CND1_SCHPO
ID CND1_SCHPO Reviewed; 1158 AA.
AC O94679;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Condensin complex subunit 1;
DE AltName: Full=XCAP-D2 homolog;
DE AltName: Full=p128;
GN Name=cnd1; ORFNames=SPBC776.13;
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 518-536; 658-667 AND
RP 1126-1138, AND IDENTIFICATION IN A CONDENSIN COMPLEX WITH CUT3; CUT14; CND2
RP 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).
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.
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 -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In
CC interphase cells, the majority of the condensin complex is found in the
CC cytoplasm, while a minority of the complex is associated with
CC chromatin. A subpopulation of the complex however remains associated
CC with chromosome foci in interphase cells. During mitosis, most of the
CC condensin complex is associated with the chromatin. At the onset of
CC prophase, condensin associates with chromosome arms and to chromosome
CC condensation. Dissociation from chromosomes is observed in late
CC telophase.
CC -!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family.
CC {ECO:0000305}.
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DR EMBL; AB030212; BAA82624.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22886.1; -; Genomic_DNA.
DR PIR; T43519; T43519.
DR RefSeq; NP_596329.1; NM_001022250.2.
DR AlphaFoldDB; O94679; -.
DR SMR; O94679; -.
DR BioGRID; 277715; 11.
DR DIP; DIP-59184N; -.
DR IntAct; O94679; 2.
DR STRING; 4896.SPBC776.13.1; -.
DR iPTMnet; O94679; -.
DR MaxQB; O94679; -.
DR PaxDb; O94679; -.
DR EnsemblFungi; SPBC776.13.1; SPBC776.13.1:pep; SPBC776.13.
DR GeneID; 2541201; -.
DR KEGG; spo:SPBC776.13; -.
DR PomBase; SPBC776.13; cnd1.
DR VEuPathDB; FungiDB:SPBC776.13; -.
DR eggNOG; KOG0414; Eukaryota.
DR HOGENOM; CLU_001867_1_0_1; -.
DR InParanoid; O94679; -.
DR OMA; RNCVLQI; -.
DR PhylomeDB; O94679; -.
DR Reactome; R-SPO-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:O94679; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IBA:GO_Central.
DR GO; GO:0000796; C:condensin complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0000791; C:euchromatin; IDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010032; P:meiotic chromosome condensation; IBA:GO_Central.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:PomBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026971; CND1/NCAPD3.
DR InterPro; IPR032682; Cnd1_C.
DR InterPro; IPR007673; Condensin_cplx_su1.
DR InterPro; IPR024324; Condensin_cplx_su1_N.
DR PANTHER; PTHR14222; PTHR14222; 1.
DR PANTHER; PTHR14222:SF2; PTHR14222:SF2; 1.
DR Pfam; PF12717; Cnd1; 1.
DR Pfam; PF12922; Cnd1_N; 1.
DR PIRSF; PIRSF017127; Condensin_D2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Cytoplasm;
KW Direct protein sequencing; DNA condensation; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..1158
FT /note="Condensin complex subunit 1"
FT /id="PRO_0000095043"
FT REGION 800..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..825
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1158 AA; 131324 MW; 37A7A2206830DF3D CRC64;
MSLDLLSRLK KYIHDEENSD LDSIYAECEN AGLTAVVNDV IDTLLLGTSS CFDEDCLEKL
FAICSHFADL SSSVRNKVYD LLTSNISSES AILEDMISAN ATDFTVPQTN LETTGIAFQL
TVNSLSSSNQ LSVIRSSTNT VKGRKKNPTT NSNWNGISHV NALLDAIITL FQKKLSRVWT
TSSERDMFLS LFLKPIYTLM ESEINIKNAS FRSRLFNIIG LAVQFHNHTT AAETNIIQNL
QYFEHLSEYA ADLVHIVTVQ FNSVTLAEGI IRTLCSLEFN DNDVKGPKQV ALFLVRLSSL
IPNLCLKQLT QLVKLLDSES YTLRCAIIEV LANVVIDQIH DEAQNEMSES VPATVQSLMD
LLSERLLDIS PYCRTKVLHV FIKIFDLPIK YPRKRQEIAE LVIRCLQDRS SHVRRNAIKL
FSKLLTTHPF SVMHNGLLTR NIWEKGLSII EEQLNSLQPK QQEKVVDSEL EVDENLLEDA
TMIQDDESHE GESHLENSLS EYVDSVPAEE IVKVNLTKRF YLEALQYIDI VEAGAKIISQ
LLFAKNKSEV IESMDFFVFC NSFGISSSKL YIKKMIHLIW VKGTSDEGNN IQNHVLSCYK
TLFFEPPPNS GTNEAANYIA RNLISLTYDA SLAELTSLEQ MLCILMKDGY FSHLVITKLW
QVYSYQKKDI SRTQRRGSII VIGMLALGNT DVVMQGLDHL IQIGLGPPGL EDLVLARYTC
IAIKRIGKDA SGSSNINFPN SHTLCQKLCM LLLRPSFSEE WFGLEEQAIE AIYAVAKHPD
ELCTNIILLL TKQLFKPSNH ENTTSNDDHA MDEDLDDSPE EETLKDEEEI GIRLAHLIFL
VGHVAIKQLV YIEYCEAEFK RRKADAERLA VQNSNNPING QETSEYDLIT GTSEDDFSEA
MTFIRERELL YGENSLLSRF APLVVELCSN HKSHNNQSLL LAASLTLSKF MCLSNNFCME
HLPLLITILE KCDNPIIRNN LVIGLADLTV CFNHFIDEIS EYLYRRLMDE ESSVKKTCFM
TLAFLILAGQ IKVKGQLGIM ARSLEDEDAR ISDLARMFFT DFAAKDNSVY NNFIDIFSVL
SRSAEEQDED DAKFKRIIRF LTSFIEKERH TKQLAERLAA RLDRCKTQRQ WDHVVYALSL
LPHKADNIQK LIDDGYHE
