CND2_XENLA
ID CND2_XENLA Reviewed; 699 AA.
AC O13067;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Condensin complex subunit 2;
DE AltName: Full=Barren homolog;
DE AltName: Full=Chromosome assembly protein xCAP-H;
DE AltName: Full=Chromosome-associated protein H;
DE AltName: Full=Non-SMC condensin I complex subunit H;
GN Name=ncaph; Synonyms=brrn1, caph;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 117-132; 135-153; 233-250
RP AND 632-652, AND IDENTIFICATION IN A CONDENSIN COMPLEX WITH XCAP-C; XCAP-E;
RP XCAP-D2 AND XCAP-G.
RX PubMed=9160743; DOI=10.1016/s0092-8674(00)80233-0;
RA Hirano T., Kobayashi R., Hirano M.;
RT "Condensins, chromosome condensation protein complexes containing XCAP-C,
RT XCAP-E and a Xenopus homolog of the Drosophila Barren protein.";
RL Cell 89:511-521(1997).
RN [2]
RP FUNCTION OF THE CONDENSIN COMPLEX, AND PHOSPHORYLATION BY CDK1.
RX PubMed=9774278; DOI=10.1126/science.282.5388.487;
RA Kimura K., Hirano M., Kobayashi R., Hirano T.;
RT "Phosphorylation and activation of 13S condensin by Cdc2 in vitro.";
RL Science 282:487-490(1998).
RN [3]
RP FUNCTION OF THE CONDENSIN COMPLEX.
RX PubMed=10428035; DOI=10.1016/s0092-8674(00)81018-1;
RA Kimura K., Rybenkov V.V., Crisona N.J., Hirano T., Cozzarelli N.R.;
RT "13S condensin actively reconfigures DNA by introducing global positive
RT writhe: implications for chromosome condensation.";
RL Cell 98:239-248(1999).
CC -!- FUNCTION: Regulatory subunit of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerase. {ECO:0000269|PubMed:10428035,
CC ECO:0000269|PubMed:9774278}.
CC -!- SUBUNIT: Component of the condensin complex, which contains the XCAP-
CC E/SMC2 and XCAP-C/SMC4 heterodimer, and three non SMC subunits that
CC probably regulate the complex: XCAP-H/NCAPH, XCAP-D2/NCAPD2 and XCAP-
CC G/NCAPG. {ECO:0000269|PubMed:9160743}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the
CC condensin complex is found in the cytoplasm, while a minority of the
CC complex is associated with chromatin. A subpopulation of the complex
CC however remains associated with chromosome foci in interphase cells.
CC During mitosis, most of the condensin complex is associated with the
CC chromatin. At the onset of prophase, the regulatory subunits of the
CC complex are phosphorylated by CDK1, leading to condensin's association
CC with chromosome arms and to chromosome condensation. Dissociation from
CC chromosomes is observed in late telophase (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that of
CC XCAP-D2 and XCAP-G subunits, activates the condensin complex and is
CC required for chromosome condensation. {ECO:0000269|PubMed:9774278}.
CC -!- SIMILARITY: Belongs to the CND2 (condensin subunit 2) family.
CC {ECO:0000305}.
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DR EMBL; U90125; AAC60203.1; -; mRNA.
DR RefSeq; NP_001081818.1; NM_001088349.1.
DR AlphaFoldDB; O13067; -.
DR BioGRID; 99404; 2.
DR DNASU; 398069; -.
DR GeneID; 398069; -.
DR KEGG; xla:398069; -.
DR CTD; 398069; -.
DR Xenbase; XB-GENE-5738491; ncaph.S.
DR OrthoDB; 702078at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR GO; GO:0000796; C:condensin complex; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IEA:InterPro.
DR InterPro; IPR022816; Condensin_barren_su2.
DR PANTHER; PTHR13108; PTHR13108; 1.
DR Pfam; PF05786; Cnd2; 1.
DR PIRSF; PIRSF017126; Condensin_H; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Cytoplasm;
KW Direct protein sequencing; DNA condensation; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..699
FT /note="Condensin complex subunit 2"
FT /id="PRO_0000095040"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 233
FT /note="K -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 77778 MW; 71B7B671A4F415A5 CRC64;
MSTSTPQSGG RRKPETPDSA FLSPATRPQP ISAAATPTLL NFTSNDDERE RKLRRMSRVI
DLQLSNANSP ATAISPAQSR GADTPTSLLP KLNNTQISDH YSTCIKLSQE NKITTKNAFG
LHLIDYMGDI LKHKDSELTN FKVAAGTLDA SAKIYAVRVD AVHADVYKVL GGLGKESQAT
EDTENQETDT GPQDGRKNPK RRKCSYKTIE RNLNSINRSE TERKSEIDPL FQKAAASFDE
FSTAGVFLST LKCHSYHSEL HFDADVKPLS TAEETEPPSP GSMDSTELKS LFLQCVEKRP
LCPSLSGFRF MQWNSDAQNE NLSLLMDKFK KSDHVFDINA EVEDDFVESE APVADEFDAD
VCEGMDAGDI GEFAEHREAC RLERKGAQLT QIGNGDIGTM CLQLSSCPGE YSYFSPRTMS
MWAGPEHWRF RPRQKASTDS DQQRVKKAKK VFELNFEDDI DFEVHFRKTR AATTLTKSTL
ESQNKKSTTL PADFHYDPDN IARMSLRPKD RIRKTTVQES VSEPEDDIGD YDYNNPNDTS
NFCPALQAAD SDDDDGAFLG PESNSAGFSA ENQMNITSYG ESNLVAGQKV NKIEIQYAKT
AKKMDMKRLK SSMWSLLANC PESQEEMPSS KEEIDAALIT DEQVFSSVTH GLQKRLPPVM
AQNLSVPLAF ACLLHLANEK NLKLQGMDDL SDVMIMQDD