ID   INT13_DROER             Reviewed;         689 AA.
AC   B3P100;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=GG16989;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1] {ECO:0000312|EMBL:EDV49119.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV49119.1};
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; CH954181; EDV49119.1; -; Genomic_DNA.
DR   RefSeq; XP_001980161.1; XM_001980125.2.
DR   AlphaFoldDB; B3P100; -.
DR   SMR; B3P100; -.
DR   STRING; 7220.FBpp0135535; -.
DR   EnsemblMetazoa; FBtr0137043; FBpp0135535; FBgn0109217.
DR   GeneID; 6553317; -.
DR   KEGG; der:6553317; -.
DR   eggNOG; KOG3711; Eukaryota.
DR   HOGENOM; CLU_012654_1_0_1; -.
DR   OMA; CMDEAPS; -.
DR   OrthoDB; 676663at2759; -.
DR   PhylomeDB; B3P100; -.
DR   Proteomes; UP000008711; Unassembled WGS sequence.
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   Spermatogenesis.
FT   CHAIN           1..689
FT                   /note="Protein asunder"
FT                   /id="PRO_0000385340"
FT   REGION          578..619
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        581..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  75637 MW;  2F1E6C5A9AD0B5D7 CRC64;
     MFERNQKTIF VLDHTRYFSI ASEEYISMDF LKGKPSADGG ATGAAGNATG GGGSQFSKSL
     WTCACESSIE YCRVVWDLFP GKKHVRFIVS DTAAHIVNTW SHSTQNMSHV MNAMVMVGVP
     SRNVATSSDY SVIHGLRAAI EALAEPTDEQ LAAMADLGTD ELPRIPNKGR VICITSARDN
     TSMKSLEDIF NTVLVQQNAL AAPPAKKGLV IDHCHLVILN IVPLGVESLV TNRSLLKISP
     LLDVEIHTVS APDISYKLTH LILNHYDLAS TTVTNIPMKE EQNANSSANY DVEILHSRRA
     HSITCGPDFS LPTSIKQGAT YETVTLKWCT PRGCGSADLQ PCLGQFLVTP VDVTSRPSSC
     LINFLLNGRS VLLEMPRKTG SKATSHMLSA RGGEIFVHSL CITRSCMDEA PSITDGPGGR
     VSDYRTAELG QLIKMSRMVP LKVKDPSAPP LARRLPRYFP LTTSSSILFH LQRHINWLPH
     FLHILVKEDM DKQDEVRCQQ HIHELYKSAS RGDVLPFTHT NGARLKLSKA KDQYRLLYRE
     LEQLIQLNAT TMHHKNLLES LQSLRAAYGD APLKSEPGAS LLRSYTESPL SPERLEPITS
     GSASGSSNSN SLLKASKRRM SSCGQRSLLD IISSAERSQS NKRLDFSGRL CTPLGQVAKL
     YPDFGNKDKD SVVTAASITP NVKEESVRS