ID   FBX6_BOVIN              Reviewed;         265 AA.
AC   Q3SX24;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=F-box only protein 6;
DE   AltName: Full=F-box protein that recognizes sugar chains 2;
GN   Name=FBXO6; Synonyms=FBS2, FBX6;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1-F-box
CC       protein)-type E3 ubiquitin ligase complexes. Involved in endoplasmic
CC       reticulum-associated degradation pathway (ERAD) for misfolded lumenal
CC       proteins by recognizing and binding sugar chains on unfolded
CC       glycoproteins that are retrotranslocated into the cytosol and promoting
CC       their ubiquitination and subsequent degradation. Able to recognize and
CC       bind denatured glycoproteins, which are modified with not only high-
CC       mannose but also complex-type oligosaccharides. Also recognizes
CC       sulfated glycans. Also involved in DNA damage response by specifically
CC       recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting
CC       its ubiquitination and degradation. Ubiquitination of CHEK1 is required
CC       to insure that activated CHEK1 does not accumulate as cells progress
CC       through S phase, or when replication forks encounter transient
CC       impediments during normal DNA replication (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       Interacts with VCP, CHEK1 and CUL1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; BT030507; ABQ12947.1; -; mRNA.
DR   EMBL; BC104546; AAI04547.1; -; mRNA.
DR   RefSeq; NP_001029605.1; NM_001034433.1.
DR   RefSeq; XP_005217017.1; XM_005216960.3.
DR   RefSeq; XP_005217020.1; XM_005216963.3.
DR   RefSeq; XP_005217021.1; XM_005216964.2.
DR   RefSeq; XP_010811560.1; XM_010813258.2.
DR   RefSeq; XP_015330583.1; XM_015475097.1.
DR   AlphaFoldDB; Q3SX24; -.
DR   SMR; Q3SX24; -.
DR   STRING; 9913.ENSBTAP00000034071; -.
DR   PaxDb; Q3SX24; -.
DR   PRIDE; Q3SX24; -.
DR   Ensembl; ENSBTAT00000034170; ENSBTAP00000034071; ENSBTAG00000014777.
DR   GeneID; 513023; -.
DR   KEGG; bta:513023; -.
DR   CTD; 26270; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014777; -.
DR   VGNC; VGNC:28918; FBXO6.
DR   eggNOG; ENOG502RZA6; Eukaryota.
DR   GeneTree; ENSGT00940000159980; -.
DR   HOGENOM; CLU_068548_0_0_1; -.
DR   InParanoid; Q3SX24; -.
DR   OMA; QDTQYWA; -.
DR   OrthoDB; 922544at2759; -.
DR   TreeFam; TF320527; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000014777; Expressed in urethra and 105 other tissues.
DR   ExpressionAtlas; Q3SX24; baseline.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IBA:GO_Central.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR   InterPro; IPR007397; F-box-assoc_dom.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR039752; F-box_only.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   PANTHER; PTHR12125; PTHR12125; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF04300; FBA; 1.
DR   SMART; SM01198; FBA; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS51114; FBA; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; DNA damage; DNA repair; Phosphoprotein; Reference proteome;
KW   Ubl conjugation pathway; Unfolded protein response.
FT   CHAIN           1..265
FT                   /note="F-box only protein 6"
FT                   /id="PRO_0000385626"
FT   DOMAIN          3..50
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   DOMAIN          71..252
FT                   /note="FBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00482"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRD1"
SQ   SEQUENCE   265 AA;  30767 MW;  49506F70B568E5F5 CRC64;
     MALVSINQLP ENILLEVFMH VPARQLLRNC RPVCCLWRDL IDLVSLWKRK CLREGYVTED
     WDQPVSDWKV FYFLCSLRRN LLRNPCAEED MKSWKIDSNG GDQWKVESLP GAHGTGFPDS
     KVKKYFVTSY DMCLKSQIID LKAEGYWEEL LDKFRPDIVV KDWFAPRADC GCTYQIRVQL
     ASADYLVLAS FEPPPVTIHQ WNDAKWTEVS HTFSDYPPGV RHIFFQHGGK DTQFWAGWYG
     PRVTNSSVVI SHRVTRNPPH AMAQP