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FBX17_MOUSE
ID   FBX17_MOUSE             Reviewed;         286 AA.
AC   Q9QZM8;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=F-box only protein 17;
DE   AltName: Full=F-box only protein 26;
GN   Name=Fbxo17; Synonyms=Fbx17, Fbxo26;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=10531037; DOI=10.1016/s0960-9822(00)80021-4;
RA   Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.;
RT   "A family of mammalian F-box proteins.";
RL   Curr. Biol. 9:1180-1182(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   TISSUE SPECIFICITY.
RX   PubMed=18203720; DOI=10.1074/jbc.m709508200;
RA   Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.;
RT   "Diversity in tissue expression, substrate binding, and SCF complex
RT   formation for a lectin family of ubiquitin ligases.";
RL   J. Biol. Chem. 283:12717-12729(2008).
CC   -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC       protein)-type E3 ubiquitin ligase complex. Able to recognize and bind
CC       denatured glycoproteins, which are modified with complex-type
CC       oligosaccharides. Also recognizes sulfated glycans. Does not bind high-
CC       mannose glycoproteins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       Interacts with SKP1 and CUL1 (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9QZM8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QZM8-2; Sequence=VSP_012981, VSP_012982;
CC   -!- TISSUE SPECIFICITY: Expressed primarily in the brain.
CC       {ECO:0000269|PubMed:18203720}.
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DR   EMBL; AF176532; AAF09141.1; -; mRNA.
DR   EMBL; BC026470; AAH26470.1; -; mRNA.
DR   CCDS; CCDS39863.2; -. [Q9QZM8-1]
DR   CCDS; CCDS80688.1; -. [Q9QZM8-2]
DR   RefSeq; NP_001297616.1; NM_001310687.1. [Q9QZM8-2]
DR   RefSeq; NP_056611.2; NM_015796.2. [Q9QZM8-1]
DR   AlphaFoldDB; Q9QZM8; -.
DR   SMR; Q9QZM8; -.
DR   STRING; 10090.ENSMUSP00000032818; -.
DR   PaxDb; Q9QZM8; -.
DR   PRIDE; Q9QZM8; -.
DR   Antibodypedia; 68422; 54 antibodies from 17 providers.
DR   DNASU; 50760; -.
DR   Ensembl; ENSMUST00000032818; ENSMUSP00000032818; ENSMUSG00000030598. [Q9QZM8-1]
DR   Ensembl; ENSMUST00000108278; ENSMUSP00000103913; ENSMUSG00000030598. [Q9QZM8-1]
DR   Ensembl; ENSMUST00000108279; ENSMUSP00000103914; ENSMUSG00000030598. [Q9QZM8-2]
DR   Ensembl; ENSMUST00000167118; ENSMUSP00000130422; ENSMUSG00000030598. [Q9QZM8-1]
DR   GeneID; 50760; -.
DR   KEGG; mmu:50760; -.
DR   UCSC; uc009fzl.2; mouse. [Q9QZM8-2]
DR   UCSC; uc009fzn.2; mouse. [Q9QZM8-1]
DR   CTD; 115290; -.
DR   MGI; MGI:1354707; Fbxo17.
DR   VEuPathDB; HostDB:ENSMUSG00000030598; -.
DR   eggNOG; ENOG502RZA6; Eukaryota.
DR   GeneTree; ENSGT00940000162455; -.
DR   HOGENOM; CLU_068548_0_0_1; -.
DR   InParanoid; Q9QZM8; -.
DR   OMA; YAVVQRC; -.
DR   PhylomeDB; Q9QZM8; -.
DR   TreeFam; TF320527; -.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   BioGRID-ORCS; 50760; 4 hits in 73 CRISPR screens.
DR   ChiTaRS; Fbxo17; mouse.
DR   PRO; PR:Q9QZM8; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9QZM8; protein.
DR   Bgee; ENSMUSG00000030598; Expressed in humerus cartilage element and 144 other tissues.
DR   ExpressionAtlas; Q9QZM8; baseline and differential.
DR   Genevisible; Q9QZM8; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:GOC.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; 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   Alternative splicing; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..286
FT                   /note="F-box only protein 17"
FT                   /id="PRO_0000119899"
FT   DOMAIN          15..62
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   DOMAIN          107..283
FT                   /note="FBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00482"
FT   VAR_SEQ         240..242
FT                   /note="VSH -> GLP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10531037"
FT                   /id="VSP_012981"
FT   VAR_SEQ         243..286
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10531037"
FT                   /id="VSP_012982"
SQ   SEQUENCE   286 AA;  32500 MW;  F303B2414406259B CRC64;
     MGARPSRRQM TEARRLALTK LPPELLVQVL SHVPPRALVT RCRPVCRAWR DLVDGPSIWL
     LQLARDRSAE GRALYALAQR CPADADADAD ADGNRHDEFP FCALARFCLR APFGRNLIHN
     SCGEQGFRGW EVEHGGNGWA VEKNLTLVPG APSQTCFVTS FEWCSKRQLV DLVKEGVWQE
     LLDSGQIEIC IADWWGAREN CGCIYRLRVR LLDEYENEVV KFSASPNPVL QWTERSCRQV
     SHVFTNFGKG IRYVSFEQYG RDTRSWVGHY GALVTHSSVR VRIRLS
 
 
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