CND1_CAEEL
ID CND1_CAEEL Reviewed; 1499 AA.
AC Q9U2M1;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Condensin complex subunit 1 {ECO:0000255|PIRNR:PIRNR017127};
DE AltName: Full=Non-SMC condensin I complex subunit dpy-28 {ECO:0000305};
GN Name=dpy-28 {ECO:0000312|WormBase:Y39A1B.3};
GN ORFNames=Y39A1B.3 {ECO:0000312|WormBase:Y39A1B.3};
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|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 [2] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-1122.
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 [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A DOSAGE COMPENSATION COMPLEX, AND INTERACTION
RP WITH MIX-1; DPY-27 AND DPY-26.
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 [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A DOSAGE COMPENSATION COMPLEX, INTERACTION WITH
RP MIX-1; DPY-26 AND DPY-27, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, 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 [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A CONDENSIN I COMPLEX AND IN A DOSAGE
RP COMPENSATION COMPLEX, INTERACTION WITH DPY-26 AND SMC-4, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLY-1122.
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 [6] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A CONDENSIN I COMPLEX AND IN A DOSAGE
RP COMPENSATION COMPLEX, INTERACTION WITH DPY-27; DPY-26; CAPG-1 AND SMC-4,
RP 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 [7]
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 [8]
RP SUMOYLATION.
RX PubMed=24043781; DOI=10.1073/pnas.1315793110;
RA Pferdehirt R.R., Meyer B.J.;
RT "SUMOylation is essential for sex-specific assembly and function of the
RT Caenorhabditis elegans dosage compensation complex on X chromosomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E3810-E3819(2013).
RN [9]
RP INTERACTION WITH SMCL-1; DPY-27 AND DPY-26, AND IDENTIFICATION BY MASS
RP 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
CC during mitosis and meiosis and X-chromosome dosage compensation
CC depending on its binding partners (PubMed:19119011, PubMed:19781752,
CC PubMed:3779843, PubMed:18198337). Regulatory subunit of the condensin I
CC complex, a complex required for conversion of interphase chromatin into
CC mitotic-like condense chromosomes (PubMed:19781752, PubMed:19119011).
CC The condensin I complex probably introduces positive supercoils into
CC relaxed DNA in the presence of type I topoisomerases and converts
CC nicked DNA into positive knotted forms in the presence of type II
CC topoisomerases (By similarity). The condensin I complex function is
CC required for proper chromosome segregation in mitosis and meiosis
CC (PubMed:19119011). As a member of the condensin I complex, further
CC controls the crossover number and distribution in meiosis by
CC restricting double strand break formation, possibly by influencing
CC higher-order chromosome structure (PubMed:18198337, PubMed:19781752).
CC Plays a role in robust cytokinesis upon presence of chromatin
CC obstructions (PubMed:23684975). Also a member of the condensin I-like
CC dosage compensation complex that associates specifically with
CC hermaphrodite X chromosomes to reduce their gene transcription during
CC interphase, possibly through chromatin reorganization (PubMed:3779843,
CC PubMed:19119011, PubMed:15557118). {ECO:0000250|UniProtKB:Q9YHY6,
CC ECO:0000255|PIRNR:PIRNR017127, ECO:0000269|PubMed:15557118,
CC ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:19119011,
CC ECO:0000269|PubMed:19781752, ECO:0000269|PubMed:23684975,
CC ECO:0000269|PubMed:3779843}.
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:19781752, PubMed:19119011, PubMed:18198337). Within the
CC complex, interacts with dpy-26 and smc-4 (PubMed:19781752,
CC PubMed:19119011, PubMed:28301465). Component of the dosage compensation
CC complex, which consist of the condensin I like components mix-1/SMC2
CC and dpy-27/SMC4, and the three non SMC subunits dpy-26, capg-1 and dpy-
CC 28 (PubMed:18198337, PubMed:19781752, PubMed:19119011,
CC PubMed:15557118). Within the complex, interacts with mix-1, dpy-27,
CC dpy-26 and capg-1 (PubMed:15557118, PubMed:18198337, PubMed:19119011,
CC PubMed:28301465). Interacts with smcl-1 (PubMed:28301465).
