DPY26_CAEEL
ID DPY26_CAEEL Reviewed; 1263 AA.
AC G5EGE9;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Condensin complex subunit dpy-26 {ECO:0000305};
GN Name=dpy-26 {ECO:0000312|WormBase:C25G4.5};
GN ORFNames=C25G4.5 {ECO:0000312|WormBase:C25G4.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAC47411.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC47411.1};
RX PubMed=8939869; DOI=10.1126/science.274.5293.1732;
RA Lieb J.D., Capowski E.E., Meneely P., Meyer B.J.;
RT "DPY-26, a link between dosage compensation and meiotic chromosome
RT segregation in the nematode.";
RL Science 274:1732-1736(1996).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH MIX-1.
RX PubMed=9458050; DOI=10.1016/s0092-8674(00)80920-4;
RA Lieb J.D., Albrecht M.R., Chuang P.-T., Meyer B.J.;
RT "MIX-1: an essential component of the C. elegans mitotic machinery executes
RT X chromosome dosage compensation.";
RL Cell 92:265-277(1998).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=2917714; DOI=10.1093/genetics/121.1.57;
RA Plenefisch J.D., DeLong L., Meyer B.J.;
RT "Genes that implement the hermaphrodite mode of dosage compensation in
RT Caenorhabditis elegans.";
RL Genetics 121:57-76(1989).
RN [5]
RP FUNCTION, INTERACTION WITH DPY-27, AND DISRUPTION PHENOTYPE.
RX PubMed=8939870; DOI=10.1126/science.274.5293.1736;
RA Chuang P.-T., Lieb J.D., Meyer B.J.;
RT "Sex-specific assembly of a dosage compensation complex on the nematode X
RT chromosome.";
RL Science 274:1736-1739(1996).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11937488; DOI=10.1101/gad.972702;
RA Chu D.S., Dawes H.E., Lieb J.D., Chan R.C., Kuo A.F., Meyer B.J.;
RT "A molecular link between gene-specific and chromosome-wide transcriptional
RT repression.";
RL Genes Dev. 16:796-805(2002).
RN [7]
RP INTERACTION WITH DPY-28 AND MIX-1.
RX PubMed=15557118; DOI=10.1083/jcb.200408061;
RA Chan R.C., Severson A.F., Meyer B.J.;
RT "Condensin restructures chromosomes in preparation for meiotic divisions.";
RL J. Cell Biol. 167:613-625(2004).
RN [8]
RP FUNCTION, INTERACTION WITH DPY-27; DPY;28 AND MIX-1, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=18198337; DOI=10.1101/gad.1618508;
RA Tsai C.J., Mets D.G., Albrecht M.R., Nix P., Chan A., Meyer B.J.;
RT "Meiotic crossover number and distribution are regulated by a dosage
RT compensation protein that resembles a condensin subunit.";
RL Genes Dev. 22:194-211(2008).
RN [9]
RP FUNCTION, IDENTIFICATION IN A CONDENSIN I COMPLEX AND IN A DOSAGE
RP COMPENSATION COMPLEX, AND INTERACTION WITH SMC-4; DPY-27; DPY-28; MIX-1 AND
RP CAPG-1.
RX PubMed=19781752; DOI=10.1016/j.cell.2009.07.035;
RA Mets D.G., Meyer B.J.;
RT "Condensins regulate meiotic DNA break distribution, thus crossover
RT frequency, by controlling chromosome structure.";
RL Cell 139:73-86(2009).
RN [10]
RP FUNCTION, IDENTIFICATION IN A CONDENSIN I COMPLEX AND IN A DOSAGE
RP COMPENSATION COMPLEX, INTERACTION WITH DPY-27; SMC-4; CAPG-1; MIX-1 AND
RP DPY-28, AND DISRUPTION PHENOTYPE.
RX PubMed=19119011; DOI=10.1016/j.cub.2008.12.006;
RA Csankovszki G., Collette K., Spahl K., Carey J., Snyder M., Petty E.,
RA Patel U., Tabuchi T., Liu H., McLeod I., Thompson J., Sarkeshik A.,
RA Sarkesik A., Yates J., Meyer B.J., Hagstrom K.;
RT "Three distinct condensin complexes control C. elegans chromosome
RT dynamics.";
RL Curr. Biol. 19:9-19(2009).
RN [11]
RP FUNCTION.
RX PubMed=23684975; DOI=10.1016/j.cub.2013.04.028;
RA Bembenek J.N., Verbrugghe K.J., Khanikar J., Csankovszki G., Chan R.C.;
RT "Condensin and the spindle midzone prevent cytokinesis failure induced by
RT chromatin bridges in C. elegans embryos.";
RL Curr. Biol. 23:937-946(2013).
RN [12]
RP INTERACTION WITH SMCL-1; MIX-1; SMC-4; DPY-27; DPY-28 AND CAPG-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28301465; DOI=10.1371/journal.pgen.1006614;
RA Chao L.F., Singh M., Thompson J., Yates J.R. III, Hagstrom K.A.;
RT "An SMC-like protein binds and regulates Caenorhabditis elegans
RT condensins.";
RL PLoS Genet. 13:E1006614-E1006614(2017).
