ID   FBX32_RAT               Reviewed;         350 AA.
AC   Q91Z62;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=F-box only protein 32;
DE   AltName: Full=Atrogin-1;
DE   AltName: Full=Muscle atrophy F-box protein;
DE            Short=MAFbx;
GN   Name=Fbxo32;
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 [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=11679633; DOI=10.1126/science.1065874;
RA   Bodine S.C., Latres E., Baumhueter S., Lai V.K.-M., Nunez L., Clarke B.A.,
RA   Poueymirou W.T., Panaro F.J., Na E., Dharmarajan K., Pan Z.-Q.,
RA   Valenzuela D.M., DeChiara T.M., Stitt T.N., Yancopoulos G.D., Glass D.J.;
RT   "Identification of ubiquitin ligases required for skeletal muscle
RT   atrophy.";
RL   Science 294:1704-1708(2001).
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. Probably recognizes and binds to phosphorylated target
CC       proteins during skeletal muscle atrophy. Recognizes TERF1 (By
CC       similarity). {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(FBXO32) formed of CUL1, SKP1, RBX1 and FBXO32.
CC       {ECO:0000250|UniProtKB:Q969P5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969P5}. Nucleus
CC       {ECO:0000250|UniProtKB:Q969P5}. Note=Shuttles between cytoplasm and the
CC       nucleus. {ECO:0000250|UniProtKB:Q969P5}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in cardiac and skeletal
CC       muscle.
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DR   EMBL; AY059628; AAL16406.1; -; mRNA.
DR   RefSeq; NP_598205.1; NM_133521.1.
DR   AlphaFoldDB; Q91Z62; -.
DR   STRING; 10116.ENSRNOP00000010361; -.
DR   PaxDb; Q91Z62; -.
DR   GeneID; 171043; -.
DR   KEGG; rno:171043; -.
DR   UCSC; RGD:620373; rat.
DR   CTD; 114907; -.
DR   RGD; 620373; Fbxo32.
DR   eggNOG; KOG3926; Eukaryota.
DR   InParanoid; Q91Z62; -.
DR   OrthoDB; 623008at2759; -.
DR   Reactome; R-RNO-8951664; Neddylation.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q91Z62; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; NAS:BHF-UCL.
DR   GO; GO:0030018; C:Z disc; ISO:RGD.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:RGD.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISO:RGD.
DR   GO; GO:0014889; P:muscle atrophy; IDA:RGD.
DR   GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
DR   GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IGI:BHF-UCL.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; ISS:UniProtKB.
DR   GO; GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation; IDA:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:RGD.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR040394; FBX25/32.
DR   PANTHER; PTHR13123; PTHR13123; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..350
FT                   /note="F-box only protein 32"
FT                   /id="PRO_0000119924"
FT   DOMAIN          218..266
FT                   /note="F-box"
FT   MOTIF           57..62
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           164..168
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           275..290
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   350 AA;  40926 MW;  24AB59BC74F72472 CRC64;
     MPFLGQDWRS PGQSWVKTAD GWKRFLDEKS GTFVSDLSSY CNKENLFNSL NYDVAAKKRK
     KDIQNSKTKT QYFHQEKWIY VHKGSTKERH GYCTLGEAFN RLDFSTAILD SRRFNYVVRL
     LELIAKSQLT SLSGIAQKNF MNILEKVVLK VLEDQQNIRL IRELLQTLYT SLCTLVQRVG
     KSVLVGNINM WVYRMETTLH WQQQLNSIQI SRPAFKGLTI TDLPVCLQLN IMQRLSDGRD
     LVSLGQAAPD LHVLSEDRLL WKRLCQYHFS ERQIRKRLIL SDKGQLDWKK MYFKLVRCYP
     RREQYGVTLQ LCKHCHILSW KGTDHPCTAN NPESCSVSLS PQDFINLFKF