DPY27_CAEEL
ID DPY27_CAEEL Reviewed; 1469 AA.
AC P48996;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Chromosome condensation protein dpy-27;
DE AltName: Full=Protein dumpy-27;
GN Name=dpy-27; ORFNames=R13G10.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF LYS-128.
RC STRAIN=Bristol N2;
RX PubMed=7954812; DOI=10.1016/0092-8674(94)90255-0;
RA Chuang P.-T., Albertson D.G., Meyer B.J.;
RT "DPY-27: a chromosome condensation protein homolog that regulates C.
RT elegans dosage compensation through association with the X chromosome.";
RL Cell 79:459-474(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 FUNCTION.
RX PubMed=3779843; DOI=10.1016/0092-8674(86)90802-0;
RA Meyer B.J., Casson L.P.;
RT "Caenorhabditis elegans compensates for the difference in X chromosome
RT dosage between the sexes by regulating transcript levels.";
RL Cell 47:871-881(1986).
RN [4]
RP FUNCTION, AND 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 [5]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DPY-26, AND SUBCELLULAR
RP LOCATION.
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.
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 FUNCTION, INTERACTION WITH DPY-21, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=14660541; DOI=10.1242/dev.00886;
RA Yonker S.A., Meyer B.J.;
RT "Recruitment of C. elegans dosage compensation proteins for gene-specific
RT versus chromosome-wide repression.";
RL Development 130:6519-6532(2003).
RN [8]
RP IDENTIFICATION IN A DOSAGE COMPENSATION COMPLEX, AND INTERACTION WITH
RP 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 [9]
RP FUNCTION, IDENTIFICATION IN A DOSAGE COMPENSATION COMPLEX, AND INTERACTION
RP WITH DPY-26; DPY-28 AND MIX-1.
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 [10]
RP IDENTIFICATION IN A DOSAGE COMPENSATION COMPLEX, AND INTERACTION WITH
RP DPY-26.
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 [11]
RP FUNCTION, IDENTIFICATION IN A DOSAGE COMPENSATION COMPLEX, INTERACTION WITH
RP MIX-1; DPY-28; DPY-26 AND CAPG-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP 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 [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22393255; DOI=10.1128/mcb.06546-11;
RA Wells M.B., Snyder M.J., Custer L.M., Csankovszki G.;
RT "Caenorhabditis elegans dosage compensation regulates histone H4 chromatin
RT state on X chromosomes.";
RL Mol. Cell. Biol. 32:1710-1719(2012).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=23028348; DOI=10.1371/journal.pgen.1002933;
RA Vielle A., Lang J., Dong Y., Ercan S., Kotwaliwale C., Rechtsteiner A.,
RA Appert A., Chen Q.B., Dose A., Egelhofer T., Kimura H., Stempor P.,
RA Dernburg A., Lieb J.D., Strome S., Ahringer J.;
RT "H4K20me1 contributes to downregulation of X-linked genes for C. elegans
RT dosage compensation.";
RL PLoS Genet. 8:E1002933-E1002933(2012).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23884442; DOI=10.1242/dev.094292;
RA Webster C.M., Wu L., Douglas D., Soukas A.A.;
RT "A non-canonical role for the C. elegans dosage compensation complex in
RT growth and metabolic regulation downstream of TOR complex 2.";
RL Development 140:3601-3612(2013).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26641248; DOI=10.1371/journal.pgen.1005698;
RA Kramer M., Kranz A.L., Su A., Winterkorn L.H., Albritton S.E., Ercan S.;
RT "Developmental dynamics of X-chromosome dosage compensation by the DCC and
RT H4K20me1 in C. elegans.";
RL PLoS Genet. 11:E1005698-E1005698(2015).
RN [16]
RP INTERACTION WITH SMCL-1; MIX-1; DPY-26; 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: Central component of the condensin I-like dosage compensation
CC complex that associates specifically with hermaphrodite X chromosomes
CC to reduce their gene transcription throughout development
CC (PubMed:7954812, PubMed:3779843, PubMed:26641248, PubMed:8939870,
CC PubMed:14660541, PubMed:22393255, PubMed:19119011). Its strong
CC similarity with the condensin subunit smc4 suggests that it may reduce
CC the X-chromosome transcript level by condensing the chromatin structure
CC during interphase (PubMed:8939870). Involved in the recruitment of the
CC dosage compensation proteins mix-1 and dpy-21 to the X chromosome
CC (PubMed:14660541, PubMed:9458050). Might be involved in the reduction
CC of histone H4 lysine 16 acetylation (H4K16ac) on dosage compensated X
CC chromosomes (PubMed:22393255). As a member of the dosage compensation
CC complex, also binds to regulatory regions of the autosomal her-1 gene,
CC required for male development, possibly contributing to its repression
CC in hermaphrodites (PubMed:11937488). Also plays a role in the
CC regulation of growth and body fat metabolism downstream of the TOR
CC complex 2 pathway (PubMed:23884442). {ECO:0000269|PubMed:11937488,
CC ECO:0000269|PubMed:14660541, ECO:0000269|PubMed:18198337,
CC ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:22393255,
CC ECO:0000269|PubMed:23884442, ECO:0000269|PubMed:26641248,
CC ECO:0000269|PubMed:3779843, ECO:0000269|PubMed:7954812,
CC ECO:0000269|PubMed:8939870, ECO:0000269|PubMed:9458050}.
