ID A0A6J2NC16_9CHIR Unreviewed; 1405 AA.
AC A0A6J2NC16;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 08-OCT-2025, entry version 22.
DE RecName: Full=Condensin complex subunit 1 {ECO:0000256|ARBA:ARBA00016064, ECO:0000256|PIRNR:PIRNR017127};
GN Name=NCAPD2 {ECO:0000313|RefSeq:XP_028387505.1,
GN ECO:0000313|RefSeq:XP_035873209.1, ECO:0000313|RefSeq:XP_035873210.1,
GN ECO:0000313|RefSeq:XP_035873211.1};
OS Phyllostomus discolor (pale spear-nosed bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Phyllostomidae;
OC Phyllostominae; Phyllostomus.
OX NCBI_TaxID=89673 {ECO:0000313|Proteomes:UP000504628, ECO:0000313|RefSeq:XP_028387505.1};
RN [1] {ECO:0000313|RefSeq:XP_028387505.1, ECO:0000313|RefSeq:XP_035873209.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028387505.1,
RC ECO:0000313|RefSeq:XP_035873209.1};
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
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. May target the condensin
CC complex to DNA via its C-terminal domain. May promote the resolution of
CC double-strand DNA catenanes (intertwines) between sister chromatids.
CC Condensin-mediated compaction likely increases tension in catenated
CC sister chromatids, providing directionality for type II topoisomerase-
CC mediated strand exchanges toward chromatid decatenation. Required for
CC decatenation of non-centromeric ultrafine DNA bridges during anaphase.
CC Early in neurogenesis, may play an essential role to ensure accurate
CC mitotic chromosome condensation in neuron stem cells, ultimately
CC affecting neuron pool and cortex size. {ECO:0000256|ARBA:ARBA00053151}.
CC -!- SUBUNIT: Component of the condensin complex, which contains the SMC2
CC and SMC4 heterodimer, and three non SMC subunits that probably regulate
CC the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and NCAPG. Interacts with
CC histones H1 and H3. {ECO:0000256|ARBA:ARBA00064826}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family.
CC {ECO:0000256|ARBA:ARBA00009606, ECO:0000256|PIRNR:PIRNR017127}.
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DR RefSeq; XP_028387505.1; XM_028531704.2.
DR RefSeq; XP_035873209.1; XM_036017316.1.
DR RefSeq; XP_035873210.1; XM_036017317.1.
DR RefSeq; XP_035873211.1; XM_036017318.1.
DR GeneID; 114512711; -.
DR KEGG; pdic:114512711; -.
DR CTD; 9918; -.
DR OrthoDB; 436262at2759; -.
DR Proteomes; UP000504628; Chromosome 2.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:TreeGrafter.
DR GO; GO:0000796; C:condensin complex; IEA:TreeGrafter.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042393; F:histone binding; IEA:TreeGrafter.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010032; P:meiotic chromosome condensation; IEA:TreeGrafter.
DR GO; GO:0007076; P:mitotic chromosome condensation; IEA:InterPro.
DR FunFam; 1.25.10.10:FF:000695; Condensin complex subunit 1; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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; CONDENSIN; 1.
DR PANTHER; PTHR14222:SF2; CONDENSIN COMPLEX SUBUNIT 1; 1.
DR Pfam; PF12717; Cnd1; 1.
DR Pfam; PF12922; Cnd1_N; 1.
DR PIRSF; PIRSF017127; Condensin_D2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|PIRNR:PIRNR017127};
KW Cell division {ECO:0000256|ARBA:ARBA00022618,
KW ECO:0000256|PIRNR:PIRNR017127}; Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA condensation {ECO:0000256|ARBA:ARBA00023067,
KW ECO:0000256|PIRNR:PIRNR017127};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|PIRNR:PIRNR017127};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000504628}.
FT DOMAIN 77..240
FT /note="Condensin complex subunit 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12922"
FT DOMAIN 1068..1229
FT /note="Condensin complex subunit 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12717"
FT REGION 569..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1386
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1405 AA; 157218 MW; 9EB7CFD1530CC310 CRC64;
MSSQLYEFHL PLAPEELLKS GGVNQYVVQE VLSIRNLPSQ LKAFQAAFRA KGPLAMLEHF
DTIYSILHHF RSIDPGLKED ALEFLIKVVS RHAQELPAIL DDAASSVPDR CAHLNALKMN
CYALVRLLES FETMTGQTGL MDLDLAGKGK KARAKSAHGF EWEENRQPIL QLLTQLLQLD
IRHLWNHSII EEEFVSLVTG CCYRLLENPT ISHQKNRPTR EAITHLLGVA LTHYNHMLSA
TVKIIQMLQH FEHLAPVLVA AVSLWATDYG MKSIVGEIVR EIGQKCPLEL SRDTSGAKGF
AAFLTELAER IPDILMSSMC ILVDHLDGES YMMRNAVLAA MAEMVLQVLN GDQLEEAARD
TRDQFLDTLQ AHGHDVNSFV RSRVLQLFTR IVQQKALPLT RFQAVVALAV GRLADKSVLV
CKNAIQLLAS FLANNPFSCK LSDTDFAGLL QKETQKLQEM RAERQSAAAS AVLDPEEEWE
AMLPELKSTL QQLLKLPPEE EIPEEIAATE TTEAVKGRIR QLLAKANYKQ AIILTREALD
HFQQSEPFSQ TDPDEAEETR FLNLLGTIFK SPRGPTQEKN PQGSAENVGP GQTDCRDKPS
VPQPEQSGGK DALVKQEMLV QYLQDAYSFS LKITEAIGII SKMMYENTTT VVQEVIEFFV
MAFQFGVPQA LLGVRRMLPL IWSKEHGVRE AVLNAYRQLY LNPKGDSARA KAHALIQNLS
LLLVDASVGT IQCLQEILCE FVQKDELKPA VTQLLWERAT EKVPCSPLER CSSVMLLGMM
AGGKPEIVGS NLDTLVSIGL DEKFPQDYRL AQQVCHAIAN LSDRRKPSLG KRHPPFRLPQ
GHRLFERLQE MVTEGFVHPD PLWIPFKEVA VTLIYQLAEG PEVICAQMLQ GCAKQALEKI
VEKSTPQGDP KETPVLSTFL LMNLLSLAGD VALQQLVHLE QAVSGELCRR RVLREEQENK
TKEPKEKNTS TEATMEEEMG LVGATADDTE AELIRGICEV ELLGGEQILA AFVPLLLKVC
NNPGLYSNPE LCAAAALTLG KFCMISATFC DSQLRLLFTM LEKSSLPILR SNIMIVIGDL
AIRFPNLVDP WTPHLYARLR DPAQQVRKTA GLVMTHLILK DMVKVKGQVS EMAVLLIDPV
PQIAALAKTF FNELSHKGNA IYNLLPDIIS RLSDPEGGVE EQPFHVIMKQ LLSYITKDKQ
TESLVEKLCQ RFRTARTERQ HRDLAYCMSQ LPLTERGLRK MLDNFECFGD KLSDESIFDA
FLSVVGKLRR GAKPEGKALI DEFEQKLRAC HTRGLDAIEE LELGQGDSLK TPSARKQSSV
SRHQHVASAA SDSDFVTPEP RRTARRHPTT QRHPTTQRLV KKKKPQIVFS SDESSEEELS
AEMTEDETPK KITPIRRAST RRHRS
//
