MIX1_CAEEL
ID MIX1_CAEEL Reviewed; 1244 AA.
AC Q09591;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Mitotic chromosome and X-chromosome-associated protein mix-1;
DE AltName: Full=Lethal protein 29;
DE AltName: Full=Structural maintenance of chromosomes protein 2;
GN Name=mix-1; Synonyms=let-29, smc-2; ORFNames=M106.1;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF GLY-35 AND GLU-64.
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 [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, INTERACTION WITH SMC-4 AND DPY-27, SUBCELLULAR LOCATION, AND
RP DISRUPTION 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 [4]
RP FUNCTION, IDENTIFICATION IN A DOSAGE COMPENSATION COMPLEX AND IN A
RP CONDENSIN II COMPLEX, INTERACTION WITH DPY-27; SMC-4; DPY-28 AND HCP-6,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLU-64.
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 [5]
RP FUNCTION, IDENTIFICATION IN A DOSAGE COMPENSATION COMPLEX, INTERACTION WITH
RP DPY-26; DPY-27; DPY-28, AND SUBCELLULAR LOCATION.
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 [6]
RP FUNCTION, IDENTIFICATION IN A DOSAGE COMPENSATION COMPLEX AND IN A
RP CONDENSIN I COMPLEX, AND INTERACTION WITH 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 [7]
RP FUNCTION, IDENTIFICATION IN A CONDENSIN I COMPLEX; IN A CONDENSIN II
RP COMPLEX AND IN A DOSAGE COMPENSATION COMPLEX, INTERACTION WITH DPY-27;
RP SMC-4; KLE-2; DPY-26; CAPG-1 AND HCP-6, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLY-35.
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 [8]
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 [9]
RP INTERACTION WITH SMCL-1; DPY-27 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: Essential protein required for both chromosome condensation
CC and segregation and X-chromosome dosage compensation depending on its
CC binding partners (PubMed:9458050, PubMed:11914278, PubMed:19119011,
CC PubMed:18198337, PubMed:19781752). Central component of the condensin I
CC complex, a complex required for conversion of interphase chromatin into
CC mitotic-like condense chromosomes (PubMed:11914278, PubMed:18198337,
CC PubMed:19119011). The condensin complex introduces positive supercoils
CC into relaxed DNA in the presence of type I topoisomerases
CC (PubMed:11914278). Converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases (By similarity). Central
CC component of the condensin II complex, a complex that seems to play a
CC role in prophase chromosome condensation and organization
CC (PubMed:19119011, PubMed:15557118). Both the condensin complex I and II
CC play a role in meiotic and mitotic chromosome segregation
CC (PubMed:11914278, PubMed:19119011, PubMed:15557118). Plays a role in
CC robust cytokinesis upon the presence of chromatin obstructions
CC (PubMed:23684975). Also a member of the condensin I-like dosage
CC compensation complex that associates specifically with hermaphrodite X
CC chromosomes to reduce their gene transcription during interphase
CC (PubMed:9458050, PubMed:19119011, PubMed:18198337, PubMed:19781752).
CC {ECO:0000250|UniProtKB:P50533, ECO:0000269|PubMed:11914278,
CC ECO:0000269|PubMed:15557118, ECO:0000269|PubMed:18198337,
CC ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:19781752,
CC ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:9458050}.
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:11914278, PubMed:19119011, PubMed:19781752, PubMed:18198337).
CC Within the complex, interacts with smc-4, dpy-26, dpy-28 and capg-1
CC (PubMed:11914278, PubMed:15557118, PubMed:19781752, PubMed:19119011,
CC PubMed:28301465). Interaction with smc-4 is required for mitotic
CC chromosome localization (PubMed:11914278). Component of the condensin
CC II complex, which contains the mix-1/SMC2 and smc-4/SMC4 heterodimer,
CC and three non SMC subunits, capg-2, kle-2 and hcp-6 that probably
CC regulate the complex (PubMed:19119011, PubMed:15557118). Within the
CC complex, interacts with smc-4, capg-2, kle-2 and hcp-6
CC (PubMed:11914278, PubMed:15557118, PubMed:19119011, PubMed:28301465).
CC Also a component of the condensin-like dosage compensation complex,
CC which contains the mix-1/SMC2 and dpy-27/SMC4 heterodimer, and three
CC non SMC subunits that probably regulate the complex: dpy-26, capg-1 and
CC dpy-28 (PubMed:11914278, PubMed:19119011, PubMed:18198337,
CC PubMed:19781752, PubMed:15557118). Within the complex, interacts with
CC dpy-27, dpy-26, capg-1 and dpy-28 (PubMed:11914278, PubMed:15557118,
CC PubMed:18198337, PubMed:19781752, PubMed:19119011, PubMed:28301465).
