SMC2_SCHPO
ID SMC2_SCHPO Reviewed; 1172 AA.
AC P41003; Q9P7E2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Structural maintenance of chromosomes protein 2;
DE AltName: Full=Cell untimely torn protein 14;
DE AltName: Full=Chromosome segregation protein cut14;
GN Name=cut14; Synonyms=smc2; ORFNames=SPBP4H10.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7957061; DOI=10.1002/j.1460-2075.1994.tb06821.x;
RA Saka Y., Sutani T., Yamashita Y., Saitoh S., Takeuchi M., Nakaseko Y.,
RA Yanagida M.;
RT "Fission yeast cut3 and cut14, members of a ubiquitous protein family, are
RT required for chromosome condensation and segregation in mitosis.";
RL EMBO J. 13:4938-4952(1994).
RN [2]
RP SEQUENCE REVISION.
RA Saka Y., Sutani T., Yamashita Y., Saitoh S., Takeuchi M., Nakaseko Y.,
RA Yanagida M.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH CUT3; CND1; CND2 AND CND3.
RX PubMed=10485849; DOI=10.1101/gad.13.17.2271;
RA Sutani T., Yuasa T., Tomonaga T., Dohmae N., Takio K., Yanagida M.;
RT "Fission yeast condensin complex: essential roles of non-SMC subunits for
RT condensation and Cdc2 phosphorylation of Cut3/SMC4.";
RL Genes Dev. 13:2271-2283(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.
CC -!- SUBUNIT: Forms a heterodimer with cut3/smc4. Component of the condensin
CC complex, which contains the cut3 and cut14 heterodimer, and three non
CC smc subunits that probably regulate the complex: cnd1, cnd2 and cnd3.
CC {ECO:0000269|PubMed:10485849}.
CC -!- INTERACTION:
CC P41003; P41004: cut3; NbExp=5; IntAct=EBI-1149523, EBI-1149474;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In
CC interphase cells, the majority of the condensin complex is found in the
CC cytoplasm, while a minority of the complex is associated with
CC chromatin. A subpopulation of the complex however remains associated
CC with chromosome foci in interphase cells. During mitosis, most of the
CC condensin complex is associated with the chromatin. At the onset of
CC prophase, condensin associates with chromosome arms and to chromosome
CC condensation. Dissociation from chromosomes is observed in late
CC telophase.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterodimerization with
CC cut3, forming a V-shaped heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily. {ECO:0000305}.
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DR EMBL; D30787; BAA06453.2; -; Genomic_DNA.
DR EMBL; CU329671; CAB83164.1; -; Genomic_DNA.
DR PIR; S51623; S51623.
DR RefSeq; NP_596180.1; NM_001022099.2.
DR AlphaFoldDB; P41003; -.
DR SMR; P41003; -.
DR BioGRID; 277831; 63.
DR IntAct; P41003; 2.
DR STRING; 4896.SPBP4H10.06c.1; -.
DR iPTMnet; P41003; -.
DR MaxQB; P41003; -.
DR PaxDb; P41003; -.
DR PRIDE; P41003; -.
DR EnsemblFungi; SPBP4H10.06c.1; SPBP4H10.06c.1:pep; SPBP4H10.06c.
DR GeneID; 2541319; -.
DR KEGG; spo:SPBP4H10.06c; -.
DR PomBase; SPBP4H10.06c; cut14.
DR VEuPathDB; FungiDB:SPBP4H10.06c; -.
DR eggNOG; KOG0933; Eukaryota.
DR HOGENOM; CLU_001042_9_0_1; -.
DR InParanoid; P41003; -.
DR OMA; HNKIAME; -.
DR PhylomeDB; P41003; -.
DR Reactome; R-SPO-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:P41003; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0034506; C:chromosome, centromeric core domain; IDA:PomBase.
DR GO; GO:0000793; C:condensed chromosome; IBA:GO_Central.
DR GO; GO:0000796; C:condensin complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0000791; C:euchromatin; IDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0015616; F:DNA translocase activity; TAS:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0036292; P:DNA rewinding; IDA:PomBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:PomBase.
