CIN4_CAEEL
ID CIN4_CAEEL Reviewed; 842 AA.
AC G5ECQ8;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=DNA topoisomerase-like protein cin-4 {ECO:0000305};
GN Name=cin-4 {ECO:0000312|WormBase:ZK1127.7};
GN ORFNames=ZK1127.7 {ECO:0000312|WormBase:ZK1127.7};
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:0000312|EMBL:ABW69249.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF GLU-304.
RX PubMed=18202360; DOI=10.1534/genetics.107.075275;
RA Stanvitch G., Moore L.L.;
RT "cin-4, a gene with homology to topoisomerase II, is required for
RT centromere resolution by cohesin removal from sister kinetochores during
RT mitosis.";
RL Genetics 178:83-97(2008).
RN [3] {ECO:0000305}
RP MUTAGENESIS OF GLU-304.
RX PubMed=27707787; DOI=10.1534/genetics.116.195099;
RA Jaramillo-Lambert A., Fabritius A.S., Hansen T.J., Smith H.E., Golden A.;
RT "The identification of a novel mutant allele of topoisomerase II in
RT Caenorhabditis elegans reveals a unique role in chromosome segregation
RT during spermatogenesis.";
RL Genetics 204:1407-1422(2016).
CC -!- FUNCTION: Plays a role in the removal of cohesin from kinetochores on
CC mitotic chromosomes and is required for centromere resolution.
CC {ECO:0000269|PubMed:18202360}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown leads to impaired removal
CC of the cohesin component scc-1 from kinetochores on mitotic metaphase
CC chromosomes. {ECO:0000269|PubMed:18202360}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000255|RuleBase:RU362094}.
CC -!- CAUTION: Lacks the conserved ATP binding sites, the conserved active
CC site tyrosine at position 404, the conserved isoleucine at position 455
CC important for DNA bending, and the conserved magnesium binding site at
CC position 143, and therefore probably lacks topoisomerase activity.
CC {ECO:0000305}.
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DR EMBL; EU191083; ABW69249.1; -; mRNA.
DR EMBL; BX284602; CCD73727.1; -; Genomic_DNA.
DR RefSeq; NP_495440.4; NM_063039.5.
DR AlphaFoldDB; G5ECQ8; -.
DR SMR; G5ECQ8; -.
DR STRING; 6239.ZK1127.7; -.
DR EPD; G5ECQ8; -.
DR PaxDb; G5ECQ8; -.
DR PeptideAtlas; G5ECQ8; -.
DR EnsemblMetazoa; ZK1127.7.1; ZK1127.7.1; WBGene00022854.
DR GeneID; 191525; -.
DR KEGG; cel:CELE_ZK1127.7; -.
DR CTD; 191525; -.
DR WormBase; ZK1127.7; CE42594; WBGene00022854; cin-4.
DR eggNOG; KOG0355; Eukaryota.
DR GeneTree; ENSGT00940000168342; -.
DR HOGENOM; CLU_001935_3_0_1; -.
DR InParanoid; G5ECQ8; -.
DR OMA; MAGNTEG; -.
DR OrthoDB; 117851at2759; -.
DR PhylomeDB; G5ECQ8; -.
DR Reactome; R-CEL-4615885; SUMOylation of DNA replication proteins.
DR PRO; PR:G5ECQ8; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00022854; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
DR CDD; cd00187; TOP4c; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; DNA-binding; Mitosis; Reference proteome.
FT CHAIN 1..842
FT /note="DNA topoisomerase-like protein cin-4"
FT /id="PRO_0000442730"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 304
FT /note="E->G: In av59; no effect on viability observed at
FT 15, 24 and 25 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:27707787"
FT MUTAGEN 304
FT /note="E->G: In mr127; temperature sensitive mutant. At the
FT nonpermissive temperature, failure in proper hcp-3
FT localization on mitotic chromosomes indicating unresolved
FT kinetochores, aberrant localization of the cohesin
FT component scc-1 to mitotic chromosomes and centrosomes,
FT defects in centromere resolution and in proper chromosome
FT segregation during anaphase."
FT /evidence="ECO:0000269|PubMed:18202360"
SQ SEQUENCE 842 AA; 96658 MW; 3BE8B7EFE5125578 CRC64;
MSEEDRNVFT SIDKKGGGSK QMDDLNQKCP KRKTSKLKGI PKLEDANDAG TKNSQQCTLI
LTEGDSAKTL AVSGLSVVGR DKYGVFPFRR KLLNVCDLNV NQIADSAEVN AIIKILGLQY
TKKYETEDDF KTLRYGKLLI MANHDSDGSQ FKGLLLNFFH RFWPALFKRD FVEDFITPIA
KATEGKEEVS FYSLPEYSEW RMNTDNWKSY TIKYYNGLGT LTSKEAKKCF SDMVRHRIRF
KYNGADDDKA VNMAFSKKKI EARTDYLMKL MQDKNQRKQQ GLAEECLYNK ETRFVTLKDF
FNYEIVCSWN LHSIPCLVDG LKPGQRKVLF ACFKRANKRE VKVAQLAGAV AEISAYHHGE
QSLMGTIVNL AQDYVGSHNI NLLLPIGQFG TRLQGGKDSA SARSIFAQLS QVTRTLFPAH
DDNVLRFLYE ENQRIEPEWY CPIIPMVLVN GAQGTGTGWS TNIPNYNPRE LVKNIKRLIA
GEPQKALAPW YKNFRGKIIQ IDPSRFACYG EVSVLDDNTI EITELPIKQW TQDYKEKVLE
GLMESSDKKS PVIVDYKEYH TDTTVKFVVK LSPGKLRELE RGQDLHQVFK LQAVINTTCM
VLFDAAGWLR TYTSPEAITQ EFYDSRQEKY VQRKEYLLGV LQAQSKRLTN QARFILATIN
NKIVLENKKK TAIVDVLIKM KFDADPVKKW KEDQKLKELR ESGEIELDED DLAAVAVEEG
EDISSAAKAV ETKLSDYDYL VGLALIKLSE EEKNKLIKES EEKMAEVRVL EKKTWQDLWI
TDLDNFMSEL TSRRLARKLS LRRTATRWYA MICQRRVTWS SMKESISIRT MTVWSVRMSS
RS