FBX22_MOUSE
ID FBX22_MOUSE Reviewed; 402 AA.
AC Q78JE5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=F-box only protein 22;
GN Name=Fbxo22; Synonyms=Fbx22;
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Heart;
RX PubMed=22972877; DOI=10.1161/circresaha.112.271007;
RA Spaich S., Will R.D., Just S., Spaich S., Kuhn C., Frank D., Berger I.M.,
RA Wiemann S., Korn B., Koegl M., Backs J., Katus H.A., Rottbauer W., Frey N.;
RT "F-box and leucine-rich repeat protein 22 is a cardiac-enriched F-box
RT protein that regulates sarcomeric protein turnover and is essential for
RT maintenance of contractile function in vivo.";
RL Circ. Res. 111:1504-1516(2012).
CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex. Promotes the proteasome-
CC dependent degradation of key sarcomeric proteins, such as alpha-actinin
CC (ACTN2) and filamin-C (FLNC), essential for maintenance of normal
CC contractile function. {ECO:0000269|PubMed:22972877}.
CC -!- SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:22972877}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18273.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC018273; AAH18273.1; ALT_INIT; mRNA.
DR CCDS; CCDS23202.2; -.
DR RefSeq; NP_082325.2; NM_028049.2.
DR RefSeq; XP_006511522.1; XM_006511459.2.
DR AlphaFoldDB; Q78JE5; -.
DR SMR; Q78JE5; -.
DR BioGRID; 215086; 4.
DR STRING; 10090.ENSMUSP00000034859; -.
DR iPTMnet; Q78JE5; -.
DR PhosphoSitePlus; Q78JE5; -.
DR SwissPalm; Q78JE5; -.
DR EPD; Q78JE5; -.
DR jPOST; Q78JE5; -.
DR MaxQB; Q78JE5; -.
DR PaxDb; Q78JE5; -.
DR PeptideAtlas; Q78JE5; -.
DR PRIDE; Q78JE5; -.
DR ProteomicsDB; 270965; -.
DR Antibodypedia; 27397; 187 antibodies from 25 providers.
DR DNASU; 71999; -.
DR Ensembl; ENSMUST00000034859; ENSMUSP00000034859; ENSMUSG00000032309.
DR GeneID; 71999; -.
DR KEGG; mmu:71999; -.
DR UCSC; uc009psc.1; mouse.
DR CTD; 26263; -.
DR MGI; MGI:1926014; Fbxo22.
DR VEuPathDB; HostDB:ENSMUSG00000032309; -.
DR eggNOG; ENOG502QSZ2; Eukaryota.
DR GeneTree; ENSGT00390000013049; -.
DR InParanoid; Q78JE5; -.
DR OMA; GCDRIIK; -.
DR OrthoDB; 681238at2759; -.
DR PhylomeDB; Q78JE5; -.
DR TreeFam; TF328809; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 71999; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Fbxo22; mouse.
DR PRO; PR:Q78JE5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q78JE5; protein.
DR Bgee; ENSMUSG00000032309; Expressed in optic fissure and 250 other tissues.
DR ExpressionAtlas; Q78JE5; baseline and differential.
DR Genevisible; Q78JE5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0009267; P:cellular response to starvation; IDA:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR GO; GO:0010830; P:regulation of myotube differentiation; IMP:MGI.
DR GO; GO:0048742; P:regulation of skeletal muscle fiber development; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:MGI.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR019494; FIST_C.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF10442; FIST_C; 1.
DR SMART; SM01204; FIST_C; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..402
FT /note="F-box only protein 22"
FT /id="PRO_0000119907"
FT DOMAIN 18..70
FT /note="F-box"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ5"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEZ5"
SQ SEQUENCE 402 AA; 44203 MW; A13037A4733583B7 CRC64;
MEPAGGGGGV SSSTDPRSTY VLSNLAEVVE RVFTFLPAKA LLRVAGVCRL WRECVRRVLR
THRSVTWISA GVAEAGHLEG HCLVRVVAEA LENVRILPQT VLYMADSETF ISLEECRGHK
RARKRTTMET ACALEKLFPK QCQVLGIVTP GIVVTPMGSG SNRPQEIEIG ESGFALLFPQ
IEGIKIQPFH FIKDSKNLTL ERHQLTEVGL LDNPELRVVL VFGYNCCKVG ASNYLHRVVS
TFSDMNIILA GGQVDNLSSL TCEKNPLDID ATGVVGLSFS GHRIQSATVL LTEDVNDAKT
VEAAMQRLKA ANIPEQNTIG FMFACVGRGF QYYRAKGNVE ADAFRKFFPS VPLFGFFGNG
EIGCDRIVTG NFILRRCNEV KEEDLFHSYT TIMALVHLGT SK
