ID   FBX31_XENTR             Reviewed;         551 AA.
AC   Q0D2D2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=F-box only protein 31;
GN   Name=fbxo31;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of some SCF (SKP1-cullin-F-box) protein ligase
CC       complex that plays a central role in G1 arrest following DNA damage.
CC       Specifically recognizes phosphorylated cyclin-D1 (ccnd1), promoting its
CC       ubiquitination and degradation by the proteasome, resulting in G1
CC       arrest (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FBXO31 family. {ECO:0000305}.
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DR   EMBL; BC121976; AAI21977.1; -; mRNA.
DR   RefSeq; NP_001072525.1; NM_001079057.1.
DR   AlphaFoldDB; Q0D2D2; -.
DR   SMR; Q0D2D2; -.
DR   PaxDb; Q0D2D2; -.
DR   DNASU; 779980; -.
DR   Ensembl; ENSXETT00000037873; ENSXETP00000037873; ENSXETG00000017407.
DR   GeneID; 779980; -.
DR   KEGG; xtr:779980; -.
DR   CTD; 79791; -.
DR   Xenbase; XB-GENE-953635; fbxo31.
DR   eggNOG; ENOG502QR2A; Eukaryota.
DR   HOGENOM; CLU_035961_0_0_1; -.
DR   InParanoid; Q0D2D2; -.
DR   OMA; HIQIVKR; -.
DR   OrthoDB; 484321at2759; -.
DR   PhylomeDB; Q0D2D2; -.
DR   TreeFam; TF331818; -.
DR   Reactome; R-XTR-8951664; Neddylation.
DR   Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000017407; Expressed in skeletal muscle tissue and 12 other tissues.
DR   ExpressionAtlas; Q0D2D2; differential.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0030332; F:cyclin binding; IEA:InterPro.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR026941; FBXO31.
DR   InterPro; IPR045048; FBXO31/39.
DR   PANTHER; PTHR10706; PTHR10706; 1.
DR   PANTHER; PTHR10706:SF130; PTHR10706:SF130; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; DNA damage; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..551
FT                   /note="F-box only protein 31"
FT                   /id="PRO_0000378166"
FT   DOMAIN          58..104
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REGION          12..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  63238 MW;  4119A025DBC9F707 CRC64;
     MAVCARLCGV GQSGGCRRRQ QRKGAGNGPE LEDEEEEDEV RIEAEVIGGQ AAEAPRRPRS
     LLHLPPEILV EIFSSLPGTE LPSLAQVCRK FRQILTTDTI WKRRCKQEYG VCENLRKLEV
     TGVSCRDVYV KRINPRVKSG RFMKILPDYE HMEYRDIYTC LLHQYRHILG LWQPDIGPYG
     GLLNVVVDGL FIIGWMYLPP HDPHVDEAMR LKPVFRIHLM ERNDATVECM YGHKGPHNGQ
     IQIVKKDEFS TKCIQTDYHR MSGGRQEEFR TWLREDLGRT LEDIFHEHMQ ELILMKFIYI
     CQYDNCLTYR RIYHPPSRPD DLLNPGFFKG TYGSHGLEIV MLSFHGTIAK VTKITGDPNV
     PAGQQTLEVD LTRPVQLPDV EHLRNFDEMS RLILDVQAQI HREQRQTGNE EDDGRGAGPD
     KAEHSQQPAP VLRPANEDAN KVDGGDGEEQ KPPNVQSFVL PTGVMARNEE YPRSCKMCFY
     GTGLIAGHGF SSPERTPGLF ILFDEDRFGF IWLELKSFSL YSRMRDRFQQ SEAPSVEAFE
     EMLQNMQSWT T