FBX11_RAT
ID FBX11_RAT Reviewed; 843 AA.
AC Q7TSL3;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=F-box only protein 11;
GN Name=Fbxo11;
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].
RA Shan Y.X., Ye G.M., Guo Z.K., Huang C.Q., Pan J., Yu L.;
RL Submitted (APR-2003) 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, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The SCF(FBXO11)
CC complex mediates ubiquitination and degradation of BCL6, thereby
CC playing a role in the germinal center B-cells terminal differentiation
CC toward memory B-cells and plasma cells. The SCF(FBXO11) complex also
CC mediates ubiquitination and degradation of DTL, an important step for
CC the regulation of TGF-beta signaling, cell migration and the timing of
CC the cell-cycle progression and exit. Binds to and neddylates
CC phosphorylated p53/TP53, inhibiting its transcriptional activity.
CC SCF(FBXO11) does not seem to direct ubiquitination of p53/TP53LOG.
CC {ECO:0000250|UniProtKB:Q86XK2}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the SCF(FBXO11) complex consisting of CUL1, RBX1,
CC SKP1 and FBXO11. Interacts with p53/TP53, BCL6 and DTL (when not
CC phosphorylated). Interacts with PRDM1. {ECO:0000250|UniProtKB:Q86XK2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY274810; AAP42075.1; -; mRNA.
DR RefSeq; NP_853662.1; NM_181631.2.
DR RefSeq; XP_017449602.1; XM_017594113.1.
DR AlphaFoldDB; Q7TSL3; -.
DR SMR; Q7TSL3; -.
DR STRING; 10116.ENSRNOP00000021998; -.
DR iPTMnet; Q7TSL3; -.
DR PhosphoSitePlus; Q7TSL3; -.
DR PaxDb; Q7TSL3; -.
DR GeneID; 301674; -.
DR KEGG; rno:301674; -.
DR CTD; 80204; -.
DR RGD; 727935; Fbxo11.
DR VEuPathDB; HostDB:ENSRNOG00000016396; -.
DR eggNOG; KOG1777; Eukaryota.
DR HOGENOM; CLU_005078_1_0_1; -.
DR InParanoid; Q7TSL3; -.
DR OMA; LGYFEAN; -.
DR OrthoDB; 355502at2759; -.
DR PhylomeDB; Q7TSL3; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q7TSL3; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000016396; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q7TSL3; RN.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.160.20.10; -; 3.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR029799; FBX11/DRE-1.
DR InterPro; IPR022441; Para_beta_helix_rpt-2.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR22990:SF20; PTHR22990:SF20; 1.
DR Pfam; PF13229; Beta_helix; 2.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00722; CASH; 3.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00710; PbH1; 19.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF51126; SSF51126; 3.
DR SUPFAM; SSF81383; SSF81383; 1.
DR TIGRFAMs; TIGR03804; para_beta_helix; 4.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..843
FT /note="F-box only protein 11"
FT /id="PRO_0000119892"
FT DOMAIN 69..115
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 311..333
FT /note="PbH1 1"
FT REPEAT 334..356
FT /note="PbH1 2"
FT REPEAT 357..379
FT /note="PbH1 3"
FT REPEAT 380..402
FT /note="PbH1 4"
FT REPEAT 403..425
FT /note="PbH1 5"
FT REPEAT 426..448
FT /note="PbH1 6"
FT REPEAT 449..471
FT /note="PbH1 7"
FT REPEAT 472..494
FT /note="PbH1 8"
FT REPEAT 495..517
FT /note="PbH1 9"
FT REPEAT 518..540
FT /note="PbH1 10"
FT REPEAT 541..563
FT /note="PbH1 11"
FT REPEAT 564..586
FT /note="PbH1 12"
FT REPEAT 587..609
FT /note="PbH1 13"
FT REPEAT 610..632
FT /note="PbH1 14"
FT REPEAT 633..655
FT /note="PbH1 15"
FT REPEAT 656..678
FT /note="PbH1 16"
FT REPEAT 679..701
FT /note="PbH1 17"
FT REPEAT 702..724
FT /note="PbH1 18"
FT REPEAT 725..746
FT /note="PbH1 19"
FT ZN_FING 749..820
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 94042 MW; 0C2498C81F96EB42 CRC64;
MVAEESGPGA QNSPYQLRRK TLLPKRTACP TKNSMEGAST STTENFGHRA KRARVSGKSQ
DLSAAPAEQY LQEKLPDEVV LKIFSYLLEQ DLCRAACVCK RFSELANDPI LWKRLYMEVF
EYTRPMMHPE PGKFYQINPE EYEHPNPWKE SFQQLYKGAH VKPGFAEHFY SNPARYKGRE
NMLYYDTIED ALGGVQEAHF DGLIFVHSGI YTDEWIYIES PITMIGAAPG KVADKVIIEN
TRDSTFVFME GSEDAYVGYM TIRFNPDDKS AQHHNAHHCL EITVNCSPII DHCIIRSTCT
VGSAVCVSGQ GACPTIKHCN ISDCENVGLY ITDHAQGIYE DNEISNNALA GIWVKNHGNP
IIRRNHIHHG RDVGVFTFDH GMGYFESCNI HRNRIAGFEV KAYANPTVVR CEIHHGQTGG
IYVHEKGRGQ FIENKIYANN FAGVWITSNS DPTIRGNSIF NGNQGGVYIF GDGRGLIEGN
DIYGNALAGI QIRTNSCPIV RHNKIHDGQH GGIYVHEKGQ GVIEENEVYS NTLAGVWVTT
GSTPVLRRNR IHSGKQVGVY FYDNGHGVLE DNDIYNHMYS GVQIRTGSNP KIRRNKIWGG
QNGGILVYNS GLGCIEDNEI FDNAMAGVWI KTDSNPTLRR NKIHDGRDGG ICIFNGGRGL
LEENDIFRNA QAGVLISTNS HPVLRKNRIF DGFAAGIEIT NHATATLEGN QIFNNRFGGL
FLASGVNVTM KDNKIMNNQD AIEKAVSRGQ CLYKISSYTS YPMHDFYRCH TCNTTDRNAI
CVNCIKKCHQ GHDVEFIRHD RFFCDCGAGT LSNPCTLAGE PTHDTDTLYD SAPPIESNTL
QHN
