CND1_XENLA
ID CND1_XENLA Reviewed; 1364 AA.
AC Q9YHY6; Q9YGS5;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Condensin complex subunit 1;
DE AltName: Full=Chromosome assembly protein XCAP-D2;
DE AltName: Full=Chromosome condensation-related SMC-associated protein 1;
DE AltName: Full=Chromosome-associated protein D2;
DE AltName: Full=Eg7;
DE AltName: Full=Non-SMC condensin I complex subunit D2;
GN Name=ncapd2; Synonyms=capd2, cnap1, eg7;
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], FUNCTION OF THE CONDENSIN COMPLEX, AND
RP PHOSPHORYLATION AT THR-1314; THR-1348 AND THR-1353 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Egg;
RX PubMed=9852142; DOI=10.1083/jcb.143.6.1437;
RA Cubizolles F., Legagneux V., Le Guellec R., Chartrain I., Uzbekov R.,
RA Ford C., Le Guellec K.;
RT "pEg7, a new Xenopus protein required for mitotic chromosome condensation
RT in egg extracts.";
RL J. Cell Biol. 143:1437-1446(1998).
RN [3]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH XCAP-C; XCAP-E; XCAP-H 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.
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 topoisomerases. May target the condensin
CC complex to DNA via its C-terminal domain. {ECO:0000269|PubMed:10428035,
CC ECO:0000269|PubMed:9774278, ECO:0000269|PubMed:9852142}.
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 -!- INTERACTION:
CC Q9YHY6; P50533: smc2; NbExp=4; IntAct=EBI-15815271, EBI-3511283;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9852142}. Cytoplasm
CC {ECO:0000269|PubMed:9852142}. Chromosome {ECO:0000269|PubMed:9852142}.
CC Note=In interphase cells, the majority of the condensin complex is
CC found in the cytoplasm, while a minority of the complex is associated
CC with chromatin. A subpopulation of the complex however remains
CC associated with chromosome foci in interphase cells. During mitosis,
CC most of the condensin complex is associated with the chromatin. At the
CC onset of prophase, the regulatory subunits of the complex are
CC phosphorylated by CDK1, leading to condensin's association with
CC chromosome arms and to chromosome condensation. Dissociation from
CC chromosomes is observed in late telophase.
CC -!- DOMAIN: The C-terminal domain interacts with histones H1 and H3, and
CC may be responsible for condensin complex targeting to mitotic
CC chromosomes. This domain is independent from the bipartite nuclear
CC localization signal, although they are contained within the same region
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that of
CC XCAP-H and XCAP-G subunits, activates the condensin complex and is
CC required for chromosome condensation. {ECO:0000269|PubMed:9774278}.
CC -!- SIMILARITY: Belongs to the CND1 (condensin subunit 1) family.
CC {ECO:0000305}.
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DR EMBL; AF067969; AAC64359.1; -; mRNA.
DR EMBL; AF072717; AAD15962.1; -; mRNA.
DR PIR; T14900; T14900.
DR RefSeq; NP_001081840.1; NM_001088371.1.
DR AlphaFoldDB; Q9YHY6; -.
DR SMR; Q9YHY6; -.
DR BioGRID; 99415; 2.
DR DIP; DIP-48587N; -.
DR IntAct; Q9YHY6; 2.
DR iPTMnet; Q9YHY6; -.
DR PRIDE; Q9YHY6; -.
DR GeneID; 398080; -.
DR KEGG; xla:398080; -.
DR CTD; 398080; -.
DR Xenbase; XB-GENE-5854852; ncapd2.S.
