SMC4_CAEEL
ID SMC4_CAEEL Reviewed; 1549 AA.
AC Q20060;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Structural maintenance of chromosomes protein 4;
DE Short=SMC protein 4;
DE Short=SMC-4;
GN Name=smc-4; ORFNames=F35G12.8;
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 [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]
RP FUNCTION, INTERACTION WITH MIX-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11914278; DOI=10.1101/gad.968302;
RA Hagstrom K.A., Holmes V.F., Cozzarelli N.R., Meyer B.J.;
RT "C. elegans condensin promotes mitotic chromosome architecture, centromere
RT organization, and sister chromatid segregation during mitosis and
RT meiosis.";
RL Genes Dev. 16:729-742(2002).
RN [3]
RP FUNCTION, IDENTIFICATION IN A CONDENSIN I COMPLEX AND IN A CONDENSIN II
RP COMPLEX, AND INTERACTION WITH CAPG-1; DPY-26; MIX-1; DPY-28 AND HCP-6.
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 [4]
RP FUNCTION, IDENTIFICATION IN A CONDENSIN I COMPLEX AND IN A CONDENSIN II
RP COMPLEX, AND INTERACTION WITH MIX-1; DPY-28; CAPG-1; DPY-26; HCP-6; CAPG-2
RP AND KLE-2.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [6]
RP INTERACTION WITH SMCL-1; DPY-26 AND KLE-2, 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: Central component of the condensin I complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes (PubMed:11914278, PubMed:19781752). The condensin
CC I complex introduces positive supercoils into relaxed DNA in the
CC presence of type I topoisomerases (PubMed:11914278). Converts nicked
CC DNA into positive knotted forms in the presence of type II
CC topoisomerases (By similarity). Also a central component of the
CC condensin II complex, a complex that seems to play a role in prophase
CC chromosome condensation (PubMed:19119011, PubMed:19781752). Both the
CC condensin complex I and II play a role in meiotic and mitotic
CC chromosome segregation (PubMed:11914278, PubMed:19119011,
CC PubMed:23684975). Plays a role in robust cytokinesis upon the presence
CC of chromatin obstructions (PubMed:23684975).
CC {ECO:0000250|UniProtKB:P50532, ECO:0000269|PubMed:11914278,
CC ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:19781752,
CC ECO:0000269|PubMed:23684975}.
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:11914278, PubMed:19781752). Within the
CC complex, interacts with mix-1, dpy-26, capg-1 and dpy-28
CC (PubMed:11914278, PubMed:19781752, PubMed:19119011, PubMed:28301465).
CC Component of the condensin II complex, which contains the mix-1/SMC2
CC and smc-4/SMC4 heterodimer, and three non SMC subunits, kle-2, capg-2
CC and hcp-6 that probably regulate the complex (PubMed:19781752,
CC PubMed:19119011). Within the complex, interacts with mix-1, kle-2,
CC capg-2 and hcp-6 (PubMed:19781752, PubMed:19119011, PubMed:28301465).
CC Interacts with smcl-1 (PubMed:28301465). {ECO:0000269|PubMed:11914278,
CC ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:19781752,
CC ECO:0000269|PubMed:28301465}.
CC -!- INTERACTION:
CC Q20060; Q09591: mix-1; NbExp=6; IntAct=EBI-1152127, EBI-1152136;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11914278}. Chromosome
CC {ECO:0000269|PubMed:11914278}. Note=Localizes to condensed chromosomes
CC during mitosis and meiosis. Localizes to chromosomes in a faint
CC speckled pattern during prophase, then appears in two stripes outlining
CC each chromosome during prometaphase. During metaphase, localizes at the
CC poleward face of the condensed chromosomes. Dissociation from
CC chromosomes is observed in late telophase.
CC {ECO:0000269|PubMed:11914278}.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterodimerization with
CC mix-1, forming a V-shaped heterodimer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown disrupts prometaphase
CC chromosome organization and chromosome segregation in mitosis and
CC meiosis II and leads to aneuploidy throughout development
CC (PubMed:11914278, PubMed:23684975). Disrupts mix-1 localization to
CC mitotic chromosomes (PubMed:11914278). Increased levels of
CC phosphorylated air-2 at the spindle midzone, indicating activation of
CC the abscission checkpoint (PubMed:23684975). Results in cleavage furrow
CC regression and failed cytokinesis during the first and second embryonic
CC divisions (PubMed:23684975). {ECO:0000269|PubMed:11914278,
CC ECO:0000269|PubMed:23684975}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily. {ECO:0000305}.
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DR EMBL; Z46242; CAA86336.1; -; Genomic_DNA.
DR PIR; T21809; T21809.
DR RefSeq; NP_497935.1; NM_065534.5.
DR AlphaFoldDB; Q20060; -.
DR SMR; Q20060; -.
DR BioGRID; 40839; 11.
DR ComplexPortal; CPX-1271; Condensin I complex.
DR ComplexPortal; CPX-1272; Condensin II complex.
DR IntAct; Q20060; 7.
DR STRING; 6239.F35G12.8; -.
DR iPTMnet; Q20060; -.
DR EPD; Q20060; -.
DR PaxDb; Q20060; -.
DR PeptideAtlas; Q20060; -.
DR EnsemblMetazoa; F35G12.8.1; F35G12.8.1; WBGene00004874.
