SMC4_SCHPO
ID SMC4_SCHPO Reviewed; 1324 AA.
AC P41004; Q9UTW4; Q9UUF8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Structural maintenance of chromosomes protein 4;
DE AltName: Full=Cell untimely torn protein 3;
DE AltName: Full=Chromosome segregation protein cut3;
GN Name=cut3; Synonyms=smc4; ORFNames=SPBC146.03c;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 273-486, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH CUT14; CND1; CND2 AND CND3,
RP PHOSPHORYLATION AT THR-19, AND MUTAGENESIS OF THR-19.
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).
RN [5]
RP INTERACTION WITH C1739.07.
RX PubMed=15148393; DOI=10.1073/pnas.0307976101;
RA Chen E.S., Sutani T., Yanagida M.;
RT "Cti1/C1D interacts with condensin SMC hinge and supports the DNA repair
RT function of condensin.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8078-8083(2004).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 cut14/smc2. Component of the
CC condensin complex, which contains the smc2 and smc4 heterodimer, and
CC three non smc subunits that probably regulate the complex: cnd1, cnd2
CC and cnd3. Interacts with C1739.07. {ECO:0000269|PubMed:10485849,
CC ECO:0000269|PubMed:15148393}.
CC -!- INTERACTION:
CC P41004; Q9Y7R3: cnd2; NbExp=3; IntAct=EBI-1149474, EBI-1149594;
CC P41004; P41003: cut14; NbExp=5; IntAct=EBI-1149474, EBI-1149523;
CC P41004; O74469: SPCC1739.07; NbExp=3; IntAct=EBI-1149474, EBI-1149494;
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 cut14, forming a V-shaped heterodimer. {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDC2 on Thr-19 at metaphase.
CC {ECO:0000269|PubMed:10485849}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily. {ECO:0000305}.
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DR EMBL; D30788; BAA06454.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB46756.1; -; Genomic_DNA.
DR EMBL; AB027959; BAA87263.1; -; Genomic_DNA.
DR PIR; S51622; S51622.
DR RefSeq; NP_595392.1; NM_001021299.2.
DR AlphaFoldDB; P41004; -.
DR SMR; P41004; -.
DR BioGRID; 276367; 68.
DR DIP; DIP-35048N; -.
DR IntAct; P41004; 6.
DR STRING; 4896.SPBC146.03c.1; -.
DR iPTMnet; P41004; -.
DR MaxQB; P41004; -.
DR PaxDb; P41004; -.
DR PRIDE; P41004; -.
DR EnsemblFungi; SPBC146.03c.1; SPBC146.03c.1:pep; SPBC146.03c.
DR GeneID; 2539817; -.
DR KEGG; spo:SPBC146.03c; -.
DR PomBase; SPBC146.03c; cut3.
DR VEuPathDB; FungiDB:SPBC146.03c; -.
DR eggNOG; KOG0996; Eukaryota.
DR HOGENOM; CLU_001042_4_1_1; -.
DR InParanoid; P41004; -.
DR OMA; QIYIDEC; -.
DR PhylomeDB; P41004; -.
DR Reactome; R-SPO-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:P41004; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000796; C:condensin complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA: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:0015616; F:DNA translocase activity; TAS:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:PomBase.
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; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1324
FT /note="Structural maintenance of chromosomes protein 4"
FT /id="PRO_0000119017"
FT DOMAIN 651..764
FT /note="SMC hinge"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 310..337
FT /evidence="ECO:0000255"
FT COILED 370..628
FT /evidence="ECO:0000255"
FT COILED 825..1077
FT /evidence="ECO:0000255"
FT COILED 1297..1324
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 19
FT /note="Phosphothreonine; by CDC2"
FT /evidence="ECO:0000269|PubMed:10485849"
FT MUTAGEN 19
FT /note="T->A: Defects in chromosome condensation."
FT /evidence="ECO:0000269|PubMed:10485849"
FT CONFLICT 382
FT /note="L -> V (in Ref. 1; BAA06454)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="F -> C (in Ref. 1; BAA06454)"
FT /evidence="ECO:0000305"
FT CONFLICT 1316
FT /note="I -> L (in Ref. 1; BAA06454)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1324 AA; 150653 MW; F28CEDC322E5C622 CRC64;
MSDKGIFRTS STPSIVDVTP DRGERPRKLV RSVLESPSQK DVASIVKIEQ TPSRPFFNDF
LKKRITDSLN ERPNLLNKFM SAQDGTPSKS TGFNERSSQL VSEFTTTEDI ENCEETTQVL
PPRLVVYELR LTNFKSYAGT QIVGPFHPSF SSIVGPNGSG KSNVIDALLF VFGFRASKLR
QSKASALIHK SATHPSLDSC DVEITFKEVN SDFTYVDGSE LTVRRTAYKN NTSKYFVNGV
ESSFSAVSNL LKEKGIDLNH KRFLILQGEV ESIAQMKPRA ISEGDDGLLE YLEDIIGTSK
YKPIIEENMQ ELSNSDDICA EKESRLKLVL SEKAKLEDSK NSVLSFLKDE NELFMKQNQL
YRTILYETRN KKTLVQNLLN SLEGKLQAHL EKFEQTERDI SEKNEEVKSL REKAAKVKND
CTSEKKTRQS YEQQTVKIEE QLKFLLNKEK KLKKSIEALS FEKSEAENSL SSHDIDSQKL
NSEIADLSLR LQQEELSLDD IRKSLQGKTE GISNAIEEKQ KAMAPALEKI NQLTSEKQIL
QVELDMLLNK ENDLINDVES SQSSLDKLRN DAEENRNILS SKLKVLSDLK GEKKDVSKNI
ERKKETVHNT YRNLMSNRTK LEEMKASLSS SRSRGNVLES LQRLHESDNL NGFFGRLGDL
ATIDEAYDVA ISTACPALNH IVVDNIETGQ KCVAFLRSNN LGRASFIILK ELAQKNLARI
QTPENVPRLF DLLRFNDQKF APAFYNVLQN TLVAKNLEQA NRIAYGKTRW RVVTLSGQLI
DKSGTMTGGG TRVKKGGMSS AITSDVSPAS VETCDKQVQL EDTRYRQHLS ELESLNQRFT
EISERIPSAE LEISKLQLDV SACDRLVAGE ERRILQLKSD LKSIRNNNER KRNLQNKISN
MDKEVEAINI NNEGLVTEIK TLQDKIMEIG GIRYRIQKSK VDDLHEQLKF VKDKLNKMSF
KKKKNEQRSQ SFQVELSNLT SEYDTTTESI ATLKTELQSL NKYVDEHKSR LREFENALWD
INSSIDELVK FIEFESKQMN SVKAERIELE NQIQEQRTAL SEVGNNENKY LKLMSNLKLH
NLTEFCDQTT MDSTFPEYSE DELSSVDKSE LVSNISVLKK KTEDREVDIN VLSEYRRCNK
EAEKRDSDYQ SELQKRTDLK KVVTDLQSQR LDEFMYGFGI ISMKLKEMYQ IITMGGNAEL
ELVDSLDPFS EGVLFSVMPP KKSWKNISNL SGGEKTLSSL ALVFALHNYK PTPLYVMDEI
DAALDFKNVS IVANYIKERT KNAQFIVISL RSNMFELSSR LVGIYKTANM TKSVTINNKE
ILTD
