SMC2_XENLA
ID SMC2_XENLA Reviewed; 1203 AA.
AC P50533;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Structural maintenance of chromosomes protein 2;
DE Short=SMC protein 2;
DE Short=SMC-2;
DE AltName: Full=Chromosome assembly protein XCAP-E;
DE AltName: Full=Chromosome-associated protein E;
GN Name=smc2; Synonyms=cape, smc2l1;
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], AND INTERACTION WITH XCAP-C.
RX PubMed=7954811; DOI=10.1016/0092-8674(94)90254-2;
RA Hirano T., Mitchison T.J.;
RT "A heterodimeric coiled-coil protein required for mitotic chromosome
RT condensation in vitro.";
RL Cell 79:449-458(1994).
RN [2]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH XCAP-C; XCAP-H; XCAP-D2 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 [3]
RP FUNCTION OF THE CONDENSIN COMPLEX.
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 [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: Central component 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. {ECO:0000269|PubMed:10428035,
CC ECO:0000269|PubMed:9774278}.
CC -!- SUBUNIT: Forms a heterodimer with XCAP-C/SMC4. Component of the
CC condensin complex, which contains the XCAP-E/SMC2 and XCAP-C/SMC4
CC heterodimer, and three non SMC subunits that probably regulate the
CC complex: XCAP-H/BRRN1, XCAP-D2/CNAP1 and XCAP-G/CAPG.
CC {ECO:0000269|PubMed:9160743}.
CC -!- INTERACTION:
CC P50533; Q9YHY6: ncapd2; NbExp=4; IntAct=EBI-3511283, EBI-15815271;
CC P50533; Q6GN08: ncapd3.L; NbExp=3; IntAct=EBI-3511283, EBI-15815299;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the
CC condensin complex is found in the cytoplasm, while a minority of the
CC complex is associated with chromatin. A subpopulation of the complex
CC however remains associated with chromosome foci in interphase cells.
CC During mitosis, most of the condensin complex is associated with the
CC chromatin. At the onset of prophase, the regulatory subunits of the
CC complex are phosphorylated by CDC2, leading to condensin's association
CC with chromosome arms and to chromosome condensation. Dissociation from
CC chromosomes is observed in late telophase (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The SMC hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with XCAP-C, forming
CC a V-shaped heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily. {ECO:0000305}.
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DR EMBL; U13674; AAA64680.1; -; mRNA.
DR PIR; B55094; B55094.
DR RefSeq; NP_001081372.1; NM_001087903.1.
DR AlphaFoldDB; P50533; -.
DR SMR; P50533; -.
DR BioGRID; 99139; 4.
DR DIP; DIP-48586N; -.
DR IntAct; P50533; 5.
DR MaxQB; P50533; -.
DR GeneID; 397800; -.
DR KEGG; xla:397800; -.
DR CTD; 397800; -.
DR Xenbase; XB-GENE-5826203; smc2.L.
DR OrthoDB; 119789at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 397800; Expressed in neurula embryo and 18 other tissues.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR CDD; cd03273; ABC_SMC2_euk; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR027120; Smc2_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Chromosome; Coiled coil; Cytoplasm;
KW DNA condensation; Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1203
FT /note="Structural maintenance of chromosomes protein 2"
FT /id="PRO_0000118998"
FT DOMAIN 522..640
FT /note="SMC hinge"
FT REGION 1174..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..513
FT /evidence="ECO:0000255"
FT COILED 670..1032
FT /evidence="ECO:0000255"
FT COMPBIAS 1187..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1203 AA; 136342 MW; 04323DD0027DF309 CRC64;
MHVKSIIIDG FKSYAQRTEI NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLTQVRAS
NLQDLVYKNG QAGITKATVS ITFDNYDKKQ SPLGFEAHDE ITVTRQVVIG GRNKYLINGV
NANNTRVQDL FCSVGLNVNN PHFLIMQGRI TKVLNMKPPE ILAMIEEAAG TRMYECKKIA
AQKTIEKKEA KLKEIQTILE EEITPTIHKL KEERSSYLEY QKIMREIEHL SRLYVAYQFV
CAEETKVRSA EELKEMQDSI LKLQDTMAEN ERKVKELGKE IAELEKMRDQ EVGGALRSLE
EALSEAQRAD TKVQSALDLK KQNMKAEREK KRKELVKSME EDAKVLTAKE KEVKKITDGL
SSLQEASQKD VEAFTSAQQH FNAVSAGLSS NEDGEEATLA GQMMACKNET SKAETEAKQA
QMKLKHAQQE LKTKQAEVKK MDGGYKKDNE AFEAVKKSKE KLEVEMKKLN YEDGREEQLL
EKRRGLSRDV NRLREAYESL MARFPNLQFE YKDPEKNWDS DRVKGLVASL ISIKDVSTAT
ALEVVAGGRL YNVVVDTEVT GKKLLEKGEL KRRFTIIPLN KISARCLGKD TVNVAKNLVG
ADNVNLALSL VGYESELQKA MEYVFGTTLV CDTMDNAKKV TFDKRIMTKT VTLGGDTFDP
QGTLSGGARS QNASVLVRLQ ELKDVQDELK AKETELQEVE KELMTLKNTV ERYRQLKQQW
EMKSEEAELL QTKLQQSSYH KQQEELDSLK QTIEESEETL KNTKEVQKKA EEKFKVLEHK
MKNAEAERER ELKEAQQKLD TAKKKADASN KKMKEKQQEV DALVLELEEL KREQTTYKQQ
IETVDEAMKA YQEQADSMAS EVSKNKEAVK KAQDELAKQK EIIMGHDKEI KTKSSEAGKL
RENNNDLQLK IKELEHNISK HKKDSADAAA KVAKMLNDYE WIASEKHLFG QANTAYDFKT
NNPKEAGQRL HKLQEKKEKL GRNVNMRAMN MLTQAEERYN DLMKRKRIVE NDKSKILTTI
EELDQKKNEA LNIAWQKVNK DFGSIFSTLL PGANAMLAPP EGQSVLDGLE FKVALGNTWK
ENLTELSGGQ RSLVALSLIL AMLLFKPAPI YILDEVDAAL DLSHTQNIGQ MLRTHFRHSQ
FIVVSLKDGM FNNANVLFKT KFVDGVSTVA RFAQNQNGGS SAGQQRSDKS KTKERRNRME
VDK