CC {ECO:0000269|PubMed:15557118, ECO:0000269|PubMed:18198337,
CC ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:19781752,
CC ECO:0000269|PubMed:28301465}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18198337}. Chromosome
CC {ECO:0000269|PubMed:18198337}. Note=During mitosis, localizes to
CC condensed chromosomes in both sexes. In interphase cells, diffusely
CC distributed in nuclei of hermaphrodite embryos prior to the onset of
CC dosage compensation. Localizes to the X chromosome after the 40-cell
CC stage when dosage compensation is initiated in hermaphrodite (XX) but
CC not in male (X0) embryos, where it remains diffusely nuclear.
CC {ECO:0000269|PubMed:18198337}.
CC -!- TISSUE SPECIFICITY: Expressed in somatic and germline tissues (at
CC protein level). {ECO:0000269|PubMed:18198337}.
CC -!- DEVELOPMENTAL STAGE: Associates with meiotic and mitotic chromosomes
CC prior to the onset of dosage compensation and with hermaphrodite X
CC chromosomes after the onset of dosage compensation (at protein level).
CC {ECO:0000269|PubMed:18198337}.
CC -!- PTM: Sumoylated. Sumoylated in the context of the dosage compensation
CC complex but not in the condensin I complex. Sumoylation is important
CC for assembly of the dosage compensation complex and its robust binding
CC to the X chromosome. {ECO:0000269|PubMed:24043781}.
CC -!- DISRUPTION PHENOTYPE: Results in high larval lethality in
CC hermaphrodites, and survivors exhibit a XX-specific shorter and stouter
CC body morphology (PubMed:18198337). Higher percentage of spontaneous
CC males through X chromosome non-disjunction (PubMed:18198337). Increased
CC number of crossovers, redistribution of crossovers and a reduction in
CC crossover interference in meiosis (PubMed:18198337). Increased number
CC of rad-51 foci in early to mid-pachytene indicating double strand break
CC formation (PubMed:18198337, PubMed:19781752). Increase in X chromosome
CC axis length indicating aberrant chromosome structure (PubMed:19781752).
CC RNAi-mediated knockdown results in chromosome segregation defects in
CC mitosis (PubMed:19119011). {ECO:0000269|PubMed:18198337,
CC ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:19781752}.
CC -!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family.
CC {ECO:0000255|PIRNR:PIRNR017127}.
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DR EMBL; BX284603; CAA16340.3; -; Genomic_DNA.
DR PIR; C88589; C88589.
DR PIR; T26747; T26747.
DR RefSeq; NP_499379.2; NM_066978.4.
DR AlphaFoldDB; Q9U2M1; -.
DR SMR; Q9U2M1; -.
DR ComplexPortal; CPX-1271; Condensin I complex.
DR ComplexPortal; CPX-1273; Condensin I-like dosage compensation complex.
DR IntAct; Q9U2M1; 4.
DR STRING; 6239.Y39A1B.3; -.
DR EPD; Q9U2M1; -.
DR PaxDb; Q9U2M1; -.
DR PeptideAtlas; Q9U2M1; -.
DR EnsemblMetazoa; Y39A1B.3.1; Y39A1B.3.1; WBGene00001087.
DR GeneID; 176509; -.
DR KEGG; cel:CELE_Y39A1B.3; -.
DR UCSC; Y39A1B.3; c. elegans.
DR CTD; 176509; -.
DR WormBase; Y39A1B.3; CE31734; WBGene00001087; dpy-28.
DR eggNOG; KOG0414; Eukaryota.
DR GeneTree; ENSGT00940000153566; -.
DR HOGENOM; CLU_004539_0_0_1; -.
DR InParanoid; Q9U2M1; -.
DR OMA; DVIAKLW; -.
DR OrthoDB; 166920at2759; -.
DR PhylomeDB; Q9U2M1; -.
DR Reactome; R-CEL-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:Q9U2M1; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001087; Expressed in embryo and 4 other tissues.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IBA:GO_Central.
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:0043073; C:germ cell nucleus; IDA:WormBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0000805; C:X chromosome; IDA:WormBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:WormBase.
DR GO; GO:0042464; P:dosage compensation by hypoactivation of X chromosome; IC:ComplexPortal.
DR GO; GO:0010032; P:meiotic chromosome condensation; IBA:GO_Central.
DR GO; GO:0045132; P:meiotic chromosome segregation; IC:ComplexPortal.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IC:ComplexPortal.
DR GO; GO:0045128; P:negative regulation of reciprocal meiotic recombination; IMP:WormBase.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026971; CND1/NCAPD3.
DR InterPro; IPR032682; Cnd1_C.
DR InterPro; IPR007673; Condensin_cplx_su1.
DR PANTHER; PTHR14222; PTHR14222; 1.
