FBX2_BOVIN
ID FBX2_BOVIN Reviewed; 297 AA.
AC Q17QK6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=F-box only protein 2;
GN Name=FBXO2;
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].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex that mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Involved in the endoplasmic reticulum-associated degradation
CC pathway (ERAD) for misfolded lumenal proteins by recognizing and
CC binding sugar chains on unfolded glycoproteins that are
CC retrotranslocated into the cytosol and promoting their ubiquitination
CC and subsequent degradation. Prevents formation of cytosolic aggregates
CC of unfolded glycoproteins that have been retrotranslocated into the
CC cytosol. Able to recognize and bind denatured glycoproteins,
CC preferentially those of the high-mannose type (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the SCF(FBXO2) complex consisting of CUL1, RBX1,
CC SKP1 and FBXO2. Predominantly detected as heterodimer with SKP1; the
CC heterodimer with SKP1 is not part of the SCF(FBXO2) complex (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Microsome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}.
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DR EMBL; BC118302; AAI18303.1; -; mRNA.
DR RefSeq; NP_001069037.1; NM_001075569.1.
DR AlphaFoldDB; Q17QK6; -.
DR SMR; Q17QK6; -.
DR STRING; 9913.ENSBTAP00000048374; -.
DR PaxDb; Q17QK6; -.
DR PRIDE; Q17QK6; -.
DR Ensembl; ENSBTAT00000009501; ENSBTAP00000009501; ENSBTAG00000007223.
DR GeneID; 512589; -.
DR KEGG; bta:512589; -.
DR CTD; 26232; -.
DR VEuPathDB; HostDB:ENSBTAG00000007223; -.
DR VGNC; VGNC:28897; FBXO2.
DR eggNOG; ENOG502QS9C; Eukaryota.
DR GeneTree; ENSGT00940000160929; -.
DR HOGENOM; CLU_068548_0_0_1; -.
DR InParanoid; Q17QK6; -.
DR OMA; YEWCRKA; -.
DR OrthoDB; 922544at2759; -.
DR Reactome; R-BTA-8951664; Neddylation.
DR Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000007223; Expressed in retina and 89 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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; PF00646; F-box; 1.
DR Pfam; PF04300; FBA; 1.
DR SMART; SM01198; FBA; 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; Endoplasmic reticulum; Lectin; Membrane; Microsome;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..297
FT /note="F-box only protein 2"
FT /id="PRO_0000284977"
FT DOMAIN 45..92
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 114..297
FT /note="FBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00482"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 211..213
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 279..280
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT SITE 174
FT /note="Important for carbohydrate binding"
FT /evidence="ECO:0000250"
SQ SEQUENCE 297 AA; 33601 MW; 218B1BDEB6DD8DC1 CRC64;
MDGDGDPESV GQPEEASPEE QQEEACAEEA NGGEERPEDD GEGEAAYLDE LPEPLLLRVL
AELPAAQLVQ ACRLVCLRWK ELVDGAPLWL LKCQQEGLVP QDGPEDERDH WQQFYFLSKR
RRNLLRNPCG EEDLEGWCDV EHGGDGWRVE ELPGDCGVEF IHDESVKKYF ASSFEWCRKA
QIIDLQAEGY WEELLDTTQP AIVVKDWYSG RRDAGCLYEL TVKLLSEHED VLAEFNSGQV
AVPADSDDGG WTEISHTFTD YGPGVRFIRF EHGGQDCVYW KGWFGARVTN SSVWVEP
