KBTB8_RAT
ID KBTB8_RAT Reviewed; 575 AA.
AC B1H285;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Kelch repeat and BTB domain-containing protein 8 {ECO:0000250|UniProtKB:Q8NFY9};
GN Name=Kbtbd8 {ECO:0000312|EMBL:AAI60902.1, ECO:0000312|RGD:1563166};
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] {ECO:0000312|EMBL:EDL91413.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAI60902.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:AAI60902.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAI60902.1};
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-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin ligase complex that acts as a regulator of neural crest
CC specification. The BCR(KBTBD8) complex acts by mediating
CC monoubiquitination of NOLC1 and TCOF1: monoubiquitination promotes the
CC formation of a NOLC1-TCOF1 complex that acts as a platform to connect
CC RNA polymerase I with enzymes responsible for ribosomal processing and
CC modification, leading to remodel the translational program of
CC differentiating cells in favor of neural crest specification.
CC {ECO:0000250|UniProtKB:Q8NFY9}.
CC -!- SUBUNIT: Component of the BCR(KBTBD8) E3 ubiquitin ligase complex, at
CC least composed of CUL3, KBTBD8 and RBX1.
CC {ECO:0000250|UniProtKB:Q8NFY9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q8NFY9}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q8NFY9}. Note=Translocates to the spindle
CC apparatus during mitosis. {ECO:0000250|UniProtKB:Q8NFY9}.
CC -!- SIMILARITY: Belongs to the KBTBD8 family. {ECO:0000305}.
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DR EMBL; CH473957; EDL91413.1; -; Genomic_DNA.
DR EMBL; BC160902; AAI60902.1; -; mRNA.
DR RefSeq; NP_001102720.2; NM_001109250.3.
DR RefSeq; XP_006236994.1; XM_006236932.2.
DR AlphaFoldDB; B1H285; -.
DR SMR; B1H285; -.
DR BioGRID; 271570; 1.
DR STRING; 10116.ENSRNOP00000017889; -.
DR PaxDb; B1H285; -.
DR PRIDE; B1H285; -.
DR GeneID; 500262; -.
DR KEGG; rno:500262; -.
DR UCSC; RGD:1563166; rat.
DR CTD; 84541; -.
DR RGD; 1563166; Kbtbd8.
DR eggNOG; KOG4441; Eukaryota.
DR InParanoid; B1H285; -.
DR OrthoDB; 398028at2759; -.
DR PhylomeDB; B1H285; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:B1H285; -.
DR Proteomes; UP000002494; Unplaced.
DR Proteomes; UP000234681; Chromosome 4.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0014032; P:neural crest cell development; ISS:UniProtKB.
DR GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR028764; KBTBD8.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412:SF433; PTHR24412:SF433; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 3.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 3.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Golgi apparatus; Kelch repeat; Reference proteome;
KW Repeat; Translation regulation; Ubl conjugation pathway.
FT CHAIN 1..575
FT /note="Kelch repeat and BTB domain-containing protein 8"
FT /id="PRO_0000393570"
FT DOMAIN 23..91
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 126..228
FT /note="BACK"
FT /evidence="ECO:0000255"
FT REPEAT 310..364
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 365..415
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 417..455
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 457..506
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT REPEAT 516..562
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
SQ SEQUENCE 575 AA; 66322 MW; FD0F72C893554CC2 CRC64;
MDPFHACSIL KQLKTMYDEG QLTDIVVEVD HGKTFSCHRN VLAAISPYFR SMFTSGLTES
TQKEVRIIGV EAESMGLVLN YAYTSRVILT EANVQALFTT ASIFQIPSIQ DQCAKYMISH
LDPQNSIGVF IFADHYGHQE LGDRSKEYIR KKFLCVTKEQ EFLQLTKDQL ISILDSDDLN
VDREEHVYES IIRWFEHEQN EREVHLPEIF AKCIRFPLME DAFIEKIPPR FAQAIVKSCG
EKGPSNTNGC TQRLGMTASE MIICFDAAHK HSGKKQTVPC LDIVTGRVFK LCKPPNDLRE
VGILVSPDND IYIAGGYRPS SSEVSIDHKA ENDFWMYDHS TNRWLSKPSL LRARIGCKLV
YCCGKMYAIG GRVYEGDGRN SLKSVECYDS RENCWMTVCA MPVAMEFHNA VEHKEKIYVL
QGEFFLFYEP QKDYWGFLTP MTVPRIQGLA AVYKDSIYYI AGTCGNHQRV FTVEAYDIEL
NKWTRKKDFP CDQSINPYLK LVLFQNKLHL FVRATQVTVE EHIFRTSRKN SLYQYDDIAD
QWMKVYETPD RLWDLGRHFE CAVAKLYPQC LQKVL
