FBX7_BOVIN
ID FBX7_BOVIN Reviewed; 522 AA.
AC Q2T9S7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=F-box only protein 7;
GN Name=FBXO7;
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) 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 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; BC111286; AAI11287.1; -; mRNA.
DR RefSeq; NP_001033148.1; NM_001038059.1.
DR AlphaFoldDB; Q2T9S7; -.
DR SMR; Q2T9S7; -.
DR STRING; 9913.ENSBTAP00000027498; -.
DR PaxDb; Q2T9S7; -.
DR GeneID; 508235; -.
DR KEGG; bta:508235; -.
DR CTD; 25793; -.
DR eggNOG; ENOG502QTNJ; Eukaryota.
DR InParanoid; Q2T9S7; -.
DR OrthoDB; 999024at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISS:UniProtKB.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IBA:GO_Central.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
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_0000284973"
FT DOMAIN 328..374
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 1..87
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000250"
FT REGION 88..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..128
FT /note="Important for interaction with PINK1"
FT /evidence="ECO:0000250"
FT REGION 128..168
FT /note="Important for interaction with CDK6"
FT /evidence="ECO:0000250"
FT REGION 179..323
FT /note="Important for dimerization and interaction with
FT PSMF1"
FT /evidence="ECO:0000250"
FT REGION 380..522
FT /note="Important for interaction with CDK6"
FT /evidence="ECO:0000250"
FT REGION 484..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 481..484
FT /note="RFDP motif"
FT COMPBIAS 88..137
FT /note="Polar 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; 57965 MW; C35C26343DCAB1FA CRC64;
MKLRVRLQKR TWPLDMPEVE PTLGQLRAYL SQALPTWGYS SDARFAITLN NKDALTGDEE
TLASYGIVSG DLLCLILEDA IAAPNLPSST VSEHSSVQNN DQPSLATSSS QSNIQDAQLH
DSLQGQATQS EVWNDDSVSG PGQHFEAEAV PDVVDVEEGT GYYLAEPMLC SESVEGQVPH
SLEILYQSAD CLNPCDALIV SIHLLMLESG YIPQGTEAKA VSMPQNWRLG GVYKLQYTHP
LCEGGSAALT CVPLGNLIVI NATLKINSEV RSVKRLQLLP ESFICKEESG ENVAMIYKDL
QKLSRLFKDQ LVYPLLAFTR QALNLPDVFG LVVLPLELKL RIFRLLDVRS VLSLSAVCRD
LCITSNDQLL WRCLYLRDFR DGSIRGRDTD WKELYKKRYK QRKEAQRGRH VMFLPSSPHP
IPFYPSPLHP RPFPPSSLHP PGIIGGEYDQ RLTLPYVGDP INSLIPGPGE TPSQFPPLRP
RFDPVGPLPG PNPILPGRGG PSDRFPLRPS RGWPTDSRLP FM
