CAPG1_CAEEL
ID CAPG1_CAEEL Reviewed; 1153 AA.
AC G5EFJ4;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Condensin complex subunit capg-1 {ECO:0000305};
GN Name=capg-1 {ECO:0000312|WormBase:F29D11.2};
GN ORFNames=F29D11.2 {ECO:0000312|WormBase:F29D11.2};
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;
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, IDENTIFICATION IN A CONDENSIN I COMPLEX, AND INTERACTION WITH
RP DPY-26 AND SMC-4.
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 [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A CONDENSIN I COMPLEX AND IN A DOSAGE
RP COMPENSATION COMPLEX, INTERACTION WITH MIX-1; SMC-4; DPY-27; DPY-28 AND
RP DPY-26, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 [4]
RP SUBCELLULAR LOCATION.
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 [5]
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: Member of two distinct condensin I complexes, the condensin I
CC complex and the condensin I-like dosage compensation complex
CC (PubMed:19781752, PubMed:19119011). The condensin I complex is required
CC for conversion of interphase chromatin into mitotic-like condensed
CC chromosomes and for chromosome segregation in meiosis and mitosis
CC (PubMed:19781752, PubMed:19119011). As a member of the condensin I
CC complex, further controls crossover number and distribution in meiosis
CC by restricting double strand break formation, probably by influencing
CC higher-order chromosome structure (PubMed:19781752). Regulatory subunit
CC of the condensin I-like dosage compensation complex that associates
CC specifically with hermaphrodite X chromosomes to reduce their gene
CC transcription during interphase, possibly through chromatin
CC reorganization (PubMed:19119011). {ECO:0000269|PubMed:19119011,
CC ECO:0000269|PubMed:19781752}.
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). Within the complex, interacts with
CC dpy-26, mix-1, smc-4 and dpy-28 (PubMed:19781752, PubMed:19119011,
CC PubMed:28301465). Component of the dosage compensation complex, which
CC consists of the condensin I-like components mix-1/SMC2 and dpy-27/SMC4,
CC and the three non-SMC subunits dpy-26, capg-1 and dpy-28
CC (PubMed:19119011). Within the complex, interacts with mix-1, dpy-27,
CC dpy-26 and dpy-28 (PubMed:19119011, PubMed:28301465). Interacts with
CC smcl-1 (PubMed:28301465). {ECO:0000269|PubMed:19119011,
CC ECO:0000269|PubMed:19781752, ECO:0000269|PubMed:28301465}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:19119011,
CC ECO:0000269|PubMed:23684975}. Note=During meiosis and mitosis,
CC localizes to condensed chromosomes in both sexes (PubMed:19119011).
CC Localizes to the spindle midzone in between separating chromosomes
CC during anaphase and to the midbody during cytokinesis
CC (PubMed:23684975). During interphase, localizes specifically to X
CC chromosomes in hermaphrodites after the onset of dosage compensation
CC (PubMed:19119011). {ECO:0000269|PubMed:19119011,
CC ECO:0000269|PubMed:23684975}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos and in somatic and germline
CC tissues in adult animals (at protein level).
CC {ECO:0000269|PubMed:19119011}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown disrupts X-chromosome
CC localization of dpy-27, mix-1, dpy-26 and sdc-3. Results in chromosome
CC segregation defects in mitosis leading to aneuploidy. In a sex-1 mutant
CC background, leads to high embryonic lethality.
CC {ECO:0000269|PubMed:19119011}.
CC -!- SIMILARITY: Belongs to the CND3 (condensin subunit 3) family.
CC {ECO:0000305}.
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DR EMBL; BX284601; CAA98126.1; -; Genomic_DNA.
DR PIR; T21386; T21386.
DR RefSeq; NP_492128.1; NM_059727.4.
DR AlphaFoldDB; G5EFJ4; -.
DR ComplexPortal; CPX-1271; Condensin I complex.
DR ComplexPortal; CPX-1273; Condensin I-like dosage compensation complex.
DR IntAct; G5EFJ4; 5.
DR STRING; 6239.F29D11.2; -.
DR EPD; G5EFJ4; -.
DR PaxDb; G5EFJ4; -.
DR PeptideAtlas; G5EFJ4; -.