DR GeneID; 175603; -.
DR KEGG; cel:CELE_F35G12.8; -.
DR UCSC; F35G12.8; c. elegans.
DR CTD; 175603; -.
DR WormBase; F35G12.8; CE03287; WBGene00004874; smc-4.
DR eggNOG; KOG0996; Eukaryota.
DR GeneTree; ENSGT00900000141094; -.
DR HOGENOM; CLU_001042_4_1_1; -.
DR InParanoid; Q20060; -.
DR OMA; QIYIDEC; -.
DR OrthoDB; 326079at2759; -.
DR PhylomeDB; Q20060; -.
DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-CEL-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:Q20060; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004874; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:WormBase.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0000796; C:condensin complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045132; P:meiotic chromosome segregation; IC:ComplexPortal.
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:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR CDD; cd03274; ABC_SMC4_euk; 2.
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; IPR041738; SMC4_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
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; Cell cycle; Cell division; Chromosome; Coiled coil;
KW DNA condensation; Meiosis; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1549
FT /note="Structural maintenance of chromosomes protein 4"
FT /id="PRO_0000119024"
FT DOMAIN 619..734
FT /note="SMC hinge"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 326..604
FT /evidence="ECO:0000255"
FT COILED 786..1058
FT /evidence="ECO:0000255"
FT COILED 1144..1182
FT /evidence="ECO:0000255"
FT COMPBIAS 18..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
SQ SEQUENCE 1549 AA; 176572 MW; DF752147301934BF CRC64;
MPPKTSAAPP QSDESDSDFD DAPVKKPQKK TTKPVNRHKE GSKDPEEELQ RAVNEKFDGS
DGEDDDSDLF SLQLPSRPDF LTKPNRADRL MIRNVEVDNF KSYFGKASIG PFHKSFTSII
GPNGSGKSNL IDSLLFVFGF RASKIRSAKV SNLIHKSAGR NPDKCTVTIH FQRIVDIPGH
YEVVKDSEFT ISRTAFQNNS SSYAIDGRPA TKNEVEARLR RVDIDIEHNR FLILQGEVEQ
IAMMKPVKTT KSETGMVEYL EDIIGTNRLE PFVKLFQRRV NRLTCDLSQQ RIARDHARNS
KVAMENPVRA AIEFLMKENE ATTIHMKLEQ RRRQRYLDKI APKQAELDKM KEEMKSIAET
LDTNKNEYKQ SEEAQKVMIE ERSKLDKNFD SLSKELSDLG TEETRRKEAL KRHQANISKA
EAEKEKEVKK RSNLEAAPEK AERKIAKCQE EVEQLLEIEK TANEEADKNL DEFEKRSEAP
KEEQKKIQET WAQKSNEFNK VRGEARIARE DFEDLKKLAN SGTDKLIELK KRLESSEESY
AKEKDELDKL KPEFDSWNDK LKQLSTELPT LRNTARQKNQ DLAKTRDRLE TLRQQNSSCS
SSNKVIQALM KEKEAGRIKS FHGRLGDLGV IDPKYEGAIC TNFGARLNYL IVGKEEDAKN
VINFLVANKL PRQTVQPLDK IKCDKRDLAP NPTNPLPAPR LIDLIDCDPV LKPAFYDMVR
SAIVGDSTQE AQRMHRMPAC RGVTVCTLEG SMIHPSGSFT GGGKTVKGLI LTDKNKMAKQ
VTPEDKAAER DLAEKLGKLR DEADELKGQE HEMDGQLIEA RRKVAEMSNR LSIVTSSVQS
AAPAIETLKK TIANQEKEAA KVKVDAKTLE DKQKIVEELE KKRDELGEEA AKVKARQAEI
QSKLDGIFKE LVQCHRDEAK ESLQKRQKLE KDIAKETANI SNSGRNIAKC DENISRHDKD
IEKMKKKCEE LMEKAIDDEE VKSKKETVER FEKQIKKLQT KGEEMTKKQS ELSAAETKLE
GELKKCSEGI KELKESMLAD RLKVEDIEKK LAALKVNRIP RFQFLIESSR PEDLEMQIDD
KMPVVDENQS PEEVERQKKH MACVMSDAAY ALEFEMRQKV LENTESYENV DGEDRVPVEL
LSDEKINEIS SRDAEEMQMK LKVCEQQVEA LKAKVDISSI KAYVDKVKQY NEQVIKLTIA
TEVHRKHNQE LQRIKQMRLE EFHSAFEFIG KHLVAVFKML TDGGDAKLEY IDKDDPFRQG
ISFMVRPAKK AWKQIQFLSG GEKTLSSLAL IFALHMFRPT PFYVMDEIDA ALDYRNVSII
AQYVRQKTEN AQFIIISLRN NMFELANRLV GIYKVDGCTR NVAIDPLRVC EMAKQITDSL
GQATCTLPDE VTQRFNETMS RQNKEMIAQE KQYPNFPSSN EISKAEKIVN VEGRVRKELI
QTTRDVTSRP QSKATTSGDG TERPASRSAS RPESRINQMK YPAPRLVERS SSQNVRSPRK
ARNIEADETT PPSKRSNSAS TPKRSPMKPL TPSSKKKEKA IVDDDDDME