DR PANTHER; PTHR14222:SF2; PTHR14222:SF2; 1.
DR Pfam; PF12717; Cnd1; 1.
DR PIRSF; PIRSF017127; Condensin_D2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; DNA condensation; Meiosis; Mitosis;
KW Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..1499
FT /note="Condensin complex subunit 1"
FT /id="PRO_0000439858"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1421..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1122
FT /note="G->E: In y1; leads to XX-specific lethality.
FT Surviving hermaphrodites exhibit increased X-linked gene
FT transcripts and a shorter and stouter body morphology. XO
FT animals are wild-type males. Defects in mitotic chromosome
FT segregation."
FT /evidence="ECO:0000269|PubMed:19781752,
FT ECO:0000269|PubMed:3779843"
SQ SEQUENCE 1499 AA; 171022 MW; 779D91C23166E355 CRC64;
MPRKQRVVTT PSPPTSDEDE DMDFGSTSQQ QQQQPTRNND GLSGFKSITE IIAEADNNIP
SEQIDKDIDS FSSYSDISDW RGIPKFFPSL SSLSRRASTY ENWENRFKVV DYLVSCSGAL
KDSVSDYVAD YFEKNESGED HSVDVELVHA VSMFVILTQR LTVQLQLYVS KSIASANQQA
KRGTGRGGRQ VDLDDDIVKW KDIQRHRMIN CLLELLELRV DTVAGTKKKA IQYVFAPDVM
EKDFLLRFLD TVVQLLEDPE NMARSSQQWI SHYFRILKVL SADYGMTKDV ANCLFTALSH
SYLEAANTFP FIEPLVTLMK ENGEGSGRIY QPLRNVLQLV ICRVGNLYAG ERAEKPPPKA
FCMMVQSLAI NVHDLMLQDI THVYRLLQNQ HVNVRMSTLH ALADMFSSSY LSQSLCDTFA
SRRLKREGIF KRLLAHTNDE ATNVRSKAVS LLRNIMENRR IPEEFESCGL LSIVGSRLND
KSVQVRKSAI QFLTTFLDNN RHGHDFNREM HQLKLNAKCS ELRNAEEPQS KAIQGAENAF
RQNLFTLTAG VRVEVYDIFR RRYRVEPERS ITDILTGLFS PGSGNRLVRY YVAQENFPFR
DRIPSLRERR SDDMEDDDDD TVSLEDDDMT SLVSEVVKWV VAQAEEDYVT FKVQLTQMDD
DQLLENEQEA RDRNNQIMQL RAQVQQLINK MSIEQELSRC VTIALRCVLN GETAEIKEGI
RFLTRCKLFE ITGADDAIRS MCSLVWRPSA DILNELIEAA EDMFISRLDG NEKASERDSS
TVENLMKAMN GVTEKDRPSV EEVIYLLAAT ELVHVDSDKN KVPRKRRPIE ANVINKLWMI
ALDMSHGINS RKIDALRILY PISRSERGIA EARSRLRVVQ KKLMDPELAV DALRIISILG
TPTKLENEQD AYSRPLFKIH QDDSLWKSIE KLFFYEIMKA DDNPDRDWFG VIRLTITTIL
SLSMDVNVML PKLASHFVYR TKRISDFFLF YCDQVDDATD DTRKKMAQRR REYWALTYCR
VMEKLMAFIG EVAVQLNAYI QVTIPKLHTR YVSKMVDAEK NDANIREEPV RFLSDLEKSV
AQRKTIFTVP QDTTPGATSN DLHHLVSVMC DKRLFVPNKL MGRLLPIVVY GMRCKIMPTR
IRHAATVAYG KMMPLSAEIS AFAAPSFFSA MTKSSSILLR CNLVAACCDF AFAQPTLFEL
FAQSLFRMSQ DESPLAREST ILVLSHLMSN DMIQTRGVLS EAARCICDPT RAVRDVAQSF
FKELNSRTDT IIQLLPEFLY HLSNGNERMS FKSYKTVFEF LIQLLKDKPK ASADSMIDRV
CIKFSNTDMN DSETPKYLLV ALAKFVQNDG GLHRLQDNWR HWSKFMCHPS VAKEYRMMVE
HMHSTSKNDE FKSQCVELID NINKIESEGL RKEDVAIGSS ITKNKGRAKK NPTTMSGSSR
TTSRAANSRR RAPPPAQSDE DDSDSDDAPA APRSAARRKA KKSAVADDDS DSDEFMLDD
