK KQSKNRGLSN
NRHAEFIEVA QTLKNDQCLK VCVDCSSPAK YDPYLHRATC TRESCKFDFC TLCSCKYHGS
KCCQTSKPRS YRVPSEPLPG SKKSKQNLRR L