CC Requires capg-1 for hermaphrodite X chromosome localization
CC (PubMed:19119011). Interacts with smcl-1 (PubMed:28301465).
CC {ECO:0000269|PubMed:11914278, ECO:0000269|PubMed:15557118,
CC ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:19119011,
CC ECO:0000269|PubMed:19781752, ECO:0000269|PubMed:28301465}.
CC -!- INTERACTION:
CC Q09591; P48996: dpy-27; NbExp=5; IntAct=EBI-1152136, EBI-1152153;
CC Q09591; Q20060: smc-4; NbExp=6; IntAct=EBI-1152136, EBI-1152127;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11914278,
CC ECO:0000269|PubMed:15557118, ECO:0000269|PubMed:18198337,
CC ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:9458050}. Chromosome
CC {ECO:0000269|PubMed:11914278, ECO:0000269|PubMed:15557118,
CC ECO:0000269|PubMed:18198337, ECO:0000269|PubMed:19119011,
CC ECO:0000269|PubMed:9458050}. Note=During mitosis and meiosis, localizes
CC to condensed chromosomes in both sexes (PubMed:11914278,
CC PubMed:19119011, PubMed:15557118). During meiotic prophase, surrounds
CC the chromosomes, localizes between homologs during meiotic metaphase I,
CC and localizes between sister chromatids during metaphase II
CC (PubMed:11914278). During mitotic metaphase, localizes at the poleward
CC face and to the core of the condensed chromosomes (PubMed:19119011,
CC PubMed:18198337, PubMed:15557118). Requires hcp-6 for the localization
CC to meiotic chromosomes (PubMed:15557118). After the 40-cell stage when
CC dosage compensation is initiated, specifically localizes to the
CC hermaphrodite X chromosomes in interphase (PubMed:9458050,
CC PubMed:11914278). {ECO:0000269|PubMed:11914278,
CC ECO:0000269|PubMed:15557118, ECO:0000269|PubMed:18198337,
CC ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:9458050}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos and in adult somatic and
CC germline tissues (at protein level). {ECO:0000269|PubMed:15557118}.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterodimerization with
CC SMC4, forming a V-shaped heterodimer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown disrupts mitotic prophase
CC chromosome condensation and chromosome segregation in anaphase leading
CC to aneuploidy (PubMed:11914278, PubMed:19119011). Results in cleavage
CC furrow regression and failed cytokinesis during the second embryonic
CC division (PubMed:23684975). {ECO:0000269|PubMed:11914278,
CC ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:23684975}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily. {ECO:0000305}.
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; U96387; AAC47834.1; -; mRNA.
DR EMBL; Z46935; CAA87054.1; -; Genomic_DNA.
DR PIR; T23744; T23744.
DR PIR; T23981; T23981.
DR RefSeq; NP_496331.1; NM_063930.6.
DR AlphaFoldDB; Q09591; -.
DR SMR; Q09591; -.
DR BioGRID; 39979; 14.
DR ComplexPortal; CPX-1271; Condensin I complex.
DR ComplexPortal; CPX-1272; Condensin II complex.
DR ComplexPortal; CPX-1273; Condensin I-like dosage compensation complex.
DR IntAct; Q09591; 6.
DR STRING; 6239.M106.1; -.
DR iPTMnet; Q09591; -.
DR EPD; Q09591; -.
DR PaxDb; Q09591; -.
DR EnsemblMetazoa; M106.1.1; M106.1.1; WBGene00003367.
DR GeneID; 174669; -.
DR KEGG; cel:CELE_M106.1; -.
DR UCSC; M106.1; c. elegans.
DR CTD; 174669; -.
DR WormBase; M106.1; CE18083; WBGene00003367; mix-1.
DR eggNOG; KOG0933; Eukaryota.
DR GeneTree; ENSGT00550000074857; -.
DR HOGENOM; CLU_001042_9_0_1; -.
DR InParanoid; Q09591; -.
DR OMA; HNKIAME; -.
DR OrthoDB; 119789at2759; -.
DR PhylomeDB; Q09591; -.
DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-CEL-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:Q09591; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003367; Expressed in embryo and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
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:0046536; C:dosage compensation complex; IPI:WormBase.
DR GO; GO:0000805; C:X chromosome; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0042464; P:dosage compensation by hypoactivation of X chromosome; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0045132; P:meiotic chromosome segregation; IC:ComplexPortal.