DR OrthoDB; 166920at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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; 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 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Cytoplasm; DNA condensation;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1364
FT /note="Condensin complex subunit 1"
FT /id="PRO_0000095037"
FT REGION 1..588
FT /note="Interaction with XCAP-E and XCAP-C"
FT /evidence="ECO:0000250"
FT REGION 567..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1317..1326
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 575..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1314
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:9774278"
FT MOD_RES 1348
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:9774278"
FT MOD_RES 1353
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:9774278"
FT CONFLICT 22
FT /note="Q -> H (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="A -> G (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="L -> M (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="L -> P (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="E -> G (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="S -> A (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="S -> T (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="N -> S (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="E -> EE (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 511..513
FT /note="REQ -> ARR (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="E -> V (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 571..573
FT /note="PTT -> STA (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 584..588
FT /note="Missing (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="N -> K (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 752..753
FT /note="EF -> AL (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="R -> W (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 1290
FT /note="P -> A (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
FT CONFLICT 1310
FT /note="D -> G (in Ref. 2; AAD15962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1364 AA; 154191 MW; 92F8C83C95A88D4D CRC64;
MTFHFHIPLA FRDLLKSGGI GQYVVQEVLP VRHVDAQFAA FQTSFRTEAP LCILQHFDTL
YSILHHFRSL DIAIKEDVLE VMVKVASRHA NELPAILEDL NLSVPQRAAH LNALKMNCFI
LTQLIEAFEA ETYKASLGSV EPSGKGKKAK SKPEGFSWES ERESILQALT HLLQLDIRRL
WSMSVVEEEF VSMMTSCCYK MMENPNIVMA KNKSTREALG HLLGVTVKRY NHMLSASVKV
IQLLQHFEHL ASVLVHTVSL WATEYGMKPV IGEIMREIGQ KCSQDLSRES SGFKAFATFL
TELAERIPAI MMPSISVLLD YLDGENYMMR NSVLTVMGEM VVRVLSGDQL EEAEKSSRDQ
FLDTLQEHLH DVNTYVRSCV IQIYNRIVQE KALPLSRFQS VVTLVVGRLF DKSVNVCKNA
IQLLASFLAN NPFTCKLSSV DLKVPLEKET KKLKEMREKY QGPKPVVVIS PEEEWEAMLP
EVLEAFKILQ QESKEEEDIE TEEIESSQHL REQILILLRK TSYKNSIRLT QKGIERFQED
PLFSEGDSEA KSELGILEKI FTEKKADLEQ PTTKDQDDAQ VNPTSEELPS QEVQNSDMDK
QEMLVQYLSD AHHFALKIEE AIDVISKMMY ETAVSVVQEV IEFFVTVSQF GVSQALLGVR
RMLPLVWSKE PGVREAVLSA YRRLYLSSNG ESERVKAQAL VRSLSLLMVD SSAGILQCLE
EIVSEFVQKG DIHPSVIQLL WEKFTQKSPC SEFERRAAVM LLGMMTRGQP EIVMSNLDTL
VSVGLGEQVQ KDYQLAREVC NCILKITDSQ KQTLGKSTEP FRLPKDHSLF VCLTEAVAGG
IGLSGLHWLP FKETAVRLVY ELGEEPEEIC SEILLRCSQN VLDGHQTQDE VPNVPAFLLT
HLLSLAGDVA LQQVVHLERA VSAELRRRRV LKEEQEAEKV GKQRKSKANE STMEEELGLV
GASADDIEAE LIRKICDTEL LGGQQYLSAF LPLILRICNN PGRYSDPDLC TVATLALAKY
MMISSDFCDT HLRLLFTLLE KSPLPSVRSN IMIALGDLSI RFPNLIEPWT PNLYARLRDP
SREVRKTAGM VMTHLILKDM VKVKGQVSEM AVLLIESDQE ISALARNFFN ELSNKGNAVY
NLLPDIISRL SDPDCGVEEE AFRTIMKQLL SYITKDKQTE SLVEKMCHRF RTARTERQWR
DLAHCLSLLP FSEKGLRKMQ DCFDCYGDKL SDEAVYNSFL TTVAKMRRGA KPELKALIDE
FEQKLSRCHN KGLENMDVPE EPSAESDAQP PKAKRPPLAS VNVKKGKSED DFQTPKPPAS
RKSRRKVAVN FSSDEESDLE AELSEAETPK NPTPIRRTAR SRAK
