ID   FB31A_XENLA             Reviewed;         519 AA.
AC   A2RRT3;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=F-box only protein 31-A;
GN   Name=fbxo31-a; Synonyms=fbxo31;
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 [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC131839; AAI31840.1; -; mRNA.
DR   RefSeq; NP_001091294.1; NM_001097825.1.
DR   AlphaFoldDB; A2RRT3; -.
DR   SMR; A2RRT3; -.
DR   DNASU; 100037115; -.
DR   GeneID; 100037115; -.
DR   KEGG; xla:100037115; -.
DR   AGR; Xenbase:XB-GENE-953640; -.
DR   CTD; 100037115; -.
DR   Xenbase; XB-GENE-953640; fbxo31.S.
DR   OrthoDB; 5190824at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 100037115; Expressed in heart and 19 other cell types or tissues.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; ISS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; 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   CDD; cd22102; F-box_FBXO31; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR045048; FBXO31/39.
DR   PANTHER; PTHR10706; F-BOX FAMILY PROTEIN; 1.
DR   PANTHER; PTHR10706:SF130; F-BOX ONLY PROTEIN 31; 1.
DR   Pfam; PF12014; Cyclin_D1_bind; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF81383; F-box domain; 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..519
FT                   /note="F-box only protein 31-A"
FT                   /id="PRO_0000378164"
FT   DOMAIN          54..100
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REGION          11..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  59240 MW;  AFBDE2BF7A5FAB17 CRC64;
     MAMCARLCGV GQSGGCRRRQ QRKGAGNDPE LEDEEEEDEV RIEAGEAAVT PRRPHSLLLL
     PPEILVEIFS LLPGTELGGL AQVCSKFRQI LTTDTIWKRR CRQEYGVCEN LRKLEVTGVS
     CHDVYVKLLH QYRHILGLWQ PDIGPYGGLL NVVVDGLFII GWMYLPPHDP HVDEAMRMKP
     VFRIHLMERK DATVECMYGH KGPHNSQIQI VKKDEFSTKC LQTDYHRMSG GRQEEFRTWL
     REDLGRTLED IFHEHMQELI LMKFIYICQY DNCLTYRRIY HPPSHPEDLL NPGFFKGTYG
     SHGLEIVMLS FHGTIAKVTK ITGDPNVPAG QQTVEVDLTR PVQLPDVEHL RNFDEMSRLI
     LDVQAQIHRE QRQTDNEEDD GRGAGPDKAE PAQQPAPLLR PPNEDANGAD DDGDGGEQKP
     PNVQSFVLPA GVMARNEEYP RSCKMCFYGT GLIAGHGFSS PERTPGLFIL FDEDRFGFIW
     LELKSFSLYS RMRDRFQQSE APSLEAFEEM LQNMQSWTT
//