FBX6_RAT
ID FBX6_RAT Reviewed; 284 AA.
AC Q923V4; Q6P512;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=F-box only protein 6;
DE AltName: Full=F-box only protein 6b;
DE AltName: Full=F-box protein that recognizes sugar chains 2;
DE AltName: Full=F-box/G-domain protein 2;
GN Name=Fbxo6; Synonyms=Fbg2, Fbs2, Fbxo6b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley;
RX PubMed=12383498; DOI=10.1016/s0378-1119(02)00867-3;
RA Ilyin G.P., Serandour A.L., Pigeon C., Rialland M., Glaise D.,
RA Guguen-Guillouzo C.;
RT "A new subfamily of structurally related human F-box proteins.";
RL Gene 296:11-20(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-278 AND SER-283, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- DEVELOPMENTAL STAGE: Abundantly expressed in 14.5-day fetal liver.
CC Expression decreases during late liver development and stays at low
CC levels until birth. Expression increases 24 hours after birth and
CC reaches highest levels in adult liver. {ECO:0000269|PubMed:12383498}.
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; AF393484; AAK70899.1; -; mRNA.
DR EMBL; BC063148; AAH63148.1; -; mRNA.
DR RefSeq; NP_620272.3; NM_138917.3.
DR RefSeq; XP_006239434.1; XM_006239372.3.
DR RefSeq; XP_006239435.1; XM_006239373.3.
DR RefSeq; XP_006239436.1; XM_006239374.3.
DR RefSeq; XP_006239437.1; XM_006239375.3.
DR AlphaFoldDB; Q923V4; -.
DR SMR; Q923V4; -.
DR BioGRID; 251408; 1.
DR STRING; 10116.ENSRNOP00000012301; -.
DR iPTMnet; Q923V4; -.
DR PhosphoSitePlus; Q923V4; -.
DR PaxDb; Q923V4; -.
DR PRIDE; Q923V4; -.
DR Ensembl; ENSRNOT00000096248; ENSRNOP00000082391; ENSRNOG00000009217.
DR GeneID; 192351; -.
DR KEGG; rno:192351; -.
DR CTD; 26270; -.
DR RGD; 620418; Fbxo6.
DR eggNOG; ENOG502RZA6; Eukaryota.
DR GeneTree; ENSGT00940000159980; -.
DR HOGENOM; CLU_068548_0_0_1; -.
DR InParanoid; Q923V4; -.
DR OMA; QDTQYWA; -.
DR OrthoDB; 922544at2759; -.
DR PhylomeDB; Q923V4; -.
DR TreeFam; TF320527; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q923V4; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009217; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q923V4; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; ISO:RGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; ISO:RGD.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006516; P:glycoprotein catabolic process; ISO:RGD.
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 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA repair; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway; Unfolded protein response.
FT CHAIN 1..284
FT /note="F-box only protein 6"
FT /id="PRO_0000119884"
FT DOMAIN 1..48
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 69..250
FT /note="FBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00482"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRD1"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZN4"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 147
FT /note="K -> E (in Ref. 2; AAH63148)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 32786 MW; 75BFF3C69E676943 CRC64;
MVNINELPEN ILLELFTHVP APQLLRNCRL VCSLWRDLID VMTLWKRKSL REGFVTKDRD
EPVDDWKIFY ILCSLQRNLL RNPCAEENLR SWRIDSNGGD EWKVESLPGD HGTSFPDTKV
KKYFVTSYGM CLKSQMVDLK AEGYSEKLLD TVRPDIVVKD WFAPRADCGC TYHLRVQLAS
ADYIVLASFE PPPVTIEQWN DASWQEISHT FSNYPPGVRH ILFQHGGKDT QFWKGWYGPR
VTNSSIIVSH RTAKNPAPAR TLPEEDTSNR RKILSFGSWE DLSP
