CND2_SCHPO
ID CND2_SCHPO Reviewed; 742 AA.
AC Q9Y7R3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Condensin complex subunit 2;
DE AltName: Full=Barren homolog;
DE AltName: Full=CAPH homolog;
DE AltName: Full=p105;
GN Name=cnd2; ORFNames=SPCC306.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 82-113; 123-138;
RP 536-553 AND 674-689, FUNCTION, AND IDENTIFICATION IN A CONDENSIN COMPLEX
RP WITH CUT3; CUT14; CND1 AND CND3.
RX PubMed=10485849; DOI=10.1101/gad.13.17.2271;
RA Sutani T., Yuasa T., Tomonaga T., Dohmae N., Takio K., Yanagida M.;
RT "Fission yeast condensin complex: essential roles of non-SMC subunits for
RT condensation and Cdc2 phosphorylation of Cut3/SMC4.";
RL Genes Dev. 13:2271-2283(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTANT CND2-1.
RX PubMed=12000964; DOI=10.1038/417197a;
RA Aono N., Sutani T., Tomonaga T., Mochida S., Yanagida M.;
RT "Cnd2 has dual roles in mitotic condensation and interphase.";
RL Nature 417:197-202(2002).
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 topoisomerases. The condensin complex probably
CC also plays a role during interphase in processes such as DNA repair.
CC {ECO:0000269|PubMed:10485849, ECO:0000269|PubMed:12000964}.
CC -!- SUBUNIT: Component of the condensin complex, which contains the
CC cut14/smc2 and cut3/smc2 heterodimer, and three non SMC subunits that
CC probably regulate the complex: cnd1, cnd2 and cnd3.
CC {ECO:0000269|PubMed:10485849}.
CC -!- INTERACTION:
CC Q9Y7R3; Q10429: cnd3; NbExp=2; IntAct=EBI-1149594, EBI-1149700;
CC Q9Y7R3; P41004: cut3; NbExp=3; IntAct=EBI-1149594, EBI-1149474;
CC Q9Y7R3; P04910: hta2; NbExp=2; IntAct=EBI-1149594, EBI-15929287;
CC Q9Y7R3; P48003: pht1; NbExp=2; IntAct=EBI-1149594, EBI-15929575;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12000964}. Cytoplasm
CC {ECO:0000269|PubMed:12000964}. Chromosome
CC {ECO:0000269|PubMed:12000964}. Note=In interphase cells, the majority
CC of the condensin complex is found in the cytoplasm, while a minority of
CC the complex is associated with chromatin. A subpopulation of the
CC complex however remains associated with chromosome foci in interphase
CC cells. During mitosis, most of the condensin complex is associated with
CC the chromatin. At the onset of prophase, condensin associates with
CC chromosome arms and to chromosome condensation. Dissociation from
CC chromosomes is observed in late telophase.
CC -!- SIMILARITY: Belongs to the CND2 (condensin subunit 2) family.
CC {ECO:0000305}.
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DR EMBL; AB030213; BAA82625.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB41651.1; -; Genomic_DNA.
DR PIR; T43520; T43520.
DR RefSeq; NP_587811.1; NM_001022804.2.
DR PDB; 5OQR; X-ray; 2.61 A; C/D=416-544.
DR PDBsum; 5OQR; -.
DR AlphaFoldDB; Q9Y7R3; -.
DR SMR; Q9Y7R3; -.
DR BioGRID; 275327; 29.
DR DIP; DIP-35026N; -.
DR IntAct; Q9Y7R3; 7.
DR STRING; 4896.SPCC306.03c.1; -.
DR iPTMnet; Q9Y7R3; -.
DR MaxQB; Q9Y7R3; -.
DR PaxDb; Q9Y7R3; -.
DR PRIDE; Q9Y7R3; -.
DR EnsemblFungi; SPCC306.03c.1; SPCC306.03c.1:pep; SPCC306.03c.
DR GeneID; 2538744; -.
DR KEGG; spo:SPCC306.03c; -.
DR PomBase; SPCC306.03c; cnd2.
DR VEuPathDB; FungiDB:SPCC306.03c; -.
DR eggNOG; KOG2328; Eukaryota.
DR HOGENOM; CLU_010510_0_1_1; -.
DR InParanoid; Q9Y7R3; -.
DR OMA; KPKAKMG; -.
DR PhylomeDB; Q9Y7R3; -.
DR Reactome; R-SPO-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:Q9Y7R3; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0061638; C:CENP-A containing chromatin; IDA:PomBase.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000796; C:condensin complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IGI:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:PomBase.
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 3D-structure; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW Direct protein sequencing; DNA condensation; DNA damage; DNA repair;
KW Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..742
FT /note="Condensin complex subunit 2"
FT /id="PRO_0000095044"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 114
FT /note="A->T: In cnd2-1; defects in DNA repair and cell
FT cycle."
FT HELIX 421..425
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 491..495
FT /evidence="ECO:0007829|PDB:5OQR"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:5OQR"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:5OQR"
SQ SEQUENCE 742 AA; 83254 MW; 57A7F490AC17DBFE CRC64;
MKRASLGGHA PVSLPSLNDD ALEKKRAKEN SRKQRELRRS SALHSITPRR ESLNNSSPFN
SSHQVPVLSN FEEWIKLATD NKINSTNTWN FALIDYFHDM SLLRDGEDIN FQKASCTLDG
CVKIYTSRID SVATETGKLL SGLANDSKVL QQTEEGEDAE NDDEDLQKKK ERKRAQRSVK
TLVKDFESIR AKKFELECSF DPLFKKMCAD FDEDGAKGLL MNHLCVDQHG RIVFDSSDTV
IKDLENKDVE AESQEAVVAA PIESHDTEMT NVHDNISRET LNGIYKCYFT DIDQLTICPS
LQGFEFDSKG NLDVSLLKSL SDEVNMITTT SLVDNTMEKT DADAASLSSD SDGEEGHIVH
ALEEMAYDEE NPYVDVVPKA MDESENPDFG VDTEVNMADG STMNENYSII STAAANGVYE
YFDKSMKKNW AGPEHWRIQA LRKNINNAST VFNSSNTAES SDNVSRSLSS TERKKRRELD
NAIDFLQEVD VEALFTPATS SLKLPKSHWK RHNRCLLPDD YQYDSKRLLQ LFLKPKMSVL
PNADGEGQLQ LNKALDDEND LDGIQPHGFD SDGSDNVDEG IPPYGFGDSD SPKQTPLLTP
PSSSGFGDNL LLTARLAKPD MLNYAKRAKK VDVRVLKEKL WKCLDLENTI KENSINSHIE
GSEMESEETN MPVKSFFSTV NQLEETYEKK ELKDISTSFA FICVLHLANE HNLELTSNED
FSDVFIRPGP NLTTLEALEN DV