CC -!- FUNCTION: Required for both chromosome condensation and segregation and
CC for X-chromosome dosage compensation depending on its binding partners
CC (PubMed:8939869, PubMed:8939870, PubMed:19119011, PubMed:2917714,
CC PubMed:19781752). Member of the condensin I complex, a complex required
CC for conversion of interphase chromatin into mitotic-like condense
CC chromosomes and for proper chromosome segregation in mitosis and
CC meiosis (PubMed:19119011, PubMed:19781752). As a member of the
CC condensin I complex, further controls the crossover number and
CC distribution in meiosis by restricting double strand break formation,
CC probably by influencing higher-order chromosome structure
CC (PubMed:19781752, PubMed:18198337). Plays a role in robust cytokinesis
CC upon presence of chromatin obstructions (PubMed:23684975). Also a
CC member of the condensin I-like dosage compensation complex that
CC associates specifically with hermaphrodite X chromosomes to reduce
CC their gene transcription during interphase, possibly through chromatin
CC reorganization (PubMed:19119011, PubMed:8939870, PubMed:2917714,
CC PubMed:19781752). As a member of the dosage compensation complex, also
CC binds to regulatory regions of the autosomal her-1 gene, required for
CC male development, possibly contributing to its repression in
CC hermaphrodites (PubMed:11937488). {ECO:0000269|PubMed:11937488,
CC ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:19119011,
CC ECO:0000269|PubMed:19781752, ECO:0000269|PubMed:23684975,
CC ECO:0000269|PubMed:2917714, ECO:0000269|PubMed:8939869,
CC ECO:0000269|PubMed:8939870}.
CC -!- SUBUNIT: Component of the condensin I complex, which contains the mix-
CC 1/SMC2 and smc-4/SMC4 heterodimer, and three non SMC subunits that
CC probably regulate the complex: dpy-26, capg-1 and dpy-28
CC (PubMed:19119011, PubMed:19781752). Within the complex, interacts with
CC dpy-28, mix-1, smc-4 and capg-1 (PubMed:15557118, PubMed:18198337,
CC PubMed:19781752, PubMed:19119011, PubMed:28301465). Component of the
CC dosage compensation complex, which consists of the condensin I-like
CC components mix-1/SMC2 and dpy-27/SMC4, and the three non SMC subunits
CC dpy-26, capg-1 and dpy-28 (PubMed:19119011, PubMed:19781752). Within
CC the complex, interacts with dpy-27, dpy-28, mix-1 and capg-1
CC (PubMed:8939870, PubMed:15557118, PubMed:18198337, PubMed:19781752,
CC PubMed:19119011, PubMed:9458050, PubMed:28301465). The interaction with
CC dpy-27 is required for dpy-27 protein stability (PubMed:8939870).
CC Interacts with smcl-1 (PubMed:28301465). {ECO:0000269|PubMed:15557118,
CC ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:19119011,
CC ECO:0000269|PubMed:19781752, ECO:0000269|PubMed:28301465,
CC ECO:0000269|PubMed:8939870, ECO:0000269|PubMed:9458050}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11937488,
CC ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:8939869}. Chromosome
CC {ECO:0000269|PubMed:11937488, ECO:0000269|PubMed:18198337,
CC ECO:0000269|PubMed:8939869}. Note=During meiosis and mitosis, localizes
CC to condensed chromosomes (PubMed:8939869). In interphase cells,
CC diffusely distributed in nuclei of hermaphrodite embryos prior to the
CC onset of dosage compensation (PubMed:8939869). Localizes to the X
CC chromosome after the 40-cell stage when dosage compensation is
CC initiated in hermaphrodite (XX) but not in male (X0) embryos, where it
CC remains diffusely nuclear (PubMed:8939869, PubMed:18198337).
CC {ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:8939869}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos and in somatic and germline
CC tissues in L4 stage larvae (at protein level).
CC {ECO:0000269|PubMed:8939869}.
CC -!- DISRUPTION PHENOTYPE: Results in larval lethality in XX hermaphrodites;
CC survivors exhibit shorter and stouter body morphology and are egg-
CC laying defective (PubMed:2917714). Male animals are viable
CC (PubMed:2917714). Higher percentage of spontaneous males through X
CC chromosome non-disjunction (PubMed:2917714). Disrupts protein stability
CC of dpy-27 (PubMed:8939870). Disrupts localization of dpy-28 and of
CC capg-1 to the hermaphrodite X-chromosome (PubMed:18198337,
CC PubMed:19119011). RNAi-mediated knockdown results in chromosome
CC segregation defects in mitosis and meiosis (PubMed:19119011). In a sex-
CC 1 mutant background, leads to high embryonic lethality
CC (PubMed:19119011). {ECO:0000269|PubMed:18198337,
CC ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:2917714,
CC ECO:0000269|PubMed:8939870}.
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; U43562; AAC47411.1; -; mRNA.
DR EMBL; BX284604; CAA94575.1; -; Genomic_DNA.
