FBX5B_XENLA
ID FBX5B_XENLA Reviewed; 384 AA.
AC Q4V7W2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=F-box only protein 5-B {ECO:0000305};
DE AltName: Full=Early mitotic inhibitor 1-B;
GN Name=fbxo5-b; Synonyms=emi1-b;
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] {ECO:0000312|EMBL:AAH97694.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte {ECO:0000312|EMBL:AAH97694.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) 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; BC097694; AAH97694.1; -; mRNA.
DR RefSeq; NP_001089481.1; NM_001096012.1.
DR AlphaFoldDB; Q4V7W2; -.
DR PRIDE; Q4V7W2; -.
DR DNASU; 734532; -.
DR GeneID; 734532; -.
DR KEGG; xla:734532; -.
DR CTD; 734532; -.
DR Xenbase; XB-GENE-6255898; fbxo5.L.
DR OMA; MRASCAF; -.
DR OrthoDB; 521317at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 734532; Expressed in gastrula and 15 other tissues.
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: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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
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..384
FT /note="F-box only protein 5-B"
FT /id="PRO_0000258011"
FT DOMAIN 191..238
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 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..106
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"
SQ SEQUENCE 384 AA; 43171 MW; DB75043D8244E30B CRC64;
MMCGFTSNPS PKKLLSKSSA TNVHLEISPV KPDRPCKGYE NVLGSCTTVA KCADLTDDLP
VHNKENLLHG FNDLERHHDE ENSSLQDSGY SSILQNDSPC QDETDSNVSD IQVRDTPKNL
MQYQKPFHTL STRCLPILRF EAAMCSTLKK MRKTSKKIDW NAVDDVVCGG NYGLEHLIGK
SMGLERVDIL AELFHRDFKH LLTKILRHLN AMDLINVIGV STTWRKILQK DNWAYNTYKL
GCKELCEKRA KVSTHTATRD ESLCRVPLAS VQKVAASSLC TSKKQNKNGG LSNNRHAEFI
EVAQTLKNDQ SLKACVDCGS PAKYDSYLHR AICTRESCKL DFCTLCSCKY HSSKSCLISK
PRSYRIPIEP LPGSKKSKQN LRRL
