FBX7_RAT
ID FBX7_RAT Reviewed; 522 AA.
AC Q68FS3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=F-box only protein 7;
GN Name=Fbxo7;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1
CC in the clearance of damaged mitochondria via selective autophagy
CC (mitophagy) by targeting PRKN to dysfunctional depolarized
CC mitochondria. Promotes MFN1 ubiquitination (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC complex SCF(FBXO7) formed of CUL1, SKP1, RBX1 and FBXO7. Interacts via
CC its C-terminal proline-rich region with DLGAP5. Interacts with BIRC2.
CC Interacts with CDK6 and promotes its interaction with D-type cyclin.
CC Interacts (via the N-terminal Ubl domain) with PRKN. Interacts (via N-
CC terminal region) with PINK1. Interacts with PSMF1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Mitochondrion {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
CC Note=Predominantly cytoplasmic. A minor proportion is detected in the
CC nucleus. Relocates from the cytosol to depolarized mitochondria (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The ubiquitin-like region mediates interaction with PRKN.
CC {ECO:0000250}.
CC -!- DOMAIN: The proline-rich region is important for protein-protein
CC interactions. {ECO:0000250}.
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DR EMBL; BC079382; AAH79382.1; -; mRNA.
DR RefSeq; NP_001012222.1; NM_001012222.1.
DR AlphaFoldDB; Q68FS3; -.
DR SMR; Q68FS3; -.
DR STRING; 10116.ENSRNOP00000006366; -.
DR iPTMnet; Q68FS3; -.
DR PhosphoSitePlus; Q68FS3; -.
DR jPOST; Q68FS3; -.
DR PaxDb; Q68FS3; -.
DR PRIDE; Q68FS3; -.
DR Ensembl; ENSRNOT00000006366; ENSRNOP00000006366; ENSRNOG00000004637.
DR GeneID; 366854; -.
DR KEGG; rno:366854; -.
DR UCSC; RGD:1305648; rat.
DR CTD; 25793; -.
DR RGD; 1305648; Fbxo7.
DR eggNOG; ENOG502QTNJ; Eukaryota.
DR GeneTree; ENSGT00390000006670; -.
DR InParanoid; Q68FS3; -.
DR OMA; ICLVLED; -.
DR OrthoDB; 999024at2759; -.
DR PhylomeDB; Q68FS3; -.
DR TreeFam; TF329830; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q68FS3; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004637; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q68FS3; baseline and differential.
DR Genevisible; Q68FS3; RN.
DR GO; GO:0097414; C:classical Lewy body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097409; C:glial cytoplasmic inclusion; ISO:RGD.
DR GO; GO:1990037; C:Lewy body core; ISO:RGD.
DR GO; GO:1990038; C:Lewy body corona; ISO:RGD.
DR GO; GO:0097462; C:Lewy neurite; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISS:UniProtKB.
DR GO; GO:0030098; P:lymphocyte differentiation; IEA:Ensembl.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; ISO:RGD.
DR GO; GO:0045620; P:negative regulation of lymphocyte differentiation; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; ISO:RGD.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0040012; P:regulation of locomotion; ISO:RGD.
DR GO; GO:0010975; P:regulation of neuron projection development; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR021625; PI31_Prot_N.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF11566; PI31_Prot_N; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methylation; Mitochondrion; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..522
FT /note="F-box only protein 7"
FT /id="PRO_0000307723"
FT DOMAIN 329..375
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 1..88
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000250"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..129
FT /note="Important for interaction with PINK1"
FT /evidence="ECO:0000250"
FT REGION 129..169
FT /note="Important for interaction with CDK6"
FT /evidence="ECO:0000250"
FT REGION 180..324
FT /note="Important for dimerization and interaction with
FT PSMF1"
FT /evidence="ECO:0000250"
FT REGION 381..522
FT /note="Important for interaction with CDK6"
FT /evidence="ECO:0000250"
FT REGION 459..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 481..484
FT /note="RFDP motif"
FT COMPBIAS 86..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 431
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3U7U3"
FT MOD_RES 451
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3U7U3"
FT MOD_RES 518
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3U7U3"
SQ SEQUENCE 522 AA; 57561 MW; 1A1E5C131425CD7B CRC64;
MKLRVRLQKR TQPLEVPESE PTLGQLRAHL IQDLLPTLGF SSDTRFAITL NNKDALTGDE
ETLASYGIVS GDLICLVLED EMPAPNLPSS TDSEHSSLQN NDQPPLAATS SQANIPDEQG
SDSSHGQVTQ YDAWTDDSME GPSHSAEAVS IQDAMSVEEA SGFHPLEPML CSETEDGQVP
HSLEALYQSA GCSTVSDALI VLVHLLMLES GYIPQGTEAK AASMPEKWKS SGVYKLQYTH
PLCEGGSAVL TCVPLGKLIM INATIKVNGG IKNVKSVQLK PGAYVRRAEP GESAAKVYKD
LKKLSRLFKD QLVYPLLAFT RQVLNLPDVF GLVVLPLELK LRIFRLLDVH SVLALSAVCH
DLLIASNDPL LWRCLYLRDF RDSTIRGPDT DWKELYRKKH IQRKEAQRMR HVMYLPSVHP
IPFCPIPVYP RPYLPTTLLP PGIIGGEYDE RPILPSVGDP VTSLIPRPGE PPSQFRPVRP
RFDPVGPLPG SNSLLPGRAS PNNRFPFRPG RGRSADNRLP YL
