BTBDI_MOUSE
ID BTBDI_MOUSE Reviewed; 723 AA.
AC A0A0A6YY25;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=BTB/POZ domain-containing protein 18 {ECO:0000305};
GN Name=Btbd18 {ECO:0000312|MGI:MGI:3650217};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414; SER-682 AND SER-683, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=28292424; DOI=10.1016/j.devcel.2017.02.007;
RA Zhou L., Canagarajah B., Zhao Y., Baibakov B., Tokuhiro K., Maric D.,
RA Dean J.;
RT "BTBD18 regulates a subset of piRNA-generating loci through transcription
RT elongation in mice.";
RL Dev. Cell 40:453-466(2017).
CC -!- FUNCTION: Specifically required during spermatogenesis to promote
CC expression of piRNA precursors. The piRNA metabolic process mediates
CC the repression of transposable elements during meiosis by forming
CC complexes composed of piRNAs and Piwi proteins and governs the
CC methylation and subsequent repression of transposons, which is
CC essential for the germline integrity. Acts by facilitating
CC transcription elongation at piRNA loci during pachytene.
CC {ECO:0000269|PubMed:28292424}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28292424}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:28292424}.
CC -!- DEVELOPMENTAL STAGE: Expressed during pachytene in testis: accumulates
CC in early pachytene cells (stages I-VII), declines in late pachytene
CC cells (stages VIII-X) and disappears in diplotene cells (stage XI) (at
CC protein level). Expressed from spermatogonia to spermatids, with trace
CC expression in mature spermatozoa and somatic Sertoli cells.
CC {ECO:0000269|PubMed:28292424}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable but show male sterility due to
CC defects in spermatogenesis. Retrotransposons are derepressed due to DNA
CC demethylation. Defects are caused by impaired piRNA biogenesis.
CC {ECO:0000269|PubMed:28292424}.
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DR EMBL; AL929079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS79815.1; -.
DR RefSeq; NP_001138572.1; NM_001145100.1.
DR RefSeq; XP_006498589.1; XM_006498526.2.
DR AlphaFoldDB; A0A0A6YY25; -.
DR SMR; A0A0A6YY25; -.
DR iPTMnet; A0A0A6YY25; -.
DR PhosphoSitePlus; A0A0A6YY25; -.
DR ProteomicsDB; 265256; -.
DR Antibodypedia; 62798; 13 antibodies from 8 providers.
DR Ensembl; ENSMUST00000133437; ENSMUSP00000142247; ENSMUSG00000086598.
DR GeneID; 100270744; -.
DR KEGG; mmu:100270744; -.
DR CTD; 643376; -.
DR MGI; MGI:3650217; Btbd18.
DR VEuPathDB; HostDB:ENSMUSG00000086598; -.
DR GeneTree; ENSGT00560000078563; -.
DR HOGENOM; CLU_380792_0_0_1; -.
DR OMA; QQSGVFC; -.
DR OrthoDB; 1090350at2759; -.
DR BioGRID-ORCS; 100270744; 0 hits in 56 CRISPR screens.
DR PRO; PR:A0A0A6YY25; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A0A0A6YY25; protein.
DR Bgee; ENSMUSG00000086598; Expressed in cleaving embryo and 13 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
DR GO; GO:1990511; P:piRNA biosynthetic process; IMP:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR042915; BTBD18.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR47639; PTHR47639; 1.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Differentiation; Nucleus; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Transcription; Transcription regulation.
FT CHAIN 1..723
FT /note="BTB/POZ domain-containing protein 18"
FT /id="PRO_0000441744"
FT DOMAIN 34..102
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 150..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 723 AA; 79464 MW; 8B3240BD88516926 CRC64;
MCSPASSKIL YRNPRFLRVA FLQLHHQQQS GVFCDALLQA EGEAVPAHCC ILSACSPFFT
ERLERERPVQ GRKVVLEMGG LKIQTLRKLV DFLYTSEMEV SQEEAQDVLS AARQLRVSEL
ETLQLEGGKL VKAPQGRRLN RECLQPPAAA PISARVVGPK SRPQTPLPVT QTPSPLGAVR
LKSLGEEEGA HKKTNLPNAD SLSDTQLKKK ARVCLTQESR SSPSSQREGP KETKSNPGPT
ALPSLYPSVD EQLLPRKIRL SRSKPSPHVY TSTPSSILSG PSSMPTAPGR RLWRQRTVSK
EAQGVDKQKP GEVRPLQSTP DPSDVGKPAE NKKQSPELRA PTSSSVEEGQ VGRVKLRKIV
NGTCWEVVQE PPLRNTQDSP QILEPSDVEE PSGTLLSSVN EQEIPARIQL CQDSPESPRL
QDILLSASHS PDHPMVKSEF GSSPMLTGKE SDLNIDCREP YTFDTTLLGQ PCEAEQYRIT
SAAATSELEE IFDFMLCGSD VEPPVGSLES PGAEGCRTPS YHLSETGKNW IEGEEWCLPD
MELWPRDLTG LEKEPVSENK EPVEPFSPLV MRSENTESFE PLSPLVMPSE VSREELSLRG
SWTPDLEITS SQPLDGQGEK LLHFDSSDPS QRSYNHLSPP CSDWAETGLE VSLGMDDVLC
PVPKAVREVS ANPEQLDPLP GSSEDEEIDV VDWTVEKKLG PTSVPSVWPD PSSESETEVD
ILT
