CNDD2_ARATH
ID CNDD2_ARATH Reviewed; 1410 AA.
AC A0A1I9LM04; F4J245; Q9M1J4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Condensin-1 complex subunit CAP-D2 {ECO:0000303|PubMed:22855829, ECO:0000303|PubMed:23929493};
DE AltName: Full=Protein CHROMOSOME-ASSOCIATED POLYPEPTIDE D-2 {ECO:0000303|PubMed:23929493};
DE Short=AtCap-D2 {ECO:0000303|PubMed:23929493};
GN Name=CAP-D2 {ECO:0000303|PubMed:22855829, ECO:0000303|PubMed:23929493};
GN OrderedLocusNames=At3g57060 {ECO:0000312|Araport:AT3G57060};
GN ORFNames=F24I3.140 {ECO:0000312|EMBL:CAB72176.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16856987; DOI=10.1111/j.1365-313x.2006.02814.x;
RA Rama Devi S., Chen X., Oliver D.J., Xiang C.;
RT "A novel high-throughput genetic screen for stress-responsive mutants of
RT Arabidopsis thaliana reveals new loci involving stress responses.";
RL Plant J. 47:652-663(2006).
RN [4]
RP REVIEW.
RX PubMed=22855829; DOI=10.1101/gad.194746.112;
RA Hirano T.;
RT "Condensins: universal organizers of chromosomes with diverse functions.";
RL Genes Dev. 26:1659-1678(2012).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=23929493; DOI=10.1007/s00412-013-0424-y;
RA Schubert V., Lermontova I., Schubert I.;
RT "The Arabidopsis CAP-D proteins are required for correct chromatin
RT organisation, growth and fertility.";
RL Chromosoma 122:517-533(2013).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25065716; DOI=10.1111/tpj.12628;
RA Smith S.J., Osman K., Franklin F.C.;
RT "The condensin complexes play distinct roles to ensure normal chromosome
RT morphogenesis during meiotic division in Arabidopsis.";
RL Plant J. 80:255-268(2014).
CC -!- FUNCTION: Essential protein (PubMed:23929493). Regulatory subunit of
CC the condensin complex, a complex required for conversion of interphase
CC chromatin into mitotic-like condense chromosomes (By similarity). The
CC condensin complex probably introduces positive supercoils into relaxed
CC DNA in the presence of type I topoisomerases and converts nicked DNA
CC into positive knotted forms in the presence of type II topoisomerases
CC (By similarity). Required for fertility, growth and euchromatin
CC organization, but not for sister chromatid cohesion (PubMed:23929493).
CC Necessary to maintain normal structural integrity of the meiotic
CC chromosomes during the two nuclear divisions of gametogenesis,
CC especially to maintain compaction of the centromeric repeats and 45S
CC rDNA (PubMed:25065716). Seems also involved in crossover formation
CC during meiotic prophase I (PubMed:25065716). Prevents centromeric and
CC pericentromeric heterochromatin repeats association (PubMed:23929493).
CC Contributes to the induction of stress-responsive genes in response to
CC stress treatment (PubMed:16856987). {ECO:0000250|UniProtKB:Q15021,
CC ECO:0000269|PubMed:16856987, ECO:0000269|PubMed:23929493,
CC ECO:0000269|PubMed:25065716}.
CC -!- SUBUNIT: Component of the condensin complex.
CC {ECO:0000250|UniProtKB:Q15021}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:25065716}. Nucleus
CC {ECO:0000250|UniProtKB:Q15021}. Note=Associates with the chromosomes
CC throughout meiosis. {ECO:0000269|PubMed:25065716}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A1I9LM04-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A1I9LM04-2; Sequence=VSP_061381;
CC -!- TISSUE SPECIFICITY: Present in buds. {ECO:0000269|PubMed:25065716}.
CC -!- DEVELOPMENTAL STAGE: Mostly expressed at bolting, flowering and during
CC seed formation. {ECO:0000269|PubMed:23929493}.
CC -!- INDUCTION: Regulated in a cell cycle-dependent manner with an increase
CC during G2 phase, highest levels in the middle of G2 and a drop during
CC mitosis. {ECO:0000269|PubMed:23929493}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutants are not viable
CC (PubMed:23929493). Heterozygous mutants exhibit a reduced fertility
CC (PubMed:23929493, PubMed:25065716). Non-structural maintenance of
CC chromosomes condensing subunit (PubMed:23929493). During meiosis,
CC elongated chromosome at metaphase I, stretched centromeric DNA at
CC metaphase I as well as a slight reduction in crossover formation
CC (PubMed:25065716). Reduced expression of stress-responsive genes in the
CC root tip in response to stress treatment (PubMed:16856987).
CC {ECO:0000269|PubMed:16856987, ECO:0000269|PubMed:23929493,
CC ECO:0000269|PubMed:25065716}.