CC -!- SUBUNIT: Component of the dosage compensation complex, which contains
CC the mix-1/SMC2 and dpy-27/SMC4 heterodimer, and three non SMC subunits
CC that probably regulate the complex: dpy-26, capg-1 and dpy-28
CC (PubMed:8939870, PubMed:15557118, PubMed:18198337, PubMed:19781752,
CC PubMed:19119011). Within the complex, interacts with dpy-28, mix-1,
CC dpy-26 and capg-1 (PubMed:15557118, PubMed:18198337, PubMed:19781752,
CC PubMed:19119011, PubMed:9458050, PubMed:28301465). Interacts with dpy-
CC 21 (PubMed:14660541). Interacts with dpy-28; the interaction is
CC required for dpy-28 protein stability and dpy-28 association with the X
CC chromosome (PubMed:18198337). Interacts with smcl-1 (PubMed:28301465).
CC {ECO:0000269|PubMed:14660541, 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 -!- INTERACTION:
CC P48996; Q09591: mix-1; NbExp=5; IntAct=EBI-1152153, EBI-1152136;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14660541,
CC ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:23028348,
CC ECO:0000269|PubMed:7954812, ECO:0000269|PubMed:8939870}. Chromosome
CC {ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:23028348,
CC ECO:0000269|PubMed:7954812, ECO:0000269|PubMed:8939870}. Note=In
CC interphase cells, diffusely distributed in nuclei before the onset of
CC dosage compensation (PubMed:19119011). Associates with chromatin after
CC the 30-cell stage when dosage compensation is initiated
CC (PubMed:7954812, PubMed:23028348, PubMed:19119011). Specifically
CC localizes to the X chromosomes of hermaphrodite (XX) embryos, but
CC remains diffusely distributed throughout the nuclei of male (XO)
CC embryos (PubMed:7954812, PubMed:23028348). dpy-26 is required for its X
CC chromosome specific association (PubMed:8939870).
CC {ECO:0000269|PubMed:14660541, ECO:0000269|PubMed:19119011,
CC ECO:0000269|PubMed:23028348, ECO:0000269|PubMed:7954812,
CC ECO:0000269|PubMed:8939870}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and early-staged larvae
CC (PubMed:7954812). Also expressed in adult gut nuclei (PubMed:14660541).
CC {ECO:0000269|PubMed:14660541, ECO:0000269|PubMed:7954812}.
CC -!- DOMAIN: Consists of two putative central coiled-coil regions flanked by
CC putative globular regions at the N- and C-termini.
CC {ECO:0000303|PubMed:8939870}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes derepression of X
CC chromosome linked genes in embryos and in larval stages L1 and L3
CC (PubMed:26641248). Leads to an increase of 'Lys-16' acetylation of
CC histone H4 (H4K16ac) on hermaphrodite X chromosomes (PubMed:22393255).
CC In the TOR complex 2 mutant background rict-1, suppresses the growth
CC delay and elevated body fat index (PubMed:23884442). In a sex-1 mutant
CC background, leads to high XX-specific embryonic lethality
CC (PubMed:19119011). {ECO:0000269|PubMed:19119011,
CC ECO:0000269|PubMed:22393255, ECO:0000269|PubMed:23884442,
CC ECO:0000269|PubMed:26641248}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily. {ECO:0000305}.
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DR EMBL; L35274; AAA62647.1; -; Genomic_DNA.
DR EMBL; Z35602; CAA84669.1; -; Genomic_DNA.
DR PIR; T24216; T24216.
DR RefSeq; NP_497771.1; NM_065370.4.
DR AlphaFoldDB; P48996; -.
DR SMR; P48996; -.
DR BioGRID; 40730; 11.
DR ComplexPortal; CPX-1273; Condensin I-like dosage compensation complex.
DR IntAct; P48996; 4.
DR STRING; 6239.R13G10.1; -.
DR iPTMnet; P48996; -.
DR EPD; P48996; -.
DR PaxDb; P48996; -.
DR PeptideAtlas; P48996; -.
DR PRIDE; P48996; -.
DR EnsemblMetazoa; R13G10.1.1; R13G10.1.1; WBGene00001086.
DR GeneID; 175492; -.
DR KEGG; cel:CELE_R13G10.1; -.
DR UCSC; R13G10.1; c. elegans.
DR CTD; 175492; -.
DR WormBase; R13G10.1; CE01052; WBGene00001086; dpy-27.
DR eggNOG; KOG0996; Eukaryota.
