SMC4_XENLA
ID SMC4_XENLA Reviewed; 1290 AA.
AC P50532;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Structural maintenance of chromosomes protein 4;
DE Short=SMC protein 4;
DE Short=SMC-4;
DE AltName: Full=Chromosome assembly protein XCAP-C;
DE AltName: Full=Chromosome-associated protein C;
GN Name=smc4; Synonyms=capc, smc4l1;
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-E.
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-E; 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 topoisomerase. {ECO:0000269|PubMed:10428035,
CC ECO:0000269|PubMed:9774278}.
CC -!- SUBUNIT: Forms a heterodimer with XCAP-E/SMC2. 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 -!- 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-E, forming
CC a V-shaped heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily. {ECO:0000305}.
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DR EMBL; U13673; AAA64679.1; -; mRNA.
DR PIR; A55094; A55094.
DR RefSeq; NP_001081371.1; NM_001087902.1.
DR AlphaFoldDB; P50532; -.
DR SMR; P50532; -.
DR BioGRID; 99138; 7.
DR IntAct; P50532; 3.
DR PRIDE; P50532; -.
DR GeneID; 397799; -.
DR KEGG; xla:397799; -.
DR CTD; 397799; -.
DR Xenbase; XB-GENE-5865892; smc4.L.
DR OrthoDB; 326079at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 397799; Expressed in egg cell and 19 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:UniProtKB.
DR CDD; cd03274; ABC_SMC4_euk; 2.
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; IPR041738; SMC4_ABC_euk.
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..1290
FT /note="Structural maintenance of chromosomes protein 4"
FT /id="PRO_0000119009"
FT DOMAIN 607..721
FT /note="SMC hinge"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 264..594
FT /evidence="ECO:0000255"
FT COILED 764..1027
FT /evidence="ECO:0000255"
FT COILED 1094..1129
FT /evidence="ECO:0000255"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1290 AA; 146989 MW; 2931249924FE90F6 CRC64;
MPPKKTKTST AVAREATESP MAERSRAPDA LQADPPAPTQ ESNNELVDSR SLEEILSGIP
PPPPPAMTNE AGAPRLMITH IVNQNFKSYA GERILGPFHK RFSCIIGPNG SGKSNVIDSM
LFVFGYRAQK IRSKKLSVLI HNSDEHKDVQ SCTVEVHFQK IIDKEGDDFE VIPNSNFYVS
RTAYKDNSSV YHISGKKATF KDVGLLLRSH GIDLDHNRFL ILQGEVEQIA MMKPKGQTEH
DEGMLEYLED IIGSERLKEP IQILCRRVEL LNEQRGEKLN RVKMVEKEKD ALEGEKNKAI
EFLTVENETF KKKNQLCQYY IHDLQKRSRD KEAQKEKIQE DTKDISEKSN TLLETMKEKN
KALKDVEKQL NKITKFIEEN REKFTQLDLQ DVDTREKLKH SKSKVKKLQK QLQKDKEKVD
ELKNVPANSQ KIIAEETNKK DLLEKQKEKE EEKLKNVMDS LKKETQGLQE EKEVKEKELM
EISKTVNEAR SKMDVAQSEL DIYLSRHNSA LSQLNKAKEA LNTASATLKE RRAAIKELET
KLPKDEGDLK KREKELESLV SEEGNIKNQV RELRQKVEEA RSSLSANRSR GKVLDALIQQ
KKSGKIPGIF GRLGDLGAID EKYDVAISSS CGALDHIVVD TIDTAQECVN FLKKQNVGVA
TFIGLDKMKV WEKGLNKIQT PENIPRLFDM VKVKDEQIKP AFYFALRDTI VANNLDQATR
VAFQKDKRWR VVTLQGQIIE QSGTMTGGGG KVMKGRMGSS VMVEISDDQL QKMENKLKTD
TTRATEIQDR KAHLEEEVAK LRQATREMKN TFEKYTASLQ SLSEQEVHLK AQVKELEVNV
AAAAPDKNQQ KQMEKNLETL KKEYEKVAEK AGKVEAEVKR LHKLIVDINN HKLKAQQDKL
DKVTKEIDEC ASAITKAQVS IKTADRNLKK SEEAVARTEK EIVANDKSIE ELTEDLKKLE
EKATTVMNEC KEAECSLPEV QEQHRSLLQE IKAIQEKEHA LQKEALNIRL NIEQIDSHIA
EHQSKIKYWQ KEITKISLHK IEDIPEEVLP GLAQEELEAI KDPDQIINQI ALLEAKSHEM
KPNLGAIAEY KKKEELYLQR VAELDEITNE RDSFRRAYED LRKQRLNEFM AGFNIITNKL
KENYQMLTLG GDAELELVDS LDPFSEGIMF SVRPPKKSWK KIFNLSGGEK TLSSLALVFA
LHHYKPTPLY FMDEIDAALD FKNVSIVAFY IYEQTKNAQF IIISLRNNMF EIADRLIGIY
KTHNTTKSVA TNPKIIAAKG LAEMQSVGCA
