CNDD3_MOUSE
ID CNDD3_MOUSE Reviewed; 1506 AA.
AC Q6ZQK0; E9QPR0; Q9CS21;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Condensin-2 complex subunit D3;
DE AltName: Full=Non-SMC condensin II complex subunit D3;
GN Name=Ncapd3; Synonyms=Kiaa0056;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-157.
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1506.
RC TISSUE=Fetal brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP PROTEIN SEQUENCE OF 1499-1506, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulatory subunit of the condensin-2 complex, a complex
CC which establishes mitotic chromosome architecture and is involved in
CC physical rigidity of the chromatid axis. 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. Specifically
CC required for decatenation of centromeric ultrafine DNA bridges during
CC anaphase. Early in neurogenesis, may play an essential role to ensure
CC accurate mitotic chromosome condensation in neuron stem cells,
CC ultimately affecting neuron pool and cortex size.
CC {ECO:0000250|UniProtKB:P42695}.
CC -!- SUBUNIT: Component of the condensin-2 complex, which contains the SMC2
CC and SMC4 heterodimer, and 3 non SMC subunits that probably regulate the
CC complex: NCAPH2, NCAPD3 and NCAPG2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AC156163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK019297; BAB31654.1; -; mRNA.
DR EMBL; AK129046; BAC97856.1; -; mRNA.
DR CCDS; CCDS57665.1; -.
DR RefSeq; NP_835214.2; NM_178113.3.
DR AlphaFoldDB; Q6ZQK0; -.
DR BioGRID; 219559; 9.
DR ComplexPortal; CPX-986; Condensin II complex.
DR IntAct; Q6ZQK0; 2.
DR MINT; Q6ZQK0; -.
DR STRING; 10090.ENSMUSP00000072871; -.
DR iPTMnet; Q6ZQK0; -.
DR PhosphoSitePlus; Q6ZQK0; -.
DR EPD; Q6ZQK0; -.
DR jPOST; Q6ZQK0; -.
DR MaxQB; Q6ZQK0; -.
DR PaxDb; Q6ZQK0; -.
DR PRIDE; Q6ZQK0; -.
DR ProteomicsDB; 283646; -.
DR DNASU; 78658; -.
DR GeneID; 78658; -.
DR KEGG; mmu:78658; -.
DR CTD; 23310; -.
DR MGI; MGI:2142989; Ncapd3.
DR eggNOG; KOG0413; Eukaryota.
DR InParanoid; Q6ZQK0; -.
DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR BioGRID-ORCS; 78658; 20 hits in 73 CRISPR screens.
DR ChiTaRS; Ncapd3; mouse.
DR PRO; PR:Q6ZQK0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6ZQK0; protein.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IBA:GO_Central.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:ComplexPortal.
DR GO; GO:0000796; C:condensin complex; IDA:MGI.
DR GO; GO:0042585; C:germinal vesicle; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005721; C:pericentric heterochromatin; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010032; P:meiotic chromosome condensation; IBA:GO_Central.
DR GO; GO:0051307; P:meiotic chromosome separation; IMP:MGI.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:UniProtKB.
DR GO; GO:1905821; P:positive regulation of chromosome condensation; IC:ComplexPortal.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:ComplexPortal.
DR GO; GO:1905820; P:positive regulation of chromosome separation; IMP:ComplexPortal.
DR Gene3D; 1.25.10.10; -; 3.
