INT13_DROSI
ID INT13_DROSI Reviewed; 689 AA.
AC B4QX59;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Protein asunder;
DE AltName: Full=Cell cycle regulator Mat89Bb {ECO:0000250|UniProtKB:Q9VEX5};
DE AltName: Full=Maternal transcript 89Bb {ECO:0000250|UniProtKB:Q9VEX5};
DE AltName: Full=Set apart in position or space protein;
GN Name=asun; Synonyms=Mat89Bb; ORFNames=GD19084;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1] {ECO:0000312|EMBL:EDX12713.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Plays a role as a regulator of spermatogenesis. Crucial
CC regulator of the mitotic cell cycle and development. Required for the
CC correct dynein-dynactin perinuclear localization important for nucleus-
CC centrosome coupling that occur upon meiotic progression of primary
CC spermatocytes. Crucial regulator of the mitotic cell cycle and
CC development. Plays a role in sperm motility and fertility. May have a
CC role in the PNG/PLU/GNU pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q9VEX5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9VEX5}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9VEX5}. Note=Colocalizes with dynein-dynactin
CC on the nuclear surface at the meiotic G2/prophase transition in primary
CC spermatocytes. Nuclear location is required for recruitment of dynein
CC motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9VEX5}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9VEX5}.
CC -!- SIMILARITY: Belongs to the asunder family. {ECO:0000305}.
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DR EMBL; CM000364; EDX12713.1; -; Genomic_DNA.
DR AlphaFoldDB; B4QX59; -.
DR SMR; B4QX59; -.
DR STRING; 7240.B4QX59; -.
DR HOGENOM; CLU_012654_1_0_1; -.
DR OMA; CMDEAPS; -.
DR PhylomeDB; B4QX59; -.
DR Proteomes; UP000000304; Chromosome 3r.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0032039; C:integrator complex; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051642; P:centrosome localization; IEA:EnsemblMetazoa.
DR GO; GO:0046843; P:dorsal appendage formation; IEA:EnsemblMetazoa.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051663; P:oocyte nucleus localization involved in oocyte dorsal/ventral axis specification; IEA:EnsemblMetazoa.
DR GO; GO:0060814; P:posterior mRNA localization involved in anterior/posterior axis specification; IEA:EnsemblMetazoa.
DR GO; GO:0080154; P:regulation of fertilization; ISS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0034472; P:snRNA 3'-end processing; IEA:EnsemblMetazoa.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR019355; Cell_cycle_regulator_Mat89Bb.
DR PANTHER; PTHR12955; PTHR12955; 2.
DR Pfam; PF10221; DUF2151; 2.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Developmental protein;
KW Differentiation; Meiosis; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..689
FT /note="Protein asunder"
FT /id="PRO_0000385347"
FT REGION 591..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 521..550
FT /evidence="ECO:0000255"
FT MOTIF 613..619
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000250|UniProtKB:Q9VEX5"
FT COMPBIAS 600..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 75649 MW; 18EC6442964757D5 CRC64;
MFERNQKTIF VLDHTRYFSI ASEEYISMDF LKGKPSGDGG ATGAAGNATG SGGSQFSKSL
WTCACESSIE YCRVVWDLFP GKKHVRFIVS DTAAHIVNTW SPSTQNMSHV MNAMVMVGVP
SRNVPTSSDY SVIHGLRAAI EALAEPTDEQ LAAMADLGTD ELPRIPNKGR VICITSARDN
TSMKSLEDIF NTVLVQQNTL AAPPAKKGLV IDHCHLVILN IVPLGVESLV TNRSLLKISP
LLDVEIHTVS APDISYKLTH LILNHYDLAS TTVTNIPMKE EQNANSSANY DVEILHSRRA
HSITCGPDFS LPTSIKQGAT YETVTLKWCT PRGCGSAHLQ PCLGQFLVTP VDVTSRPSSC
LINFLLNGRS VLLEMPRKTG SKATSHMLSA RGGEIFVHSL CITRSCMDEA PSITDGPGGR
VSDYRTAELG QLIKMSRMVP LKVKDPSAPP LTRRLPRYFP LTTSSSILFH LQRHISWLPH
FLHLLVKEDM DKQDEVRCQQ HIHELYKSAS RGDVLPFTHT NGARLKLSKA KDQYRLLYRE
LEQLIQLNAT TMHHKNLLES LQSLRAAYGD APLKSEPGAS LLRSFTESPL SPERLEPISS
VGASGSSNSN SLLKASKRRM SSCGQRSLLD IISSAERSQS NKRLDFSGRL CTPLGQVAKL
YPEFGTKDKD AVTTGASITP NVKEESVRS