CC -!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB72176.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL138655; CAB72176.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79606.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63612.1; -; Genomic_DNA.
DR PIR; T47766; T47766.
DR RefSeq; NP_001325687.1; NM_001339840.1.
DR SMR; A0A1I9LM04; -.
DR iPTMnet; F4J245; -.
DR ProteomicsDB; 207531; -.
DR ProteomicsDB; 208342; -.
DR EnsemblPlants; AT3G57060.1; AT3G57060.1; AT3G57060. [A0A1I9LM04-2]
DR EnsemblPlants; AT3G57060.3; AT3G57060.3; AT3G57060. [A0A1I9LM04-1]
DR GeneID; 824873; -.
DR Gramene; AT3G57060.1; AT3G57060.1; AT3G57060. [A0A1I9LM04-2]
DR Gramene; AT3G57060.3; AT3G57060.3; AT3G57060. [A0A1I9LM04-1]
DR Araport; AT3G57060; -.
DR HOGENOM; CLU_001867_2_1_1; -.
DR OMA; RNCVLQI; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; A0A1I9LM04; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IEP:UniProtKB.
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; 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 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Chromosome;
KW DNA condensation; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..1410
FT /note="Condensin-1 complex subunit CAP-D2"
FT /id="PRO_0000454772"
FT REGION 469..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1282
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1363
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1370..1383
FT /note="Missing (in isoform 2)"
FT /id="VSP_061381"
SQ SEQUENCE 1410 AA; 157118 MW; ABC6EAD81C419DED CRC64;
MAPPFVFPQI LRALEEDPED NHRLFAQNPV DVTSLRPSDL EEFVKGVSFD LSDRELFCVE
DQDVFDRVYS LVRSFFSLPP SCKCNLVESL RSNLSVLLPN VDSISRSVQD QEDDVPIIDR
ITSHRNALKI YTFFLLTVVM NEESHISSVE TTKVAARGRK KQIIQSWNWE PQRGRMLNLI
ANSLEINLSL LFGSSDLDEN YLSFIVKNSF TLFENATILK DAETKDALCR IIGASATKYH
YIVQSCASIM HLIHKYDFAV VHIADAVARA ESKYSDGTLA VTIIRDIGRT DPKAYVKDTA
GADNVGRFLV ELADRLPKLM STNVGVLVPH FGGESYKIRN ALVGVLGKLV AKAFNDVEGD
MSSKSLRLRT KQAMLEILLE RCRDVSAYTR SRVLQVWAEL CEEHSVSIGL WNEVASLSAG
RLEDKSAIVR KSALNLLIMM LQHNPFGPQL RIASFEATLE QYKRKLNELE PTEHASKEST
SDGESCNGDG EIDDLHLETT TKIHQDSLSD SCQPENGEEI SEKDVSVPDI GNVEQTKALI
ASLEAGLRFS KCMSASMPIL VQLMASSSAT DVENAILLLM RCKQFQIDGA EACLRKILPL
AFSQDKSIYE AVENAFISIY IRKNPVDTAK QLLNLAIDSN IGDQAALEFI VNALVSKGEI
SSSTTSALWD FFCFNINGTT AEQSRGALSI LCMAAKSSPR ILGSHIQDII DIGFGRWAKV
EPLLARTACT VIQRFSEEDR KKLLLSSGSR LFGILESLIT GNWLPENIYY ATADKAISAI
YMIHPTPETL ASTIIKKSLS TVFDVVEQEE AQTDTENNKV DILTPVQVAK LSRFLFAVSH
IAMNQLVYIE SCIQKIRRQK TKKDKPAAES QNTEENLEAT QENNGINAEL GLAASDDALL
DTLAERAERE IVSGGSVEKN LIGECATFLS KLCRNFSLLQ KHPELQASAM LALCRFMIID
ASFCESNLQL LFTVVENAPS EVVRSNCTLS LGDLAVRFPN LLEPWTENMY ARLRDASVSV
RKNAVLVLSH LILNDMMKVK GYIYEMAICI EDDVERISSL AKLFFHELSK KGSNPIYNLL
PDILGQLSNR NLERESFCNV MQFLIGSIKK DKQMEALVEK LCNRFSGVTD GKQWEYISYS
LSLLTFTEKG IKKLIESFKS YEHALAEDLV TENFRSIINK GKKFAKPELK ACIEEFEEKI
NKFHMEKKEQ EETARNAEVH REKTKTMESL AVLSKVKEEP VEEYDEGEGV SDSEIVDPSM
EESGDNLVET ESEEEPSDSE EEPDSAQCGT AIPRYLNQKT SGDNLIETEP EEEQSDSEPD
SAQCGTTNPR SLNRKTSGDN LIETESEEEQ SDSEEEPSDS EEEPDSAQCG TTNPRSLNQK
TSGGEEGESE SKSTESSSSI RRNLRSGSRS
