CND_CAEEL
ID CND_CAEEL Reviewed; 1758 AA.
AC Q95Y84; Q9N583;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Condensin-2 complex subunit hcp-6 {ECO:0000305};
DE AltName: Full=Holocentric chromosome-binding protein hcp-6 {ECO:0000312|WormBase:Y110A7A.1b};
DE AltName: Full=Holocentric protein 6 {ECO:0000303|PubMed:12080088};
GN Name=hcp-6 {ECO:0000303|PubMed:12080088, ECO:0000312|WormBase:Y110A7A.1b};
GN ORFNames=Y110A7A.1 {ECO:0000312|WormBase:Y110A7A.1b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLY-1024.
RX PubMed=12080088; DOI=10.1101/gad.989102;
RA Stear J.H., Roth M.B.;
RT "Characterization of HCP-6, a C. elegans protein required to prevent
RT chromosome twisting and merotelic attachment.";
RL Genes Dev. 16:1498-1508(2002).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-1024.
RX PubMed=15767665; DOI=10.1128/mcb.25.7.2583-2592.2005;
RA Moore L.L., Stanvitch G., Roth M.B., Rosen D.;
RT "HCP-4/CENP-C promotes the prophase timing of centromere resolution by
RT enabling the centromere association of HCP-6 in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 25:2583-2592(2005).
CC -!- FUNCTION: Chromosomal protein which is recruited to mitotic chromosomes
CC by hcp-3 (CENP-A) and hcp-4 (CENP-C) (PubMed:12080088,
CC PubMed:15767665). Involved in chromosome segregation during mitosis,
CC playing a role in chromosome condensation and in maintaining chromosome
CC morphology, rigidity and orientation during mitosis (PubMed:12080088,
CC PubMed:15767665). {ECO:0000269|PubMed:12080088,
CC ECO:0000269|PubMed:15767665}.
CC -!- SUBUNIT: Component of the condensin-2 complex.
CC {ECO:0000250|UniProtKB:P42695, ECO:0000255|PIRNR:PIRNR036508}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PIRNR:PIRNR036508}.
CC Chromosome, centromere {ECO:0000269|PubMed:12080088,
CC ECO:0000269|PubMed:15767665}. Note=Localizes to the centromere during
CC mitosis (PubMed:12080088). Co-localizes with hcp-3 (CENP-A) at
CC prophase, metaphase, and anaphase chromosomes (PubMed:12080088,
CC PubMed:15767665). Mitotic chromosome localization is dependent on hcp-3
CC (CENP-A) and hcp-4 (CENP-C) (PubMed:12080088, PubMed:15767665).
CC Localizes along two parallel lines on individual prophase chromosomes
CC (PubMed:12080088). At metaphase, localizes at the poleward faces of the
CC metaphase plate (PubMed:12080088). During anaphase, localizes with the
CC separating groups of sister chromatids (PubMed:12080088).
CC {ECO:0000269|PubMed:12080088, ECO:0000269|PubMed:15767665}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:Y110A7A.1b};
CC IsoId=Q95Y84-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:Y110A7A.1a};
CC IsoId=Q95Y84-2; Sequence=VSP_061464, VSP_061465;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in temperature
CC sensitive embryonic lethality with chromosomes displaying segregation
CC defects with increased anaphase bridges and chromosome lagging.
CC {ECO:0000269|PubMed:12080088}.
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DR EMBL; BX284601; CCD66189.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD66190.1; -; Genomic_DNA.
DR RefSeq; NP_491537.1; NM_059136.1.
DR RefSeq; NP_491538.1; NM_059137.3.
DR AlphaFoldDB; Q95Y84; -.
DR ComplexPortal; CPX-1272; Condensin II complex.
DR IntAct; Q95Y84; 5.
DR STRING; 6239.Y110A7A.1b; -.
DR EPD; Q95Y84; -.
DR PaxDb; Q95Y84; -.
DR PeptideAtlas; Q95Y84; -.
DR EnsemblMetazoa; Y110A7A.1a.1; Y110A7A.1a.1; WBGene00001833. [Q95Y84-2]
DR EnsemblMetazoa; Y110A7A.1b.1; Y110A7A.1b.1; WBGene00001833. [Q95Y84-1]
DR GeneID; 266830; -.
DR KEGG; cel:CELE_Y110A7A.1; -.
DR UCSC; Y110A7A.1b; c. elegans. [Q95Y84-1]
DR CTD; 266830; -.
DR WormBase; Y110A7A.1a; CE24117; WBGene00001833; hcp-6. [Q95Y84-2]
DR WormBase; Y110A7A.1b; CE28104; WBGene00001833; hcp-6. [Q95Y84-1]
DR eggNOG; KOG0413; Eukaryota.
DR GeneTree; ENSGT00940000153566; -.
DR HOGENOM; CLU_002816_0_0_1; -.
DR InParanoid; Q95Y84; -.
DR OMA; DKSPMVR; -.
DR OrthoDB; 60751at2759; -.
DR PhylomeDB; Q95Y84; -.
DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001833; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q95Y84; baseline and differential.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:WormBase.
DR GO; GO:0000796; C:condensin complex; IDA:WormBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:WormBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0010032; P:meiotic chromosome condensation; IBA:GO_Central.
DR GO; GO:0045132; P:meiotic chromosome segregation; IC:ComplexPortal.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:WormBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:WormBase.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026971; CND1/NCAPD3.
DR InterPro; IPR032682; Cnd1_C.
DR InterPro; IPR012371; NCAPD3.
DR PANTHER; PTHR14222; PTHR14222; 1.
DR Pfam; PF12717; Cnd1; 1.
