CND3_XENLA
ID CND3_XENLA Reviewed; 1034 AA.
AC Q9YHB5; Q8AVZ4;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Condensin complex subunit 3;
DE AltName: Full=Chromosome assembly protein xCAP-G;
DE AltName: Full=Chromosome-associated protein G;
DE AltName: Full=Condensin subunit CAP-G;
DE AltName: Full=Non-SMC condensin I complex subunit G;
GN Name=ncapg; Synonyms=capg;
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].
RA Hirano T., Hirano M.;
RT "XCAP-G, the 130 kDa subunit of the Xenopus 13S condensin complex.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH XCAP-C; XCAP-E; XCAP-D2 AND
RP 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 [4]
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 [5]
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-H subunits, activates the condensin complex and is
CC required for chromosome condensation. {ECO:0000269|PubMed:9774278}.
CC -!- SIMILARITY: Belongs to the CND3 (condensin subunit 3) family.
CC {ECO:0000305}.
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DR EMBL; AF111423; AAD09819.1; -; mRNA.
DR EMBL; BC041184; AAH41184.1; -; mRNA.
DR PIR; T17458; T17458.
DR RefSeq; NP_001081856.1; NM_001088387.1.
DR AlphaFoldDB; Q9YHB5; -.
DR SMR; Q9YHB5; -.
DR BioGRID; 99423; 4.
DR DNASU; 398088; -.
DR GeneID; 398088; -.
DR KEGG; xla:398088; -.
DR CTD; 398088; -.
DR Xenbase; XB-GENE-5783887; ncapg.L.
DR OrthoDB; 108186at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
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 Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027165; CND3.
DR InterPro; IPR025977; Cnd3_C.
DR PANTHER; PTHR14418; PTHR14418; 1.
DR Pfam; PF12719; Cnd3; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Cytoplasm; DNA condensation;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1034
FT /note="Condensin complex subunit 3"
FT /id="PRO_0000095042"
FT REPEAT 95..132
FT /note="HEAT 1"
FT REPEAT 139..176
FT /note="HEAT 2"
FT REPEAT 178..213
FT /note="HEAT 3"
FT REPEAT 242..279
FT /note="HEAT 4"
FT REPEAT 281..317
FT /note="HEAT 5"
FT REPEAT 439..476
FT /note="HEAT 6"
FT REPEAT 618..655
FT /note="HEAT 7"
FT REPEAT 703..740
FT /note="HEAT 8"
FT REPEAT 785..823
FT /note="HEAT 9"
FT REPEAT 878..915
FT /note="HEAT 10"
FT REGION 663..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..979
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 86
FT /note="N -> D (in Ref. 2; AAH41184)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="R -> S (in Ref. 2; AAH41184)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="G -> D (in Ref. 2; AAH41184)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="V -> A (in Ref. 2; AAH41184)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="T -> K (in Ref. 2; AAH41184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1034 AA; 115815 MW; 251FAB52FEFC45D0 CRC64;
MVKEGKAMEI KEAFDLSQKA HQNHAKLVSS LRAAYNKTED KSIFLEEFIH FLKFPLIVYR
REPAVERVMD FVAKFVTSFH NSGGENEEEA DEENSPVNCL FNFLLQSHGA SSMAVRFRVC
QLINKLLVNL PENAQIDDDL FDKIHDAMLI RLKDRVPNVR IQAVLALARL QDPSDPDCPV
SNAYVHLLEN DSNPEVRRAV LTCIAPSAKS LPKIVGRTMD VKEPVRKLAY QVLSEKVHIR
ALTIAQRVKL LQQGLNDRSA AVKDVIQKKL IQAWLQYSEG DVLDLLHRLD VENSPEVSLS
ALNALFSVSP VGELVQNCKN LDERKLIPVE TLTPENVLYW RALCEHLKSK GDEGEAALEN
ILPEPAVYAR YLSSYLQTLP VLSEDQRADM TKIEDLMTKE FIGQQLILTI GCLDTSEEGG
RKRLLAVLQE ILVMQNTPTS LISSLAELLL FVLKDDDKRI QTVAEIISEL REPIVTVDNP
KDAAQSRKLQ LKLADVKVQL IEAKQALEDS LTNEDYSRAS ELKEKVKELE SLKTQLIKEA
EEPEMKEIRV EKNDPETLLK CLIMCNELLK HLSLSKGLGG TLNEICESLI LPGITNVHPS
VRNMAVLCIG CCALQNKDFA RQHLPLLLQI LQLDEVKVKN SALNAVFDML LLFGMDILKS
KPTNPDDSQC KAQENADEDI SEQEKPGSVD ENLTNEEVQE ETATVNGILH LFSGFLDSEI
AEIRTETAEG LVKLMFSGRL ISAKLLSRLI LLWYNPVTEE DTKLRHCLGV FFPIFAYSCR
SNQECFAEAF LPTLQTLFNA PASSPLADVD VANVAELLVD LTRPSGLNPQ NKQSQDYQAA
MVHDGLAIKI CNEILKDPTA PDVRIYAKAL CSLELSRENS TDLLPLLDCA VEDVTDKVCE
RAIEKVRSQL RSGREEHRVS KETEPQVSKE TEDRTNLQEN EEGKQKDEAN CDENTDTVKE
KAARGKATKG RRKGPAAAAT RRKASKAEEA EAEMERQEES QCVPVNTRPS RRAKTAALEK
TKKNLSKLLN EEAN