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..1172
FT /note="Structural maintenance of chromosomes protein 2"
FT /id="PRO_0000119012"
FT DOMAIN 520..640
FT /note="SMC hinge"
FT COILED 172..204
FT /evidence="ECO:0000255"
FT COILED 258..507
FT /evidence="ECO:0000255"
FT COILED 676..941
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 455
FT /note="Q -> P (in Ref. 1; BAA06453)"
FT /evidence="ECO:0000305"
FT CONFLICT 468..469
FT /note="TN -> PY (in Ref. 1; BAA06453)"
FT /evidence="ECO:0000305"
FT CONFLICT 475..477
FT /note="EDV -> GDA (in Ref. 1; BAA06453)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="L -> M (in Ref. 1; BAA06453)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="L -> A (in Ref. 1; BAA06453)"
FT /evidence="ECO:0000305"
FT CONFLICT 522..523
FT /note="VK -> GE (in Ref. 1; BAA06453)"
FT /evidence="ECO:0000305"
FT CONFLICT 673
FT /note="A -> T (in Ref. 1; BAA06453)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="Q -> R (in Ref. 1; BAA06453)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="Q -> R (in Ref. 1; BAA06453)"
FT /evidence="ECO:0000305"
FT CONFLICT 1046
FT /note="F -> C (in Ref. 1; BAA06453)"
FT /evidence="ECO:0000305"
FT CONFLICT 1146
FT /note="L -> H (in Ref. 1; BAA06453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1172 AA; 134137 MW; 0B785C0F2CA3025C CRC64;
MKIEELIIDG FKSYAVRTVI SNWDDQFNAI TGLNGSGKSN ILDAICFVLG ITNMSTVRAQ
NLQDLIYKRG QAGITRASVT IVFNNRDPAS SPIGFENHPQ VSVTRQIIMG GTSKYLINGH
RALQQNVQNL FQSVQLNINN PNFLIMQGRI TKVLNMKATE ILSMIEEASG TRMFEERKEK
AFRTMQRKEA KVEEINTLLR EEIEPRLTKL RTEKKTFLEY QHIYNDLERL SHLCTAYDYY
KLSLKVEELT VQASQKHSHI AEMESSLQTS KQEVLILKEK IKKIEDERMR QMSVSSDRTL
DSQLQTVNEN ITRISTSIEL KNTALEEEHG DLQQIRGKAK ELETLLRGKR KRLDEVLSVY
EKRKDEHQSI SKDFKSQEEL ISSLTTGLST TEGHETGYSR KLHEARDTLN DFKAEKETNR
LKLEGLNKQI SLTKPKKAEA TKRCDQLNRE IDILQNHVEK LKMSLKNTNS DITGEDVLQQ
KLKQLAKDRG NLLNELDALK SKLAYMEFTY TDPTPNFDRS KVKGLVAQLL TLNEENYDKQ
TALEITAGGR LYNLIVETEK IGAQLLQKGN LKRRVTIIPL NKITSFVASA ERVGAAKKIS
NNKAQLALEL IGYDDELLPA MQYVFGSTLV CDTPESAKKV TFHPSVKLKS VTLDGDVYDP
SGTLTGGSVN KSAGPLLQIQ KLNSLQLKLQ VVTSEYEKLE TQLKDLKTQN ANFHRLEQEI
QLKQHELTLL IEQRETDSSF RLLSDYQQYK DDVKDLKQRL PELDRLILQS DQAIKKIERD
MQEWKHNKGS KMAELEKEFN QYKHKLDEFT PILEKSENDY NGVKLECEQL EGELQNHQQS
LVQGESTTSL IKTEIAELEL SLVNEEHNRK KLTELIEIES AKFSGLNKEI DSLSTSMKTF
ESEINNGELT IQKLNHEFDR LEREKSVAIT AINHLEKEND WIDGQKQHFG KQGTIFDFHS
QNMRQCREQL HNLKPRFASM RKAINPKVMD MIDGVEKKEA KLRSMIKTIH RDKKKIQDTV
KSIDRFKRSA LEKTWREVNS SFGEIFDELL PGNSAELQPP ENKEFTDGLE IHVKIGSIWK
DSLAELSGGQ RSLVALALIM SLLKYKPAPM YILDEIDAAL DLSHTQNIGR LIKTKFKGSQ
FIIVSLKEGM FTNANRLFHV RFMDGSSVVQ AR