DR PIRSF; PIRSF036508; Condns_HCP-6; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; DNA condensation; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..1758
FT /note="Condensin-2 complex subunit hcp-6"
FT /id="PRO_0000455242"
FT REGION 428..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1326..1385
FT /evidence="ECO:0000255"
FT COMPBIAS 437..465
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1623..1638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1706..1724
FT /note="RSKKVKLITFTISSKRMKR -> RKSQAYHLHNIFEEDEEES (in
FT isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_061464"
FT VAR_SEQ 1725..1758
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_061465"
FT MUTAGEN 1024
FT /note="G->E: In mr17; chromosome segregation and
FT orientation defects with increased anaphase bridges and
FT chromosome lagging which have sister chromatids with a
FT single kinetochore connected to microtubules emanating from
FT both spindle poles. Furthermore, centromere organization is
FT disrupted. Chromosomes display morphological impairments
FT such as chromosome twisting, and have condensation and
FT sister centromere attachment defects. Inhibition of spindle
FT microtubules with the drug nocodazole, impairs sister
FT centromere attachment defects further. Does not localize to
FT mitotic chromosomes. Specifically, does not localize to the
FT centromeres of metaphase chromosomes."
FT /evidence="ECO:0000269|PubMed:12080088,
FT ECO:0000269|PubMed:15767665"
SQ SEQUENCE 1758 AA; 198883 MW; 3D34A1019B9205F6 CRC64;
MSNINEKDLS EFLESNLRSL NDIDDAVATS SAECNYEDYE EFTNSVDLTF FEQDLSGVLK
ELKKLAESVV ISGKKCDIRN IFEESDVATM KFNLFVWYFL ENGQRSDSSE EDVDKGVSAA
SSYIAMCSLP GAISDLYQIG LYNQCLKIIR NCCHTVRIGE TVVTKKSSGA KKKKAGGKSD
ETNVDGEMTV TTGAADPIIG PPRIAVDSAE RYLHHLTTQL FAFLHSNTFS IDTPTLMSTL
EVVEDIGRLD LDNRTAGRAI RANSVHEFRS LERFTDRYCA FVHSLVESKY KTRAEVAYGR
LIRPRLALMP YPDESNKSSK ISTERKRSGE LHVNLILSRI SRNPEARELK YIQTVTVMVY
SQCPDLAEFR TNIATFIHKI LEALPYTYTY DFVQFMNVLF KGRGAGVKSL STELSSILIS
SFDFTAPDPG AIPNLDAEQN EEEDEEEEGE DEEEEEENEQ DDVAVKEEEQ SDKSDEENDG
DNEENVSKKK EEKKKEKKAK EVKEVGRMDA MSVLYNIVYM ACLDKAAAMR LHGANSLTKI
LQSQSHREAF QLFCATINAE MDEKFGAVGD NLSESLEDLN VSGKAPSSKT KKPTDLLLDE
QQIIQKFNKL KLMNKGETRV EKDIVYMIVR RLSTDDKAPV KKAACSLLKS YLSYCDEASK
FEVVLSILQM LCRDRMVSVR KTGADAFTEL MLRDAILFKE SLSSKWLHTL ISMLNDTDND
VTEHARKLIM KVLTPLLENS SDLTWTLLDT IESVTNHRQY LMSTLKDAVR EKLVKRTVMD
SMKQHIISGS EKLDGAWMVF SQLCVQFEQN VDFAIETFSR VDLSRESNLV QYMIHVIENN
IKKIDDDTKS DLVNTLQGTF RDYCLHPSHS RSIYHCLGKL MDGIGDRSLH GKEFSDFGET
LLIKCFDTIV QSFEMFKDKD EWKRNSESQE RLLCTALNVA SEVFSYSPQL VPRHERLGKT
LSLIVNSTEN GSSDASTVNP DMPSVHHTRP PTQLSEVPSS QKSSKGGMMS HEGAMFSDKV
RAVGVVTLAN MILAHDRLLK LMPMLVKQLQ YNTAHQIRSN IVLAIGDICS SYKTDRYAPM
LAASLCDPSV IVRRHAINQI ARLISFGIFR FNGEIMIRMM LASLDANEDV RNDAKLYISE
VLQSEEPNFF PLNFVQYMIA LTQARRLVGV GHDEDDRGQV DVAIGGGDPL ARPSRIAIYT
FMIDSLDDRS RFDVKMSICQ RIFTPIVNGE YDFSDYNVQC LLDDALLIMA SNEMQVKMDV
GKNPNENAMD DPSPEVLEAA TGFMQKVYLD HYMKTIVPSI LSLREFLNQH RSPLQRKCLL
AIRMICIEHK NDIDEILQDN RQLKDEMMFE LQRVKQRTEE ANRILDEYLK RVAEFKKQQK
RLSKSPAPME LDAEPVQESA EAVEMGSPAR RIEEDQENVE EEVEMRTPQK KNPDADVPRT
PLNALRSTTE EKSTPNARLL SPKTIKKIRR SLGALIHTEM RLNPPNLEET KIDDTTINRS
KQADKTEEKT IVEEEPMEEA AAEKTVTAEN DHVDAEKTVI AVEIPPATEA EEDEVVDVQS
ESRRSRRRKT PNYDDEESVD ADGKIWKKPK IVNKSPEKEV NISANVTLRR SRRGQSTEPP
VVKENSNRKR KSVDEEEENV PTSSSGNTEN DPLSRGVTPL IFDESKLGAG RHCSTPIRSR
EDADPSDVTF SLNLSAITEK EDLKNRSKKV KLITFTISSK RMKRKADQCH CINLPSKFVL
FISTVCIIVR LSAVFSLN