DR GO; GO:0007076; P:mitotic chromosome condensation; 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.
DR GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR CDD; cd03273; ABC_SMC2_euk; 1.
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; IPR027120; Smc2_ABC.
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..1244
FT /note="Mitotic chromosome and X-chromosome-associated
FT protein mix-1"
FT /id="PRO_0000118999"
FT DOMAIN 526..654
FT /note="SMC hinge"
FT REGION 337..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..355
FT /evidence="ECO:0000255"
FT COILED 415..472
FT /evidence="ECO:0000255"
FT COILED 701..946
FT /evidence="ECO:0000255"
FT COILED 975..1037
FT /evidence="ECO:0000255"
FT COMPBIAS 337..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT MUTAGEN 35
FT /note="G->S: In mn29; induces defects in dosage
FT compensation. Defects in mitotic chromosome segregation and
FT in germline formation."
FT /evidence="ECO:0000269|PubMed:19119011,
FT ECO:0000269|PubMed:9458050"
FT MUTAGEN 64
FT /note="E->K: In b285; induces defects in dosage
FT compensation. Defects in diakinesis bivalent formation.
FT Blocks precocious homolog and sister chromatid separation
FT in a RNAi-mediated rec-8 knockdown background."
FT /evidence="ECO:0000269|PubMed:15557118,
FT ECO:0000269|PubMed:9458050"
SQ SEQUENCE 1244 AA; 140342 MW; 255FD9C3D8C4AA49 CRC64;
MHIKSIHLDG FKSYQKHTDI LDFSPTFNAI TGYNGSGKSN ILDSICFIMG INKLDNIRAK
SMHELISHGG TKAIVQVRFD NTDKRCSPFG MEHLDEIVVQ RIITAQATGK GCATSYTLNG
HAATNGKMQD FFRGVGLNVN NPHFLIMQGR ITTVLNMKPE EILGMVEEAA GTKMYDQKKK
DAEKTMFLKD AKLKEVDRIF QSSIDPRMVK FREDRKNMVE VTRLKKLKEN FSRKYEAFQY
FQTCEAVKKS AKEIEDAKKG IEDLGEKFNQ LDLDLKNKED EKKKMEESRD DQHEEAALSA
AHLSKQSIML QKETVKNQLV ETINKLKKEG EQINKSLSKD REVLDAKRKE HEDSKAANSK
DIQSQSDDEA LVTKYRNDLE SLTRGTIAND KGEHVSIESE IQSCKSTASQ MSSGITAAKK
RGERLHNQIK HLEGEKATLS ARSKSDIGSA DNYQKEVDEI NKQLQLLGFN IDADTEKREH
AAKLHESITK LKDMDTRLLN SYKDGRYALN YQRPPLHIDK FDEKRDVFGY VAHLIKMKPG
CEQFAVAADI ALGGVLGNVV VSTQDIARIL IDGKAFTSRK TMIPVSENAR NASSYNTLPD
VKLRRAKEIA EKYNDTVTKM IDLIEYPDFI SNTILNAVGQ ILVVDSLDVA REIAYDEVAK
TRMITRRGDD VRTNGIMTGG YNDPGNKPAL IALEPMYARR PQIEAQQREL DALNRELQLT
EASSQKCRDL NNQLATAMRK LAQVKTNINN SEFGIVVRDL KVHSEEYEKN QAEIEATVKT
LKDVEDKIKT LESMKNKDKN SQEKRKKELT ALLQKAEQTV AQNKNRGEKA RREVMLLQAT
VEEMEKTIKK DEGIWEQKKK ECDELEEKLP NAIAALKDAE LEQKAAQAKL NDLKNNQRQI
STRLGKIAKE CDALIREKAK TKSKREEKEK ELTSLQQSEA SNRKEARSKL KKFEWLSDEE
AHFNKKGGLY DFEGYTVSKG KDEIKELTDK IETLERSCCI QNVSNLDTCE AKVLDIKNKR
ERITEDFNML KKTIATLDKK KVDELIRAHE SVNKDFGQIF NCLLPDAHAS LVPPEGKTVC
EGLEVKVSFG GVVKDSLHEL SGGQRSLVAL SLILAMLKFK PAPLYILDEV DAALDLSHTA
NIGMMIKTHF HHNQFIIVSL KQGMFSNADV LFQTRFADGH STCTRLNGGD IAVLCQDKVL
QAQALELTDA GKAKKDAAAK KGAQKNDKEP PKKKPIVVDD DDFE