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 Cell cycle; Cell division; Coiled coil; Direct protein sequencing;
KW DNA condensation; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1506
FT /note="Condensin-2 complex subunit D3"
FT /id="PRO_0000050717"
FT REPEAT 442..476
FT /note="HEAT 1"
FT REPEAT 532..567
FT /note="HEAT 2"
FT REPEAT 574..605
FT /note="HEAT 3"
FT REPEAT 968..1004
FT /note="HEAT 4"
FT REGION 154..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1473..1506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1213..1270
FT /evidence="ECO:0000255"
FT COMPBIAS 154..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42695"
FT MOD_RES 1359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42695"
FT MOD_RES 1368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42695"
FT MOD_RES 1381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42695"
FT MOD_RES 1393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42695"
FT CONFLICT 128
FT /note="I -> S (in Ref. 2; BAB31654 and 3; BAC97856)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="T -> E (in Ref. 3; BAC97856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1506 AA; 169432 MW; D0DE95875214D3FD CRC64;
MALQDLGENL QPWCPLGLSL EWVKTVWDLD FTEIEPLDPS IVGEILETGR DAFTKLYGSL
FPFATDESGS LESIWTFFTE NDISSNTLVA LFCHFVQEAH KKSASAQYRE YGLHAAGLYF
LLLEIPGIVV NQVFHPVMFD KCIQILKRSW PQESNLTQKR KKDHSKSSKD NYRKSRKRGK
PPRKEDYQVD ELSREEEEEE EEIYFSGRDL CQIRDAIFNL LKNFLRLLPK FSLKEKPQSI
QTCIEVFVAL TSFEPIPHKF LISQARNLNE VKHISELAYY GLYLLCSPVH GEENKVIGSI
FHQMLNVILM LEVGEGSRCA PLAITSQVIN CRNQAVQFVS SLVDELQASV YPVLGTLLQH
ICAKVVDKAE YRTYAAQSLV QLLTKLPSEE YATFIAWLYK YSRSSKIPHR VFTLDVALAL
LTLPERELDD TVSLEHQKFL KHKFFVQEII FDRCLDKAPT VRSKALSSFA HCLELSSSNT
SESILEIFIN SNLVPGIQNL SNTVLNPSPV LTSRNGYSAQ SRTHNNDEQT LPGERCFMTM
LRKRIKDEKI NVRKSALQVL MSILKHCDIL SMEQDLLILQ DHCRDPAISV RKQALQSLTE
LVMAQPTCVP VQKAWLMGVI PVVMDCESTV QEKALECLDQ LLLQNIKHHK KFHSADRSQV
LAWSLLALLT IENQDLRRYL NKAFHIWSKK DKFSSTFINS VISHTDTERS APAWMLLSKI
TCSSPKLDYT KIIESWERLS REQSPNSNTL GYMLCVIGHI AKHLPKGTRD KITGVIKAKL
NGFQWSPELI SSSVDALQKL CRASAKTVLE EQGLLKQVCG DVLATCEQHL SNILLKEDGT
GNMDEGLVVK CIFTLGDIAQ LCPAIVEKRV FLLIQSILAS SAHSDHLPSS QGTTDALDSQ
PPFQPRSSAM PSVIRAHAII TLGKLCLQHE DLAKKSIPAL VRELEVSEDV AVRNNVIIVI
CDLCIRYTVM VDNYIPNISV CLKDSDPFIR KQTLVLLTNL LQEEYVKWKG SLFFRFVSTL
VDSHPDIASL GEFCLAHLLL KRNPTMFFQH FIECIFHFNS YEKHGQYNKF SQSERGKQLF
LLKGKTNKEK RMRIYKFLLE HFTDEQRFNV TSKICLNILA CFTDGILPMD MEASELLSDT
FDILNSKEIK LLAMRAQTSK DLLEEDDVAL ANVVMQEAQM KIISQVQKRN FIENIIPIII
SLKTVLEKNK IPALRELMNY LREVMQDYRD EINDFFAVDK QLASELEYDM KKYNEQLAQE
QALTEHANAT KGPEDSDRVP SAQVAPDLEA VPALAAAPMA AAAAAAPMAA AAAAAGQDNA
DVPPTQSRPS APRSNFTPTL PPISENGPLK IMSSTRPMSL STIAILNSVK KAVASKNRTR
SLGALPFNVE TGSPENPSSH ESSLSLEKES DRTVNHVTKR AISTPENSIS DVTFAAGVSY
IGTPATFFTK EKHEAQEQGS DILCLSLLDK RPPQSPQWNV KSPARSHGST RSSRRSLRKA
PLKTAN