DR EnsemblMetazoa; F29D11.2.1; F29D11.2.1; WBGene00009254.
DR GeneID; 172521; -.
DR KEGG; cel:CELE_F29D11.2; -.
DR CTD; 172521; -.
DR WormBase; F29D11.2; CE09790; WBGene00009254; capg-1.
DR eggNOG; ENOG502T1ZK; Eukaryota.
DR HOGENOM; CLU_264026_0_0_1; -.
DR InParanoid; G5EFJ4; -.
DR OMA; IMIVSAM; -.
DR OrthoDB; 571558at2759; -.
DR Reactome; R-CEL-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:G5EFJ4; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009254; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000793; C:condensed chromosome; IBA:GO_Central.
DR GO; GO:0000796; C:condensin complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046536; C:dosage compensation complex; IPI:WormBase.
DR GO; GO:0000805; C:X chromosome; IC:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0042464; P:dosage compensation by hypoactivation of X chromosome; IC:ComplexPortal.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:UniProtKB.
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 Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027165; CND3.
DR InterPro; IPR025977; Cnd3_C.
DR PANTHER; PTHR14418; PTHR14418; 1.
DR Pfam; PF12719; Cnd3; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; DNA condensation; Meiosis; Mitosis;
KW Reference proteome.
FT CHAIN 1..1153
FT /note="Condensin complex subunit capg-1"
FT /id="PRO_0000440163"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1153 AA; 131465 MW; C303376F90FE5489 CRC64;
MPPKKRIRGP KLPALREEKS TGTDVASDES FNESADFLNN EELNNDQNDA ENTVLSEGVS
TLRINENMTK EDRACISAAL FIKKRVVESI RTVFQSRDDI NDEIHTSSRK LIAAFKKADQ
NRKKKVDLMK VFLDEIDVRL SMIIEEVTVP EHRARVFKLI AVTITEIQAF KLPSDLLDFI
INFINTWGHS DNVAARINTT CFISYIFETG KRYLTTEGEY SGFEVKIAAK MFLQLKRALL
DKEQTARVPA IRGLGFLQEI PIPSNWPVDA MKHSPRELLL RSCRDTAWEC RLVAVQSMVP
LETDVRLLSD IVYYDKCLNV RVAALEQFSN LRPNKHVREK IEMLDLCLKD HEVNIRDAAK
EVLKNWVRNL STRWSESQKS KDSNDVVILN SNSESTTGEE NKMKGYILAA QALTLLWLTG
ALETLEGHSN LRRLITHTLD VIRQMYVCQA DPINTFAEVL ISDLREKMKS SAVPIITKST
VGSILDDSEL ADTQDPSTNR AMIFFWRCLV DYISDRKRND ADKINAMSRF VSPLRTMVEH
VEKILVRVKN LDVYPNISQR ADYEDHTFVL QMSIVENIIC VMRHAPTDQP GVDAYKQMLI
SMLMNVFYQK KVIDLIVQEL AQFYKEDPNA LFTLFNDRIE EMRSKYKSGQ FPVIENSVPV
GETKVRKDLE EETRKTGRRT ISDKDGIAVI DLYELKVLNA LLKTGILLGW STTYQNRYNN
KLREGISSKD LSTRVLCTEC IGIGAIYDYD QAENTLREMM KSFNTQDEPV QCSLIAALTD
IQIEHGDQVD ALFSWNSKQP NFAVFLSDIV VNAHVSGECE TMLRAVEAIS RLFLNTKIDP
NQQKWQRTMV TLMTRASYAI TNRFSAKVRS TIIVMLKFFC SINKNNQLLL IKSFHNFFDM
WANSTTPERL TENRHEMVTK LKRCAATFVA LTRHSTLPLE EQKKCKPTHV DLVDDIFHEM
AGAPDSTSVD YYICALNFVE YQSLSRSALT KIHGDLESYI FLHELDGDKH RYNELRKAHR
KIAKILGLNE DEIEEVPSKT DLRKEAAPSK TNKRNANLIS TDIAVDNDVN MEEDDKPGPS
RPATVRKPRA PRATPASATK KKPLVEEDAL EILKSPPRNT KKPPSRPTTA TRPTAVAART
APPRSARKLR SEK