DR GeneTree; ENSGT00900000141094; -.
DR HOGENOM; CLU_001042_4_1_1; -.
DR InParanoid; P48996; -.
DR OMA; PELIHNS; -.
DR OrthoDB; 326079at2759; -.
DR PhylomeDB; P48996; -.
DR PRO; PR:P48996; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001086; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0046536; C:dosage compensation complex; IPI:WormBase.
DR GO; GO:0000228; C:nuclear chromosome; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0000805; C:X chromosome; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0042464; P:dosage compensation by hypoactivation of X chromosome; IMP:WormBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IC:ComplexPortal.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 2.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromosome; Coiled coil; DNA condensation; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..1469
FT /note="Chromosome condensation protein dpy-27"
FT /id="PRO_0000119023"
FT DOMAIN 621..736
FT /note="SMC hinge"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 356..542
FT /evidence="ECO:0000255"
FT COILED 805..974
FT /evidence="ECO:0000255"
FT COILED 1016..1056
FT /evidence="ECO:0000255"
FT COILED 1159..1182
FT /evidence="ECO:0000255"
FT COMPBIAS 7..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 128
FT /note="K->E,I: Loss of function."
FT /evidence="ECO:0000269|PubMed:7954812"
SQ SEQUENCE 1469 AA; 169619 MW; EF9043CA2AC23B06 CRC64;
MQPFKRRALT SDDDRPYADT DSMPEVDLDV DRRRQYMEQL NIFDDVSSGA YMLELEAAEN
GVKYDEKEDL LNVQIPPKYE DQISDPDGNR MIILNIYVEN FKSYAGKHIL GPFHKNLTMI
LGPNGSGKSN VIDALLFVFG FKAGKIRTKK LSALINSGGN YESCSVTIMF QMVKDMPVEN
YDKYEVLTDN CVCITRTINR ENNSKYRIDD KDASQKDVQE LLLRAGIDMT HNRFLILQGE
VEAIALMKPT SKNPNEEGML EYIEDIVGTN RFVAPISKLM HRVSLLEHKS SQYGASVRRH
EGHLKVFEKA MVIGMAYLNT FNNLNYLRGI RVKHNLCRYA ETMRDAKMSL VTRTGELEEN
KDIMLEAKDE VRKKETHERS LNSIVTELEN KRIDWQSKKN DWHARDAKRK QGLKSCTQDL
GKLMKERDEA RREKFEIETA PENARISKQN MQLEWDQLKE QENVCQRTAT ENLIKYDQKS
SADRAKHDDL EKKLSDELLQ SMRAKAELDV SESELKDMTI MMEQGQKRVD ELKGTLQTMM
AENIRDNTEL NAVTTELQDR KLKFDKAVEK LPHLKSTEQL LRSKKYELDQ EVIEASNTQE
VTYRHQATAK LHELKEAGLF PGFKGRLGDL ASIPIKFDTA ISTVFFAQLD YHVVQTSDEC
RIGIGFCHEY KLPRTTFVFL DHLKDTDTSG MDSTMKFPAE RLFDKIHCVN PEIRREFYFL
IHDILVVDSL EEATRIDKKY PGRHRYCTLN GSILNRSGAL TGGGKPTTGR IRNDNNPNMS
GVKKVDLSKL RAAQEKHNHA LEAHLKLQLK QEEIRADNGP IIKQLEIRKR ELIMSTKEQK
TRIAELKSSI AAHERRMVNY REVTVEDLDE KRAQIADLKR QVEESQKSSA KIKQQIEQYK
RKMDRMFMEL VQKNKDSIEQ AKDRMGQLEQ DIARQTAIIE NNPSHLEQAE KKLSELEHMC
LEKRSEADAL AQLEVGEDVK GIDIINAQLQ TSTASIDAQR ARYTEAVAAR READAAYQTT
VDNYNMVKQT YDELMRIIDD LENKTMADNA ELDIIESAWM QPEKLYPPGK FVRYNDPDIA
AKMTDGHVVL PYECISMIEP HREAYEEHEA RMLEDDVFED TANKICKLEK DVDKFRREFD
NKGVRDYAMI VSLLMNEVTS AKKFSDKLKA HREKLNELRM ARFNEFSEAL AFLGTTTQML
YQLITNGGDA SLKFVEEGKS TDPFDGGIKF SVRPAKKSWK LIENLSGGEK TLASLCFVFA
MHHYRPTPLY VMDEIDAALD LNNVSLIANY IKHSERTRNA QFIIISLRNQ MFEVGNRLLG
IYKIDGKTYN IMVDPIAVEI KNRPILKIFE EEIKRREKLR RAEIEPEIDL SNGLSNVVIA
PKRKQRRLEM LKLSDFGLDD DSDLPEFNRF PPATRRELSV EDSDEDDEPV RRRPRRQVEE
EDEEDELIEE ATPSPPPIVV QRRVRRSRH