DR PIR; T19472; T19472.
DR RefSeq; NP_502378.1; NM_069977.5.
DR AlphaFoldDB; G5EGE9; -.
DR SMR; G5EGE9; -.
DR ComplexPortal; CPX-1271; Condensin I complex.
DR ComplexPortal; CPX-1273; Condensin I-like dosage compensation complex.
DR IntAct; G5EGE9; 5.
DR STRING; 6239.C25G4.5; -.
DR EPD; G5EGE9; -.
DR PaxDb; G5EGE9; -.
DR PeptideAtlas; G5EGE9; -.
DR EnsemblMetazoa; C25G4.5.1; C25G4.5.1; WBGene00001085.
DR GeneID; 178196; -.
DR KEGG; cel:CELE_C25G4.5; -.
DR CTD; 178196; -.
DR WormBase; C25G4.5; CE08398; WBGene00001085; dpy-26.
DR eggNOG; ENOG502TG5K; Eukaryota.
DR HOGENOM; CLU_007170_0_0_1; -.
DR InParanoid; G5EGE9; -.
DR OMA; FQKATKG; -.
DR OrthoDB; 257799at2759; -.
DR PRO; PR:G5EGE9; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001085; Expressed in embryo and 4 other tissues.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:WormBase.
DR GO; GO:0000796; C:condensin complex; IPI:ComplexPortal.
DR GO; GO:0046536; C:dosage compensation complex; IPI:WormBase.
DR GO; GO:0000228; C:nuclear chromosome; IDA:WormBase.
DR GO; GO:0000805; C:X chromosome; IC:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0042464; P:dosage compensation by hypoactivation of X chromosome; IMP:WormBase.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:WormBase.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IC:ComplexPortal.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Coiled coil; DNA condensation;
KW Meiosis; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..1263
FT /note="Condensin complex subunit dpy-26"
FT /id="PRO_0000440174"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 691..725
FT /evidence="ECO:0000255"
FT COMPBIAS 13..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 142596 MW; EA9951E848E66089 CRC64;
MDVPSSSNVT GRRKRQVLDD DEDDGFRSTP LRKVRGTKKI RPADVVPETI MTKIGAHIDD
IVNKKKVGEL NCFEYKSPLE IHTIEDMIKA KASIQEMAVV LEGAQCIIGY RVDRLHHDVR
QIDSALSSGT VMRDSNGEEI HLTLESRKAK KKMAVVDGMN GMLDFLNNMD DALTTTELDA
DNDKNWKEDE ENIAGEPRID FKANSKDVDA FLQRDIFPEK LIYALSIKRA TDLRADLLSD
VSNYISADDT AHDLKDANID WLRANPTFQK ATKGSVCNSS NSFHSLNYYG IHSPDGRTLM
LHNRIADKNA DDRFFTSDVS VSLVKNTRAL LTNSLDKKPR ILDNYLMLEV KDRPVIGRYK
IMSKDVKKST LPLAESSREK DLANLTFAEM NHRPSNLDMT VAGASDMSML PGNQGLPLAQ
GENDETIALD RLTPPLQSSV SQKASDEYVL PPLEANDLDE HLIGKLPIEP NEMDQTLANM
FDKKLEVFNT SDTLESKVWK NGIRAEEWGE DDEAIMKNDT KHPRQAGIEG WIKATDAWTN
YDVVKMNVNR EARSQLDENA IDEQESYRNM VPEIGKNLFL VKSDDYMNNY PGDRPADFTV
NDEVSDVMKM WSGEDSTAED DVPLEQIQQE IREQVQQQDV DMEPIEEMDY DAGGAAFDVD
FDDRLAAPVE VEEMEGDNNR NDGRVADILF NEQMDETEVE ERNEQDVQRE LEDIALAADE
VAELMTSAPP PQLVGPSAEM REEIQNIGKN DNAHWVPPVV GDQERQAAVT AQRKRREKKA
KSRKATVEDF VHYFRDIPDD EIEREITAAK CSKIADEKST FLSEQQLYLP TLGIENKPHV
AFEMGLLGNS GMFFKKSYGK IRLERVKNQK AEQDLFIDEA RGNKDSDCLN WLLSFSGFRC
MENPEPITGS DSDENLRTAV EQPFDDDFAN DYYDEDRYDP NYEQQLAAAQ MGPDMQRKLA
LTASHINQMF PNIHSKRYGG EYGDSDDEFD DSFDRQSIQA KNLDAAKHKK CLAEILKTDS
LSMPSIQYVL EQLTSNQTLR MNNTTIRAAD DRNETGRPAT PTMEADKTLT SVFDYRSPNK
SNHDVNETMK ALTEMPDYQA ADERPNNQPT TSTYGTANTE NRKVHINGCH TLLSLALSMP
SRMGETVRPS SIVSFLLHIA NENNLQIVQD RSKRSWMSDF IVLNSSESLP RGLKMGRIED
QDEFWKRTQD PDAIEGTASD ANNVFSNLMR RPKAVPVRKG RGAGGQPTTS DLGAIVEEEE
MEE
